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1
Johnson, Eachan, and Luet-Lok Wong. "Partial fusion of a cytochrome P450 system by carboxy-terminal attachment of putidaredoxin reductase to P450cam (CYP101A1)." Catalysis Science & Technology 2016, no. 6 (September 1, 2016): 7549–60. https://doi.org/10.1039/C6CY01042C.
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Cytochrome P450 (CYP) enzymes catalyze the insertion of oxygen into carbon–hydrogen bonds and have great potential for enzymatic synthesis. Application development of class I CYPs is hampered by their dependence on two redox partners (a ferredoxin and ferredoxin reductase), slowing catalysis compared to self-sufficient CYPs such as CYP102A1 (P450BM3). Previous attempts to address this have fused all three components in several permutations and geometries, with much reduced activity compared to the native system. We report here the new approach of fusing putidaredoxin reductase (PdR) to the carboxy-terminus of CYP101A1 (P450cam) <em>via</em> a linker peptide and reconstituting camphor hydroxylase activity with free putidaredoxin (Pdx). Initial purification of a P450cam–PdR fusion yielded 2.0% heme incorporation. Co-expression of <em>E. coli</em> ferrochelatase, lengthening the linker from 5 to 20 residues, and altering culture conditions for enzyme production furnished 85% heme content. Fusion co-expression with Pdx gave a functional system with comparable <em>in vivo</em> camphor oxidation activity as the native system. <em>In vitro</em>, the fused system's steady state NADH oxidation rate was two-fold faster than that of the native system. In contrast to the native system, NADH oxidation rates for the fusion enzyme showed non-hyperbolic dependence on Pdx concentration, suggesting a role for the PdR domain; these data were consistent with a kinetic model based on two-site binding of Pdx by P450cam–PdR and inactive dimer formation of the fusion. P450cam–PdR is the first example of a class I P450 fusion that exhibits significantly more favorable behavior than that of the native system.
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Nixon, Andrew E., Marc Ostermeier, and Stephen J. Benkovic. "Hybrid enzymes: manipulating enzyme design." Trends in Biotechnology 16, no. 6 (June 1998): 258–64. http://dx.doi.org/10.1016/s0167-7799(98)01204-9.
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Gaziola, S. A., C. M. Teixeira, A. Ando, L. Sodek, and R. A. Azevedo. "Enzyme isolation and regulation with lysine biosynthesis and degradation in developing seeds of rice." International Rice Research Notes 21, no. 1 (April 1, 1996): 27–28. https://doi.org/10.5281/zenodo.6999483.
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This article 'Enzyme isolation and regulation with lysine biosynthesis and degradation in developing seeds of rice' appeared in the International Rice Research Notes series, created by the International Rice Research Institute (IRRI) to expedite communication among scientists concerned with the development of improved technology for rice and rice-based systems. The series is a mechanism to help scientists keep each other informed of current rice research findings. The concise scientific notes are meant to encourage rice scientists to communicate with one another to obtain details on the research reported.
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Pasaribu, Tiurma, A. P. Sinurat, T. Purwadaria, and P. P. Ketaren. "Improving the nutritive values of solid heavy phase to substitute corn in laying hens diet." Jurnal Ilmu Ternak dan Veteriner 14, no. 3 (May 8, 2013): 167–76. https://doi.org/10.14334/jitv.v14i3.338.
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Solid heavy phase (SHP), a by product material of palm oil factory obtained by ceramic filtration from liquid waste could be used as a feedstuff to replace corn in poultry diet. A series of experiment was carried out to improve nutrient value of the SHP by supplementation of enzymes and amino acids in order to increase the proportion of SHP to substitute corn in layer diet. There are three enzymes i.e.: Balitnak production (BS4), a commercial single enzyme (consist of mannanase) and comercial multienzymes were tested. All the enzymes were mixed with fresh SHP in different dose, dried and ground. The nutrient digestibility of these materials was measured in order to decide the optimum level of each enzyme. Based on this result, a feeding trial was carried out. Experimental diets were formulated to study the effect of substitusion of 25% or 50% corn with dried SHP or enzymes-treated SHP on the performances of the layers. The effect of methionine and lysine supplementation into diets contained high levels of SHP was also studied. Results showed that all enzymes studied could increase the energy (TME) of the SHP. BS4 enzyme and the commercial multienzimes, except single enzyme, also increase the true protein digestibility of the SHP. The optimum dose of each enzyme for each kg dry mater of SHP was 13.3 ml BS4, 2 g single enzyme and 3 g multienzymes. Substitution of 25% corn in layer diet with dried SHP or enzymes-treated SHP did not significantly impair the performances (hen-day egg production and FCR) of layers. However, substitution of 50% corn with SHP + multienzymes or SHP + single enzyme significantly impaired the performances of the layers. Addition of methionine and lysine amino acids restored the performance of the hens fed with SHP + commercial multienzyimes, but not those fed with high levels of SHP + commercial single enzyme. Substitution of 50% corn with SHP + BS4 enzime did not significantly impaire the performance of layers and therefore, addition of amino acids into the diet was not required. Substitution of 25% or 50% corn with dried SHP or enzymes-treated SHP did not affect the egg quality (HU, yolk color index and shell thickness). It is concluded that solid heavy phase (SHP) could be used to substitute 25 to 50% corn in layer diet, especially when the SHP was treated with BS4 enzyme. Key Words: Solid Heavy Phase, Enzymes, Amino Acids, Layer
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Achmadi, Evita Riviani. "Enzymes as Potencial Source for Clean Label Bakery Product: Part 1, Mechanism and Application Single Enzym." Journal of Food and Agricultural Product 2, no. 2 (September 14, 2022): 57. http://dx.doi.org/10.32585/jfap.v2i2.2708.
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Background: Increased public awareness of consuming healthy food has driven bakery industry to applied production methods and components of food products that are tailored to the market needs. Food product can be positioned as natural, organic, or free from additives/ preservatives which often referred to clean label trend. Bakery industry commonly using chemical emulsifier as component which improve characteristic and quality baked goods. Usage of chemical component is not appropriate with perception of clean label, although it is not yet clear what a clean label exactly means. Chemical emulsifier has potentially negative effect to health such as intestinal inflammation, obesity, metabolic syndrome and glucose resistance based on several research. Food enzyme can be alternative to replace chemical emulsifier and potentially source of clean label bakery product. Therefore, sustainable study was needed to find role single enzym as food additive and processing aid in bakery product application.Scope and approach: This review explain about the role single enzyme application in bakery product which discuss under three main headings include (i) enzyme as food additive and processing aid, ii) Characteristic enzyme to improve bakery product processing (dough mixing, fermentation, baking), sensories properties and appearance iii) Enzyme mechanism and application to enhance bakery product quality. Optimization of the role and function of enzymes can be conduct by enzyme quality validation through baking tests including formulation development, process parameters (dough rheology, handling machine and baking parameter), product appearance and sensory characteristics.Key findings and conclusion: Food enzymes play a role in enzymatic modifications as biodegradable proteins which not affected to nutritional value baked goods. Enzyme technology is a clean process with low energy consumption, low waste production, safe and less toxic working environment. Therefore, enzyme has potential to fulfill clean label trends and encourage researchers and developers in food industry to explore potential use of food enzymes in bakery products. Enzymes which usually used in bakery come from hydrolase class (amylase, protease, hemicellulase, lipase, xylanase and asparaginase), oxidoreductase class (lipoxygenase and glucose oxidase) and transferase class (transglutaminase). Application enzymes in bakery processs have their respective roles according to enzymes specific characteristics. Enzymes has the main role such as improve rheological and functional properties of dough according to baked goods type, enhance quality and characteristics baked goods including volume, crumb texture, color, taste and extend shelf life (antistaling). Sustainable research and development was needed to optimize the role of enzyme in baked goods by several approach such as (i) incorporation enzymes with other ingredients in the food matrix, (ii) parameters which affect to the work of enzymes in food systems (iii) potential of enzyme combinations to improve baked goods quality and (iv) understanding of usage regulation enzymes as food additives and food processing. Keyword: enzyme, clean label, food additive, processing aid, bakery product
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Jovov, B., N. K. Wills, P. J. Donaldson, and S. A. Lewis. "Vectorial secretion of a kallikrein-like enzyme by cultured renal cells. I. General properties." American Journal of Physiology-Cell Physiology 259, no. 6 (December 1, 1990): C869—C882. http://dx.doi.org/10.1152/ajpcell.1990.259.6.c869.
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Urinary kallikreins are proteolytic enzymes known to be secreted by distal nephron tubules. In this study, we demonstrate (using the chromogenic tripeptide substrate S 2266) that the renal cell line A6 from Xenopus laevis secretes a kallikrein-like enzyme. Secretion is present only when the cells are grown on filters, and enzyme is secreted only into the apical membrane bathing solution. Enzyme secretion consists of two components, one soybean trypsin inhibitor (SBTI) sensitive (SSBTI) and the other insensitive to SBTI (ISBTI). Both enzymes were inhibited by aprotinin, a kallikrein-like enzyme inhibitor. Using a bioassay, only the ISBTI enzyme produced a hypotensive effect on blood pressure and is thus a kallikrein-like enzyme. The apical membrane of cells grown on filters contains both enzyme species, whereas the basolateral membrane contains only the ISBTI (kallikrein-like) enzyme. Both enzymes were present in the apical membrane of cells grown on plastic. Initiation of enzyme secretion occurred after the cells formed electrically tight monolayers and the increase in membrane activity always preceded enzyme secretion. Using an irreversible inhibitor of the apical membrane-bound enzymes, the turnover rate for the SSBTI and ISBTI enzymes (cells on filters) was 3 and 7 h, respectively. Because the recovery of enzyme secretion was proportional to the recovery of membrane-bound enzyme activities, this suggests that enzyme secretion is due to the release of membrane-bound enzyme.
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Mao, Shucan, Jiawen Jiang, Ke Xiong, Yiqiang Chen, Yuyang Yao, Linchang Liu, Hanbing Liu, and Xiang Li. "Enzyme Engineering: Performance Optimization, Novel Sources, and Applications in the Food Industry." Foods 13, no. 23 (November 28, 2024): 3846. http://dx.doi.org/10.3390/foods13233846.
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This review summarizes the latest progress in enzyme preparation, including enzyme design and modification technology, exploration of new enzyme sources, and application of enzyme preparation in food processing, detection, and preservation. The directed evolution technology improved the stability and catalytic efficiency of enzymes, while enzyme immobilization technology enhanced reusability and industrial applicability. Extremozymes and biomimetic enzymes exhibit excellent performance under harsh conditions. In food processing, enzyme preparation can improve food quality and flavor. In food detection, enzymes combined with immune detection and biosensors realize rapid detection of allergens, pollutants, and pesticide residues. In food preservation, enzymes enhance food quality by extending shelf life and inhibiting microbial growth. In the future, enzyme engineering will be combined with computer-aided design, artificial intelligence, and new material technology to promote intelligent enzyme design and multifunctional enzyme preparation development and help the technological upgrading and sustainable development of the food industry and green chemistry.
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Achmadi, Evita Riviani. "Enzymes as Potencial Source for Clean Label Bakery Product: Part 2, Mechanism, Application and Optimization Combination Enzymes." Journal of Food and Agricultural Product 2, no. 2 (December 16, 2022): 82. http://dx.doi.org/10.32585/jfap.v2i2.2709.
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Background: Food enzyme is important ingredient for bakery industry to improve production process, functional properties and characteristic bakery product. Food enzym can be applied as single or combination enzym based on purpose which is need on processing. Based on several literatures, application combination enzymes more effective than single enzym, due to synergism effect between enzym which combine. Combination enzymes can be mixed from same or different class of enzym, it is depended on selected specification and characteristic enzym. Application of combination enzymes commonly act as processing aid which added in flour while mixing process. Therefore, it is important to understand work mechanism of combination enzym in processing stage especially mixing, fermentation and baking. Sinergysm in combination enzym can be enhance using optimization method to improve quality of processing and bakery product. Response Surface Methode (RSM) with Central Composite Design (CCD) as a design experiment is the most effective and efficient method which commonly applied for modelling and optimization in food processing. This method helps to make informed decision on a process with the objective of improving efficiency and minimizing cost while maintaining quality.Scope and approach: This review explain about the role combination enzyme application in bakery product which discuss under four main headings include (i) Application of combination enzymes in bakery product ii) Mechanism combination enzymes to enhance bakery product quality include processing (mixing, fermentation and baking) and sensory properties (texture, taste, colour and appearance) iii) Optimization of combination enzym in bakery product using Respond Surface Method (RSM) iv) Regulation food enzym usage in United State, Europian Union and Indonesia. Evaluation mechanism, application and optimization of combination enzymes can be used as a base for sustainable development bakery product which is safe for consume and accordance to food regulation. The differences regulation between country can be considerate when supply and distribution chain of industrial and retail food companies stretch around the globe.Key findings and conclusion: The combination of enzymes provides a synergistic effect depending on the type and mechanism enzymes which is affected each other. Type and mechanism enzymes can be affected with process parameter and ingredient which is a part of food matrix while processing runs. Therefore, the suitability between process parameters, ingredient, specifications and characteristics enzyme are needed to gives significant results for optimization of enzyme combinations in bakery production. Understanding the role of enzymes as a part of food system is important as a basic knowledge in selection of enzymes to be combined. This helps researchers and developers to optimize the combination of enzymes by taking into account conditions of the process stages in bakery production. RSM with CCD as design experiments is the most efficient method because its only requires a small amount runs. CCD uses the build-up principle to build a quadratic model using the information gathered from the 2n factorial design. If the linear model of the 2n factorial is not significant, it is possible to design another trial based on the CCD principle to improve the model. Model improvement using build-up principle is suitable with the food industry needed, which requires fast, precise and accurate validation and verification in making decisions in terms of product development and production process.Keyword: Combination enzymes, RSM (Response Surface Method), CCD (Central Composite Design), regulation, mechanism, application.
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March, John B., and Jason Clark. "Enzymes by post—restriction enzyme stability." Nature Biotechnology 18, no. 3 (March 2000): 243. http://dx.doi.org/10.1038/73590.
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Städler, Brigitte, and Alexander N. Zelikin. "Enzyme prodrug therapies and therapeutic enzymes." Advanced Drug Delivery Reviews 118 (September 2017): 1. http://dx.doi.org/10.1016/j.addr.2017.10.006.
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Woggon, Wolf-Dietrich. "Lessons from Enzymes and Enzyme Models." CHIMIA 53, no. 5 (May 26, 1999): 234. https://doi.org/10.2533/chimia.1999.234.
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Results from our laboratory are presented demonstrating the significance of synthetic active-site analogs of metalloproteins to accomplish catalytic enzyme-like reactions and to identify key intermediates of the reaction cycles.
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Siregar, Benedicta Lamria, Rexi Sebastian Siallagan, Suwarnita Butar Butar, Bambang Mahmudi, and Elisabeth Sri Pujiastuti. "The Nutrient Content of Eco-enzymes from Mixture of Various Fruit Peels." Agro Bali : Agricultural Journal 7, no. 2 (July 31, 2024): 475–87. http://dx.doi.org/10.37637/ab.v7i2.1646.
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Today, many institutions and individuals are paying attention to the development of technologies used in sustainable agriculture. One of the technologies is eco-enzyme that can be used as organic fertilizer. Several researchers have studied the use of eco-enzymes in agriculture, but studies on the nutrient content of eco-enzymes are still very limited. This research was conducted to investigate the nutrient content of two eco-enzyme preparations. The eco-enzymes were produced through the fermentation process of water, fruit peels, and molasses with a weight ratio of 10 : 3 : 1. Fruit peels used for Eco-enzyme A were banana, melon, watermelon, orange, and pineapple peels, while for Eco-enzyme B were banana, mango, watermelon, orange, and pineapple peels. The fermentation period for Eco-enzyme A was seven months, while for Eco-enzyme B was eight months. The results of the analysis showed that the two eco-enzymes contained various nutrients, both macro (C, N, P, K, Mg, Ca) and micro (Mn, Zn, B, Fe, Cu) ones, that were consistently higher in Eco-enzyme A. Both eco-enzymes were acidic, where the pH of Eco-enzyme A and B were 3.95 and 3.50, respectively. The data obtained were expected to be a basic reference for further research on eco-enzymes.
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R, Kumaravelrajan, Swetha M та Suba V. "Characterization of Immobilized β-Amylase Enzyme Isolated from Sweet Potato and prepared by Entrapment Method". International Journal of Pharmaceutical Sciences and Nanotechnology(IJPSN) 15, № 6 (16 грудня 2022): 6196–203. http://dx.doi.org/10.37285/ijpsn.2022.15.6.2.
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Aim: This study attempted to isolate β-amylase from sweet potato and enzyme immobilized by encapsulation method, and characterized with various parameters. 
 Methods: The enzyme β-amylase was isolated with phosphate-buffered saline and purified by centrifugation with ammonium sulfate. The purified enzyme was immobilized on chitosan (0.25 g) and sodium alginate (0.25 g) polymers by entrapment method in the presence of calcium chloride (0.5 M). The immobilized enzyme was characterized by a starch hydrolysis test, the optimal pH and temperature were studied and the stability of the immobilized enzyme was also determined. SEM analysis was performed and Vm and Km were also found. 
 Results: The starch hydrolysis test showed positive results on the starch agar plates for immobilized enzymes. The thermal inactivation showed a severe loss in the activity of the free enzymes (49.3 %) while the temperature profile of the immobilized enzymes was much broader (84.55 %) at higher temperatures (80° C). The optimal pH and stability indicated that the immobilized enzyme has higher stability in the pH range of 5-8. The Km and Vmax value of free and immobilized enzyme was 7.67 mmol, 21.15 µmol (R2 0.8880), and 4.72 mmol,16.79 µmol (R2 0.8446) respectively. The storage of free and immobilized enzymes for one month showed that 83.5 % and 40 % of free enzymes and 11.6 % and 8.6 % of immobilized enzymes lost activity at 25° C and 4° C, respectively. SEM analysis shows the smooth, porous surface. 
 Conclusion: Immobilized enzymes (natural polymers) exhibit higher thermal stability the optimal pH and stability indicate immobilized enzyme has higher stability in the pH range of 5-8, and achieves a relative activity of 69.7 %. After 6 uses, the reuse efficiency of the immobilized enzyme decreased from 99.8 % to 52.3 %. The storage of the immobilized enzyme showed much higher stability than the found-free enzyme.
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Aliyev, Tofiq, and Səbrin Abdullayeva. "The Role of Enzymes in Modern Medicine: Advances, Applications, and Future Directions." Luminis Applied Science and Engineering 2, no. 1 (March 13, 2025): 72–76. https://doi.org/10.69760/lumin.20250001012.
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Enzymes play a critical role in modern medicine, serving as essential biological catalysts in therapeutic and diagnostic applications. This article explores the use of enzymes in enzyme replacement therapy (ERT), pharmaceutical drug development, and clinical diagnostics. The advancements in biotechnology have led to the development of engineered enzymes with improved stability and efficiency, addressing challenges such as enzyme degradation, immunogenicity, and production costs. Recent innovations, including enzyme immobilization, nanotechnology-based delivery systems, and CRISPR-engineered enzymes, have significantly enhanced the scope of enzyme-based treatments. Despite existing limitations, ongoing research continues to refine enzyme therapies, making them more accessible and effective. This study highlights the transformative impact of enzymes in medicine and discusses future directions for optimizing their clinical applications.
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Zhang, Song, Changping Wang, Hong Chang, Qiang Zhang, and Yiyun Cheng. "Off-on switching of enzyme activity by near-infrared light-induced photothermal phase transition of nanohybrids." Science Advances 5, no. 8 (August 2019): eaaw4252. http://dx.doi.org/10.1126/sciadv.aaw4252.
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The off-on manipulation of enzyme activity is a challenging task. We report a new strategy for reversible off-on control of enzyme activity by near-infrared light. Enzymes acting on macromolecular substrates are embedded with an ultrasmall platinum nanoparticle and decorated with thermoresponsive copolymers, which exhibit upper critical solution temperature (UCST) behavior. The polymer-enzyme nanohybrids form microscale aggregates in solution below the UCST to prevent macromolecular substrates from approaching the enzymes and thus inhibit the enzyme activity, and they disassemble above the UCST to reactivate the enzyme. Upon near-infrared irradiation, platinum nanoparticles inside the enzymes generate heat through a photothermal effect to cause phase transition of the copolymers. Therefore, we can reversibly switch off and on the activities of three enzymes acting on polysaccharide, protein, and plasmid. The enzyme activities are increased by up to 61-fold after laser irradiation. This study provides a facile and efficient method for off-on control of enzyme activity.
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Vovk, H., and T. Nosenko. "Influence of enzymatic treatment parameters on the press pumkin oil yeild and its properties." Scientific Works of National University of Food Technologies 29, no. 1 (February 2023): 108–18. http://dx.doi.org/10.24263/2225-2924-2023-29-1-10.
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The influence of parameters of pumpkin seeds pretreatment with enzyme preparations of proteolytic and cellulolytic activity on the yield of press oil, its composition and quality parameters were studied in this work. The enzyme preparation PENICILOPEPSIN (Enzym Biotech, Ukraine) with proteolytic activity and CELLULAD (Enzym Biotech, Ukraine) with cellulolytic, hemicellulase and xylanase activity were used for pretreatment. Enzymatic treatment of seeds was carried out with a mixture of these preparations at a ratio of 7:3 for 2 h at a pH 5.2 and 48—54°C. The following parameters of enzymatic pretreatment were studied: the amount of the enzyme mixture, which varied from 0.3% to 2.4% of the weight of the seeds and the amount of moisture added together with the enzymes — from 15% to 50%. It was established that the rational parameters of the enzymatic treatment of pumpkin seeds are the mass of the enzyme mixture of 0.6% and the amount of moisture added with enzymes — 35% of the seed mass. Under such technological parameters, the yield of press pumpkin oil was 65.6%, which is almost 6% higher than in the control sample. The acid and anisidine value of the control oil sample and the oil extracted after the enzymatic treatment of the seeds did not differ significantly. However, the content of peroxide compounds in the oil extracted after enzymatic treatment of seeds was lower. The total antioxidant activity of the oil, determined by the reaction of the 2,2-diphenyl-1- picrylhydrazyl radicals quenching within 30 min, was higher in the oil samples after seed pretreatment at the maximum tested moisture (50%). The obtained results indicate that the enzymatic pretreatment of pumpkin seeds with proteolytic and cellulolytic enzyme preparations is a promising method of oil yield increasing.
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Fadlilla, Thanya, MTh Sri Budiastuti, and MMA Retno Rosariastuti. "Potential of Fruit and Vegetable Waste as Eco-enzyme Fertilizer for Plants." Jurnal Penelitian Pendidikan IPA 9, no. 4 (April 30, 2023): 2191–200. http://dx.doi.org/10.29303/jppipa.v9i4.3010.
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This study aims to determine the source of eco-enzyme raw materials and the most appropriate dilution volume to produce quality eco-enzyme fertilizer for plant growth. 1 (sugar): 3 (fruit and vegetable waste): 10 (water). The resulting eco-enzyme liquid is processed into fertilizer through the dilution process. Eco-enzyme fertilizers from each raw material source contain different organic N, P, K, and C nutrients. Besides that, some enzymes are beneficial to plants. This research is experimental in the laboratory. The experimental design was factorial design using a completely randomized design as the based design with the treatment of various sources of raw material for eco-enzyme E1 (fruit waste), E2 (vegetable waste), and E3 (fruit and vegetable waste). The parameters observed are N, P, K, and C Organic. The results showed that in terms of the quality of eco-enzyme fertilizers, the best order of eco-enzyme fertilizers was eco-enzyme fertilizer from vegetable waste (E2), eco-enzyme fertilizer from fruit and vegetable waste (E3), and eco-enzyme fertilizer from fruit waste (E1). Based on the NPK content in eco-enzyme fertilizer, eco-enzyme fertilizer is still below the quality standard for liquid organic fertilizer but the enzymes contained in eco-enzymes can also spur growth in plants.
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Ginting, N., and R. E. Mirwandhono. "Productivity of Turi (Sesbania grandiflora) as a multi purposes plant by eco enzyme application." IOP Conference Series: Earth and Environmental Science 912, no. 1 (November 1, 2021): 012023. http://dx.doi.org/10.1088/1755-1315/912/1/012023.
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Abstract Turi (Sesbania grandiflora) is a multi-purpose plant, including leaves for animal feed, flowers for human food and wood for wood pellets. Eco enzyme is produced from the fermentation of fruits containing enzymes and organic acids. The application of Eco enzyme, among others as biocatalist to improve plant productivity. This paper aims to study dilution of Eco Enzym which was applied to Turi plants to increase its productivity This study used a completely randomized design, namely: T1: Eco enzyme dilution 1: 100; T2: 1: 200; T3: 1: 300 whereas there were 5 replications. Parameters were plant height, stem diameter, number of branches, leaf width and number of flowers. The results of this research were that the parameters of plant height, leaf of width, number of flowers had significant effect by the 1:100 dilution treatment (p<0,05). However, there was no significant effect on stem diameter and and the number of branches. The best response to eco enzyme was 1: 100.
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Chang, Antje, Lisa Jeske, Sandra Ulbrich, Julia Hofmann, Julia Koblitz, Ida Schomburg, Meina Neumann-Schaal, Dieter Jahn, and Dietmar Schomburg. "BRENDA, the ELIXIR core data resource in 2021: new developments and updates." Nucleic Acids Research 49, no. D1 (November 19, 2020): D498—D508. http://dx.doi.org/10.1093/nar/gkaa1025.
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Abstract The BRENDA enzyme database (https://www.brenda-enzymes.org), established in 1987, has evolved into the main collection of functional enzyme and metabolism data. In 2018, BRENDA was selected as an ELIXIR Core Data Resource. BRENDA provides reliable data, continuous curation and updates of classified enzymes, and the integration of newly discovered enzymes. The main part contains &gt;5 million data for ∼90 000 enzymes from ∼13 000 organisms, manually extracted from ∼157 000 primary literature references, combined with information of text and data mining, data integration, and prediction algorithms. Supplements comprise disease-related data, protein sequences, 3D structures, genome annotations, ligand information, taxonomic, bibliographic, and kinetic data. BRENDA offers an easy access to enzyme information from quick to advanced searches, text- and structured-based queries for enzyme-ligand interactions, word maps, and visualization of enzyme data. The BRENDA Pathway Maps are completely revised and updated for an enhanced interactive and intuitive usability. The new design of the Enzyme Summary Page provides an improved access to each individual enzyme. A new protein structure 3D viewer was integrated. The prediction of the intracellular localization of eukaryotic enzymes has been implemented. The new EnzymeDetector combines BRENDA enzyme annotations with protein and genome databases for the detection of eukaryotic and prokaryotic enzymes.
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Li, Can, Zhishang Shi, Jinxing Cai, Ping Wang, Fang Wang, Meiting Ju, Jinpeng Liu, and Qilin Yu. "Synthesis of Phenylboronic Acid-Functionalized Magnetic Nanoparticles for Sensitive Soil Enzyme Assays." Molecules 27, no. 20 (October 14, 2022): 6883. http://dx.doi.org/10.3390/molecules27206883.
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Soil enzymes, such as invertase, urease, acidic phosphatase and catalase, play critical roles in soil biochemical reactions and are involved in soil fertility. However, it remains a great challenge to efficiently concentrate soil enzymes and sensitively assess enzyme activity. In this study, we synthesized phenylboronic acid-functionalized magnetic nanoparticles to rapidly capture soil enzymes for sensitive soil enzyme assays. The iron oxide magnetic nanoparticles (MNPs) were firstly prepared by the co-precipitation method and then functionalized by (3-aminopropyl)triethoxysilane, polyethyleneimine and phenylboric acid in turn, obtaining the final nanoparticles (MNPPBA). Protein-capturing assays showed that the functionalized MNPs had a much higher protein-capturing capacity than the naked MNPs (56% versus 6%). Moreover, MNPPBA almost thoroughly captured the tested enzymes, i.e., urease, invertase, and alkaline phosphatase, from enzyme solutions. Based on MNPPBA, a soil enzyme assay method was developed by integration of enzyme capture, magnetic separation and trace enzyme analysis. The method was successfully applied in determining trace enzyme activity in rhizosphere soil. This study provides a strategy to sensitively determine soil enzyme activity for mechanistic investigation of soil fertility and plant–microbiome interaction.
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Sunaga, H., H. Sugimoto, Y. Nagamachi, and S. Yamashita. "Purification and properties of lysophospholipase isoenzymes from pig gastric mucosa." Biochemical Journal 308, no. 2 (June 1, 1995): 551–57. http://dx.doi.org/10.1042/bj3080551.
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Two lysophospholipases, named gastric lysophospholipases I and II (enzymes I and II), were purified 3730- and 2680-fold from pig gastric mucosa. The preparations showed 22 and 23 kDa single protein bands on SDS/PAGE respectively. Both enzymes lacked transacylase activity and appeared to exist as monomers. Their activities were not affected by Ca2+, Mg2+ or EDTA. Enzyme I was most active at pH 8.5 and hydrolysed a variety of lysophospholipids including acidic lysophospholipids and the acyl analogue of platelet-activating factor, whereas enzyme II was most active at pH 8 and its activity was confined to lysophosphatidylcholine and lysophosphatidylethanolamine. When 1-palmitoylglycerophosphocholine was used as substrate, enzymes I and II showed half-maximal activities at 11 and 12 microM respectively. The enzymes exhibited no phospholipase B, lipase or general esterase activity. Enzyme II was significantly inhibited by lysophosphatidic acid whereas enzyme I was only moderately inhibited. Peptide mapping with V8 protease and papain revealed structural dissimilarity between the two enzymes. Antiserum raised against enzyme I did not recognize enzyme II, but did recognize the small-sized lysophospholipase purified from rat liver. Anti-(enzyme II) consistently did not cross-react with enzyme I or the liver enzyme. These antisera specifically recognized neither the 60 kDa lysophospholipase transacylase purified from liver nor any peritoneal macrophage protein. Thus gastric mucosa contains two different small-sized lysophospholipases: one is closely related to the small-sized lysophospholipase of liver, but the other appears to be a novel isoform.
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Dzulqaidah, Intan, Regina Brigita Zanuba, Andi Siti Fatimah Alwi, Arista Rizkika Putri Salsabila, Siswandi Mursidi, and Handa Muliasari. "Ekstraksi dan Uji Aktivitas Enzim Bromelin Kasar dari Buah Nanas." Journal of Agritechnology and Food Processing 1, no. 2 (December 31, 2021): 80. http://dx.doi.org/10.31764/jafp.v1i2.6974.
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Pineapple (Ananas comosus) is a source of protease enzymes. The protease enzyme present in pineapple is the bromelain enzyme. Bromelain enzymes are widely used in various industrial fields. The purpose of this experiment was to isolate the bromelain enzyme from pineapple plants, to test the activity of the enzyme, and to determine the optimum temperature of the enzyme. Isolation of the bromelain enzyme from pineapple was carried out by precipitating the pineapple fruit filtrate using table salt (NaCl). Then the crude extract of the enzyme obtained was tested on pieces of meat with variations in the testing temperature (room temperature, hot, and cold). The yield of the crude extract of the enzyme obtained from the experiment was 40%. The results of testing the bromelain enzyme activity of pineapple showed that room temperature was the best temperature for the enzyme to tenderize meat compared to hot and cold temperatures.
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Jun, Jin-Sung, Ye-Lim You, Ha-Jun Byun, Kyung-Hoon Han, Jay Kim, Jea-Bum Jung, Hyeon-Son Choi, and Sung-Hee Han. "Enzyme Activity and Lipogenesis Inhibition by Fermented Grain Using Natural Enzymes." Molecules 28, no. 21 (October 26, 2023): 7285. http://dx.doi.org/10.3390/molecules28217285.
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This study aims to compare the effects of three enzyme-rich foods, including one fermented (grain enzyme) and two non-fermented foods (enzyme foods 1 and 2), by investigating their antioxidant, anti-inflammatory, and anti-adipogenic properties. Grain enzyme exhibited the highest radical scavenging activity and was rich in antioxidant components, including total polyphenol and total flavonoid contents. Grain enzyme and enzyme foods 1 and 2 inhibited nitric oxide production by 27, 34, and 17%, respectively, at a concentration of 200 μg/mL in LPS-stimulated macrophages. Among the tested enzymes, grain enzyme demonstrated the strongest inhibition on the expression of inducible nitric oxide synthase (INOS), cyclooxygenase-2 (COX-2), and interleukin (IL)-1β, while Enzyme Food 2 exhibited the most significant suppression of IL-6 mRNA levels. Furthermore, Grain Enzyme demonstrated a stronger inhibitory effect compared to Enzyme Food 1 and 2. Grain Enzyme decreased the mRNA expression of peroxisome proliferator-activated receptor (PPAR)γ, CCAAT/enhancer-binding protein (C/EBP)α, and fatty acid-binding protein (FABP)4 by 28, 21, and 30%, respectively, at a concentration of 400 μg/mL. In summary, fermented grain enzymes outperformed non-fermented enzymes in suppressing inflammation and adipogenesis. This study highlights the anti-inflammatory and anti-adipogenic effects of grain enzyme, suggesting its potential as a valuable dietary supplement for managing metabolic disorders.
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Høst, Amalie Vang, Roberto Morellon-Sterling, Diego Carballares, John M. Woodley, and Roberto Fernandez-Lafuente. "Co-Enzymes with Dissimilar Stabilities: A Discussion of the Likely Biocatalyst Performance Problems and Some Potential Solutions." Catalysts 12, no. 12 (December 3, 2022): 1570. http://dx.doi.org/10.3390/catal12121570.
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Enzymes have several excellent catalytic features, and the last few years have seen a revolution in biocatalysis, which has grown from using one enzyme to using multiple enzymes in cascade reactions, where the product of one enzyme reaction is the substrate for the subsequent one. However, enzyme stability remains an issue despite the many benefits of using enzymes in a catalytic system. When enzymes are exposed to harsh process conditions, deactivation occurs, which changes the activity of the enzyme, leading to an increase in reaction time to achieve a given conversion. Immobilization is a well-known strategy to improve many enzyme properties, if the immobilization is properly designed and controlled. Enzyme co-immobilization is a further step in the complexity of preparing a biocatalyst, whereby two or more enzymes are immobilized on the same particle or support. One crucial problem when designing and using co-immobilized enzymes is the possibility of using enzymes with very different stabilities. This paper discusses different scenarios using two co-immobilized enzymes of the same or differing stability. The effect on operational performance is shown via simple simulations using Michaelis–Menten equations to describe kinetics integrated with a deactivation term. Finally, some strategies for overcoming some of these problems are discussed.
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Kopetzki, E., K. Lehnert, and P. Buckel. "Enzymes in diagnostics: achievements and possibilities of recombinant DNA technology." Clinical Chemistry 40, no. 5 (May 1, 1994): 688–704. http://dx.doi.org/10.1093/clinchem/40.5.688.
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Abstract We discuss, from an industrial point of view, the scope and possibilities of recombinant DNA technology for "diagnostic enzyme" production and application. We describe the construction of enzyme-overproducing strains and show how to simplify downstream processing, increase product quality and process profitability, improve diagnostic enzyme properties, and adjust enzymes to harsh assay conditions. We also consider some safety and environmental aspects of enzyme production. Other aspects of diagnostic enzymes that we cover are the facilitation of enzyme purification by attachment of short amino acid tails, the introduction of tails or tags for site-specific conjugation or oriented immobilization, the construction of bi- or multifunctional enzymes, and the production of enzyme-based diagnostic tests as demonstrated by the homogeneous immunoassay system of CEDIA tests. We use as examples of diagnostic enzymes glucose-6-phosphate dehydrogenase (EC 1.1.1.49), glucose oxidase (EC 1.1.3.4), alkaline phosphatase (EC 3.1.3.1), alpha-glucosidase (EC 3.2.1.20), pyruvate oxidase (EC 1.2.3.3), creatinase (EC 3.5.3.3), and beta-galactosidase (EC 3.2.1.23).
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Ariga, Kotoko, Seiya Tsujimura, and Tsutomu Mikawa. "Evaluation of Enzyme Cascade Electrode Reactions at Nanoscale Area." ECS Meeting Abstracts MA2024-02, no. 54 (November 22, 2024): 3675. https://doi.org/10.1149/ma2024-02543675mtgabs.
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Introduction Enzymes are promising catalysts with high selectivity and low environmental load. Especially, redox enzymes are attracting attentions because of their applicability to electrodes for biosensors and biofuel cells. For example, wearable lactate biosensors which can detect lactate in sweat and use the reaction to drive itself have been developed recently[1]. Various biosensors are already available today. However, most of them use single-enzyme electrodes. Compared to single-enzyme electrodes, multi-enzyme electrodes are expected to improve the performance of conventional biosensors and biofuel cells by realizing detection of multiple biomarkers and increased energy density. This study uses the multi-enzyme system involving lactate oxidase (LOx), pyruvate decarboxylase (PDC), and aldehyde dehydrogenase (ALDH) as the reaction model. In this system, four electrons are produced during one lactate molecule is converted into acetate via pyruvate, which is double the number of what are produced by an LOx single-enzyme electrode used in conventional lactate biosensors. This study aims to improve the current response of bioelectrodes by causing enzyme cascade reactions within nanoscale pores of MgO-templated carbon (MgOC). MgOC is a porous carbon material, which is believed to enhance the efficiency of cascade reactions by providing high surface area and control the enzyme activity by changing the solution environment within the nanoscale pores[2]. The prepared electrodes were evaluated electrochemically to investigate how enzyme cascade and the use of MgOC affect the electrode performance. Experimental The ink containing MgOC was dropped to glassy carbon (GC) electrodes to make MgOC electrodes. Subsequently, solution of 1,2-naphtoquinone, the mediator, was added to the MgOC surface. Finally, the mixture of certain ratios of enzymes, crosslinker, Mg-salt, and thiamine pyrophosphate (TPP) was dropped. The latter two were added to promote enzyme reactions. Using the MgOC electrode as a working electrode, three-electrode measurement system was constructed. The measurement solution was 0.1 M phosphate buffer solution (pH 7.0) containing about 15 mM of L-lactate as the substrate. Chronoamperometry (CA) was carried out with an MgOC electrode and a flat GC electrode immobilized with the same amount and ratio of enzymes to see how the use of MgOC affect the current response. Then, the enzyme cascade effect was evaluated by measuring CA of single-enzyme (LOx) electrodes and multi-enzyme (LOx+PDC+ALDH) electrodes. Furthermore, solution environment dependence of the cascade effect was measured by changing the concentration of enzymes and ammonium sulfate ((NH4)2SO4), a kosmotropic salt which is known to salt out enzymes. Results and Discussion The current density observed with the MgOC electrode immobilized with LOx, PDC, and ALDH was about 6.8 times higher than that obtained from the GC electrode also dropped with the three kinds of enzymes. This result indicates the use of MgOC as the electrode surface material is beneficial for enzyme cascade systems because of its higher surface area. We also consider that MgOC has the effect to promote product transfer in cascade systems by containing enzymes in nanoscale pores. The relationship between the pore size of MgOC and the performance of enzyme cascade electrodes will be explored in future experiments. Enzyme cascade effect was evaluated by comparing the current density of single-enzyme MgOC electrodes dropped with only LOx and multi-enzyme MgOC electrodes with LOx, PDC, and ALDH. The figure shows the results. The multi-enzyme electrodes exhibited about 1.98 times higher current density than the single-enzyme electrodes. It implies that the enzyme cascade reactions caused by LOx, PDC, and ALDH increased the number of electrons produced in the system. In this experiment, enzyme solution contained 10 mg/mL of each enzyme and 1.5 mol/L of (NH4)2SO4. When the (NH4)2SO4 concentration was raised to 3.0 mol/L, the current density increased by 2.40 times from single-enzyme to multi-enzyme. On the other hand, it rose by 2.51 times with 5 mg/mL of enzymes and 3.0 mol/L of (NH4)2SO4. Judging from the reaction scheme, the current increase should not be more than double. The increase reached around 2.5 times probably because the forward enzyme reactions were promoted to balance the equilibrium which was displaced by the addition of PDC and ALDH. The enzyme cascade effect was enhanced with increased (NH4)2SO4 concentration, but was slightly affected by the enzyme concentration. These results indicate kosmotropic salts like (NH4)2SO4 shorten the distance between enzymes by salting them out, which can positively impact the cascade reactions. The relationship between enzyme cascade effect and (NH4)2SO4 concentration will be further investigated in future studies. [1] I. Shitanda, et al., ACS Sens. 8(2023), 6, 2368-2374. [2] S. Tsujimura, K. Murata, and W. Akatsuka, J. Am. Chem. Soc. 136 (2014) 14432-14437. Figure 1
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Pancapalaga, Wehandaka, and Endang Sri Hartati. "PELATIHAN PEMBUATAN ECO ENZYME DI PONDOK PESANTREN DAARUL FIKRI MALANG." Jurnal Pengabdian Masyarakat Bumi Raflesia 5, no. 1 (April 29, 2022): 777–81. http://dx.doi.org/10.36085/jpmbr.v5i1.3190.
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Eco enzim adalah cairan serba guna hasil fermentasi selama 90 hari dari sisa buah dan sayuran yang di campur dengan gula dan air. Adapun manfaatnya untuk kesehatan manusia, pertanian dan kesehatan lingkungan. Oleh karena itu tujuan pengabdian ini adalah untuk memperkenalkan dan mensosialisasikan eco enzyme kepada siswa siswi  pondok pesantren Daarul Fikri  dalam memanfaatkan limbah disekitar pondok pesantren, selain itu untuk melatih siswa siswi pondok pesantren  membuat eco enzyme. Metode pengabdian yang digunakan berupa sosialisasi dan pelatihan pembuatan eco enzym. Metode yang digunakan secara pendidikan, pelatihan dan pendampingan. Pendidikan dalam bentuk penyuluhan tentang pentingnya eco enzyme. Pelatihan diberikan untuk  meningkatkan ketrampilan dalam hal membuat eco enzyme. Sedangkan pendampingan di khususkan bagi mereka yang sungguh sungguh mau meneruskan untuk wirausaha dengan jalan membantu dalam hal pemasaran. Evaluasi kegiatan dilakukan dengan membandingkan peningkatan persentase pengetahuan dan ketrampilan sebelum dan sesudah pelatihan membuat eco enzyme. Hasil pengabdian menunjukan bahwa Berdasarkan hasil kegiatan pelatihan di pondok Daarul fikri malang dapat disimpulkan bahwa : Pelatihan pembuatan eco enzyme dapat meningkatkan pengetahuan siswa       (152 %) dan meningkatkan ketrampilan            siswa (200 %).
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Antoun, G. R., I. Brglez та D. G. Williamson. "A 17 β-hydroxysteroid dehydrogenase of female rabbit liver cytosol. Purification and characterization of multiple forms of the enzyme". Biochemical Journal 225, № 2 (15 січня 1985): 383–90. http://dx.doi.org/10.1042/bj2250383.
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Multiple forms of the soluble 17 beta-hydroxysteroid dehydrogenase of female rabbit liver were identified. NAD-dependent and NADP-dependent enzyme activities were separated by affinity chromatography on agarose-immobilized Procion Red HE3B, and three forms of the NADP-dependent enzyme activity were purified by chromatofocusing. These three enzyme forms are charge isomers and have no quaternary structure. The enzymes catalysed the C-17 oxidoreduction of oestrogens and androgens; with all enzyme forms the activity towards androgens was higher than that toward oestrogens. The enzymes also exhibited 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. Comparison of the relative activities of the enzymes towards a number of oestrogen and androgen substrates revealed differences among the enzyme forms for both the oxidative and the reductive reactions. In particular, one enzyme form had a significantly lower Km for the 3 alpha-hydroxysteroid substrate and a higher 3 alpha-/17 beta-hydroxysteroid dehydrogenase activity ratio than the other two enzyme forms.
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Li, Jie, Xin Jin, Yang Liu, Fan Li, Linlin Zhang, Xianyuan Zhu, and Yunfeng Lu. "Robust enzyme–silica composites made from enzyme nanocapsules." Chemical Communications 51, no. 47 (2015): 9628–31. http://dx.doi.org/10.1039/c5cc02053k.
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Novel enzyme composites are synthesized first by in situ polymerization around enzymes and a subsequent sol–gel process. Both the polymer shell and the silica shell with desired functional moieties provide not only great enzyme protection but also a favorable microenvironment, resulting in significantly enhanced activity and stability.
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Zhu, Zheng, Song Ling, Qi-Heng Yang, and Lin Li. "The Difference in the Carboxy-Terminal Sequence Is Responsible for the Difference in the Activity of Chicken and Rat Liver Fructose-2,6-Bisphosphatase." Biological Chemistry 381, no. 12 (December 18, 2000): 1195–202. http://dx.doi.org/10.1515/bc.2000.147.
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Abstract The fructose-2,6-bisphosphatase domain of the bifunctional chicken liver enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase shares approximately 95% amino acid sequence homology with that of the rat enzyme. However, these two enzymes are significantly different in their phosphatase activities. In this report, we show that the COOH-terminal 25 amino acids of the two enzymes are responsible for the different enzymatic activities. Although these 25 amino acids are not required for the phosphatase activity, their removal diminishes the differences in the activities between the two enzymes. In addition, two chimeric molecules (one consisting of the catalytic core of the chicken bisphosphatase domain and the rat COOH-terminal 25 amino acids, and the other consisting of most of the intact chicken enzyme and the rat COOH-terminal 25 amino acids) showed the same kinetic properties as the rat enzyme. Furthermore, substitution of the residues Pro456pro457Ala458 of the chicken enzyme with GluAlaGlu, the corresponding sequence in the rat liver enzyme, yields a chicken enzyme that behaves like the rat enzyme. These results demonstrate that the different bisphosphatase activities of the chicken and rat liver bifunctional enzymes can be attributed to the differences in their COOH-terminal amino acid sequences, particularly the three residues.
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Galperin, Michael Y., D. Roland Walker, and Eugene V. Koonin. "Analogous Enzymes: Independent Inventions in Enzyme Evolution." Genome Research 8, no. 8 (August 1, 1998): 779–90. http://dx.doi.org/10.1101/gr.8.8.779.
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Lieberman, Jack. "Enzymes in Sarcoidosis: Angiotensin-Converting-Enzyme (ACE)." Clinics in Laboratory Medicine 9, no. 4 (December 1989): 745–56. http://dx.doi.org/10.1016/s0272-2712(18)30602-4.
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Maeda, Masako. "New label enzymes for bioluminescent enzyme immunoassay." Journal of Pharmaceutical and Biomedical Analysis 30, no. 6 (January 2003): 1725–34. http://dx.doi.org/10.1016/s0731-7085(02)00514-9.
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Sree Kumar, K., Yashesh N. Vaishnav, and Joseph F. Weiss. "Radioprotection by antioxidant enzymes and enzyme mimetics." Pharmacology & Therapeutics 39, no. 1-3 (January 1988): 301–9. http://dx.doi.org/10.1016/0163-7258(88)90076-9.
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Mebs, D., S. Mieseler, U. Rimpau, C. Vossius, B. König, and S. Benesch. "Enzymes and enzyme inhibitors from marine sponges." Toxicon 33, no. 3 (March 1995): 304. http://dx.doi.org/10.1016/0041-0101(95)99364-9.
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Datta, Rahul, Swati Anand, Amitava Moulick, Divyashri Baraniya, Shamina Imran Pathan, Klement Rejsek, Valerie Vranova, et al. "How enzymes are adsorbed on soil solid phase and factors limiting its activity: A Review." International Agrophysics 31, no. 2 (April 25, 2017): 287–302. http://dx.doi.org/10.1515/intag-2016-0049.
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Abstract A majority of biochemical reactions are often catalysed by different types of enzymes. Adsorption of the enzyme is an imperative phenomenon, which protects it from physical or chemical degradation resulting in enzyme reserve in soil. This article summarizes some of the key results from previous studies and provides information about how enzymes are adsorbed on the surface of the soil solid phase and how different factors affect enzymatic activity in soil. Many studies have been done separately on the soil enzymatic activity and adsorption of enzymes on solid surfaces. However, only a few studies discuss enzyme adsorption on soil perspective; hence, we attempted to facilitate the process of enzyme adsorption specifically on soil surfaces. This review is remarkably unmatched, as we have thoroughly reviewed the relevant publications related to protein adsorption and enzymatic activity. Also, the article focuses on two important aspects, adsorption of enzymes and factors limiting the activity of adsorbed enzyme, together in one paper. The first part of this review comprehensively lays emphasis on different interactions between enzymes and the soil solid phase and the kinetics of enzyme adsorption. In the second part, we encircle various factors affecting the enzymatic activity of the adsorbed enzyme in soil.
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Lee, Hyeryeong, Yuna Bang, and In Seop Chang. "Facilitated Enzymatic Chain Reaction-Based Bioelectrocatalysis via Solid Binding Peptide-Guided Bienzyme Co-Immobilization Strategy." ECS Meeting Abstracts MA2023-01, no. 42 (August 28, 2023): 2357. http://dx.doi.org/10.1149/ma2023-01422357mtgabs.
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The multienzyme complex in biological systems are highly ordered so that intermediate molecules occurred during enzymatic sequential reaction are efficiently delivered to downstream enzymes without diffused to bulk phase. Recently, the cascadic multienzymes have been adopted to enzymatic electrocatalytic platform to be applied for enzyme-based bioelectronics such as enzyme fuel cell, biosensors, and electrosynthetic system. This cascadic enzyme-electrode, in which interfacial electron transfer (ET) occurs concurrently with inter-enzyme chain reaction, has been regarded promising for the advancement of enzyme-based bioelectronics performance. However, co-regulation of interfacial electrical connection and inter-enzyme chain reaction efficiency has been known to be highly challenging due to systematic complexity. In this context, the generalized enzyme immobilization tool is significantly needed to be developed to control inter-enzyme and enzyme-electrode interface concurrently. Herein, enzyme cascade-based direct bioelectrocatalytic system has been constructed by immobilizing enzymes using the solid binding peptide (SBP) linker that can control surface-orientation of enzymes on electrode. Here, invertase (INV) and FAD-dependent glucose dehydrogenase gamma-alpha complex (GDHγα) were utilized as upstream- and downstream enzyme so that the sucrose hydrolysis (at INV) and glucose oxidation (at GDHγα) is concomitantly occurred. Especially, the GDHγα that is direct electron transfer (DET)-capable oxidoreductase, has bi-function that are downstream catalysis and transport of produced electrons toward electrode that cause bioelectrocatalytic current signal. To immobilize enzymes and control relative orientation of coupling enzymes, the SBP linker was tethered various termini (C-, N-, or both termini) of INV when SBP fusion site of GDHγα was fixed to C-terminus of GDH α subunit to enable efficient interfacial DET, based on previous study. Therefore, the inter-enzyme relative orientation dependent chain reaction efficiency was evaluated with resulting DET-based electrocatalytic current. In the result, it was found that the interfacial DET at GDHγα-electrode could be affected by binding conformation of co-immobilized enzyme, fusion INV. Most importantly, the chain reaction efficiency between INV and GDHγα was revealed to be diverse depending on different relative orientation determined by SBP tethering sites in enzymes. The intermediate delivery route was changed by relative positioning of coupling active sites, affecting overall cascade reaction rate. Taking into account the factors related with interfacial DET and intermediate delivery, precise design of bienzymatic electrode is indeed necessary in order to introduce SBP-tethering technique to cascadic enzyme-derived direct electrocatalytic platform. Figure 1
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Mirzaei, Mitra, та Per Berglund. "Engineering of ωTransaminase for Effective Production of Chiral Amines". Journal of Computational and Theoretical Nanoscience 17, № 6 (1 червня 2020): 2827–32. http://dx.doi.org/10.1166/jctn.2020.8947.
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ωTransaminases are pyridoxal-5-phosphat (PLP) dependent enzymes having the ability to catalyze the transference of an amino group to a keto compound. These enzymes are used for production of chiral amines which are important building blocks in pharmaceutical industry. There is often a need to improve enzyme properties such as enzyme stability, enzyme specificity and to decrease substrate-product inhibition. Here, protein engineering was applied to improve the enzyme activity of the enzyme from Chromobacterium violaceum Rational-design and site-directed mutagenesis were applied on position of (W60) in the active site of the enzyme. Different mutated enzyme variants such as W60H, W60F and W60Y were made. Also, the enantiopreference of the wild type enzyme was reversed to produce (R)-chiral amines. For this aim, a screening assay was followed by semi-rational approach and saturation mutagenesis in the active site of the enzyme. Creating the mutated enzyme libraries resulted to obtaining two enzyme variants. Their properties were low enantiopreference towards formations of (R)-enantiopreference and low specific constant ratio between fast and slow enantiomers (Evalue around one).
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Wakano, Fahruddin. "POTENSI ECO-ENZYME DALAM MENINGKATKAN PERTUMBUHAN DAN PRODUKSI TANAMAN." Journal Gallus Gallus 2, no. 3 (July 13, 2024): 38–44. https://doi.org/10.51978/gallusgallus.v2i3.489.
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ABSTRAK Eco-enzyme merupakan produk hasil fermentasi bahan-bahan organik yang berasal dari limbah-limbah pertanian dan rumah tangga. Eco-enzyme memiliki beragam kegunaan mulai dari sebagai pupuk organik cair hingga sebagai pestisida nabati.eco-enzyme juga dapat digunakan dalam beberapa keperluan kebersihan rumah tangga. Dengan segudang manfaat tersebut penelitian mengenai potensi eco-enzyme telah dilakukan oleh beberapa peneliti dalam kurun waktu beberapa tahun ini, mulai dari pemanfaatan berbagai jenis jenis limbah seperti kulit jeruk, kulit kentang, kulit wortel, kulit bawang hingga limbah-limbah rumah tangga. Selain kulit, batang dan daun dari limbah-limbah tersebut juga dapat dimanfaatkan sebagai bahan untuk membuat eco-enzyme. Penggunaan eco-enzyme pada tanaman juga memiliki pengaruh yang signifikan dalam meningkatkan pertumbuhan serta produksi tanaman-tanaman pertanian. Sehingga dengan pemanfaatan eco-enzyme sebagai sumber pupuk organik, penangan pencemaran limbah sekaligus penerapan sistem pertanian organik dapat dicapai sekaligus. Keywords: Eco-enzyme, pupuk organik, limbah, pertumbuhan dan produksi tanaman. ABSTRACT Eco-enzyme is a product resulting from the fermentation of organic materials from agricultural and household waste. Eco-enzyme has various uses, ranging from liquid organic fertilizer to vegetable pesticide. Eco-enzyme can also be used for several household cleaning purposes. With a multitude of benefits, research on the potential of eco-enzymes has been carried out by several researchers over the past few years, starting from the use of various types of waste such as orange peels, potato peels, carrot peels, onion peels to household waste. Apart from the skin, stems, and leaves, these wastes can also be used as ingredients to make eco-enzymes. The use of eco-enzymes in plants also significantly influences the growth and production of agricultural plants. So using eco-enzymes as a source of organic fertilizer, handling waste pollution and implementing an organic farming system can be achieved simultaneously. Keywords: Eco-enzyme, organic fertilizer, waste, plant growth and production.
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Szczepanowski, Roman H., Renata Filipek, and Matthias Bochtler. "Crystal Structure of a Fragment of Mouse Ubiquitin-activating Enzyme." Journal of Biological Chemistry 280, no. 23 (March 16, 2005): 22006–11. http://dx.doi.org/10.1074/jbc.m502583200.
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Protein ubiquitination requires the sequential activity of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-ligase (E3). The ubiquitin-transfer machinery is hierarchically organized; for every ubiquitin-activating enzyme, there are several ubiquitin-conjugating enzymes, and most ubiquitin-conjugating enzymes can in turn interact with multiple ubiquitin ligases. Despite the central role of ubiquitin-activating enzyme in this cascade, a crystal structure of a ubiquitin-activating enzyme is not available. The enzyme is thought to consist of an adenylation domain, a catalytic cysteine domain, a four-helix bundle, and possibly, a ubiquitin-like domain. Its adenylation domain can be modeled because it is clearly homologous to the structurally known adenylation domains of the activating enzymes for the small ubiquitin-like modifier (SUMO) and for the protein encoded by the neuronal precursor cell-expressed, developmentally down-regulated gene 8 (NEDD8). Low sequence similarity and vastly different domain lengths make modeling difficult for the catalytic cysteine domain that results from the juxtaposition of two catalytic cysteine half-domains. Here, we present a biochemical and crystallographic characterization of the two half-domains and the crystal structure of the larger, second catalytic cysteine half-domain of mouse ubiquitin-activating enzyme. We show that the domain is organized around a conserved folding motif that is also present in the NEDD8- and SUMO-activating enzymes, and we propose a tentative model for full-length ubiquitin-activating enzyme.
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Hickey, A. M., L. Marle, T. McCreedy, P. Watts, G. M. Greenway, and J. A. Littlechild. "Immobilization of thermophilic enzymes in miniaturized flow reactors." Biochemical Society Transactions 35, no. 6 (November 23, 2007): 1621–23. http://dx.doi.org/10.1042/bst0351621.
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The exploitation of enzymes for biotransformation reactions for the production of new and safer drug intermediates has been the focus of much research. While a number of enzymes are commercially available, their use in an industrial setting is often limited to reactions that are cost-effective and they are rarely investigated further. However, the development of miniaturized flow reactor technology has meant that the cost of such research, once considered cost- and time-inefficient, would be much less prohibitive. The use of miniaturized flow reactors for enzyme screening offers a number of advantages over batch enzyme assay systems. Since the assay is performed on a miniaturized scale, enzyme, substrate and cofactor quantities are significantly reduced, thus reducing the cost of laboratory-scale investigations. Since flow reactors use microfluidic systems, where the substrate and products flow out of the system, the problems of substrate inhibition and product inhibition encountered by some enzymes are avoided. Quite often, enzymes fulfil a single-use function in biotransformation processes; however, enzyme immobilization allows enzyme reuse and often helps to increase enzyme stability. We have used an aminoacylase enzyme with potential use for industrial biotransformation reactions and have successfully immobilized it in miniaturized flow reactors. This L-aminoacylase is from the thermophilic archaeon Thermococcus litoralis. Two approaches to enzyme immobilization have been examined, both involving enzyme cross-linking. The first reactor type has used monoliths, to which the enzyme was attached, and the second contained previously cross-linked enzyme trapped using frits, in the microfluidic channels. Two different microreactor designs were used in the investigation: microreactor chips for the monoliths and capillary flow reactors for the cross-linked enzyme. These systems allowed passage of the substrate and product through the system while retaining the aminoacylase enzyme performing the catalytic conversion. The enzyme has been successfully immobilized and used to produce stable biocatalytic microreactors that can be used repeatedly over a period of several months.
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Ahmad, Raneem, Jordan Shanahan, Sydnie Rizaldo, Daniel S. Kissel, and Kari L. Stone. "Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst." Catalysts 10, no. 5 (May 2, 2020): 499. http://dx.doi.org/10.3390/catal10050499.
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In many respects, enzymes offer advantages over traditional chemical processes due to their decreased energy requirements for function and inherent greener processing. However, significant barriers exist for the utilization of enzymes in industrial processes due to their limited stabilities and inability to operate over larger temperature and pH ranges. Immobilization of enzymes onto solid supports has gained attention as an alternative to traditional chemical processes due to enhanced enzymatic performance and stability. This study demonstrates the co-immobilization of glucose oxidase (GOx) and horseradish peroxidase (HRP) as an enzyme system on Metal-Organic Frameworks (MOFs), UiO-66 and UiO-66-NH2, that produces a more effective biocatalyst as shown by the oxidation of pyrogallol. The two MOFs utilized as solid supports for immobilization were chosen to investigate how modifications of the MOF linker affect stability at the enzyme/MOF interface and subsequent activity of the enzyme system. The enzymes work in concert with activation of HRP through the addition of glucose as a substrate for GOx. Enzyme immobilization and leaching studies showed HRP/GOx@UiO-66-NH2 immobilized 6% more than HRP/GOx@UiO-66, and leached only 36% of the immobilized enzymes over three days in the solution. The enzyme/MOF composites also showed increased enzyme activity in comparison with the free enzyme system: the composite HRP/GOx@UiO-66-NH2 displayed 189 U/mg activity and HRP/GOx@UiO-66 showed 143 U/mg while the free enzyme showed 100 U/mg enzyme activity. This increase in stability and activity is due to the amine group of the MOF linker in HRP/GOx@UiO-66-NH2 enhancing electrostatic interactions at the enzyme/MOF interface, thereby producing the most stable biocatalyst material in solution. The HRP/GOx@UiO-66-NH2 also showed long-term stability in the solid state for over a month at room temperature.
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Antoun, G. R., та D. G. Williamson. "Age-dependent changes in the multiple forms of the soluble 17 β-hydroxysteroid dehydrogenase of female rabbit liver". Biochemical Journal 225, № 2 (15 січня 1985): 391–98. http://dx.doi.org/10.1042/bj2250391.
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The soluble NADP-dependent 17 beta-hydroxysteroid dehydrogenase activity of female rabbit liver increases with the age of the animal, the specific activity of the enzyme in the 56-day-old rabbit being 3 times that of the 28-day-old animal. The increase in activity is accompanied by a change in the molecular heterogeneity of the enzyme. Three forms (enzymes I, II and III) were identified in the liver cytosol of the 56-day-old female rabbit, whereas only one major form (enzyme IIIY) was present in the 28-day-old animal. Peptide maps of the four purified enzymes showed that there were minor differences in structure. The enzyme present in the liver of the 28-day-old rabbit was distinct from the three enzymes of the 56-day-old animal. All of the enzymes exhibited bifunctional activity, having 17 beta-hydroxysteroid dehydrogenase activity towards androgen and oestrogen substrates and 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. The differences in substrate specificity of the enzymes paralleled their differences in structure. The data suggest that one enzyme (enzyme III) may have a special role in steroid metabolism during development in the female rabbit.
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Gakhar, Lokesh, Zulfiqar A. Malik, Christopher C. R. Allen, David A. Lipscomb, Michael J. Larkin, and S. Ramaswamy. "Structure and Increased Thermostability of Rhodococcus sp. Naphthalene 1,2-Dioxygenase." Journal of Bacteriology 187, no. 21 (November 1, 2005): 7222–31. http://dx.doi.org/10.1128/jb.187.21.7222-7231.2005.
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ABSTRACT Rieske nonheme iron oxygenases form a large class of aromatic ring-hydroxylating dioxygenases found in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth, making them good candidates for use in synthesis of chiral intermediates and bioremediation. Studies of the chemical stability and thermostability of these enzymes thus become important. We report here the structure of free and substrate (indole)-bound forms of naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038. The structure of the Rhodococcus enzyme reveals that, despite a ∼30% sequence identity between these naphthalene dioxygenases, their overall structures superpose very well with a root mean square deviation of less than 1.6 Å. The differences in the active site of the two enzymes are pronounced near the entrance; however, indole binds to the Rhodococcus enzyme in the same orientation as in the Pseudomonas enzyme. Circular dichroism spectroscopy experiments show that the Rhodococcus enzyme has higher thermostability than the naphthalene dioxygenase from Pseudomonas species. The Pseudomonas enzyme has an apparent melting temperature of 55°C while the Rhodococcus enzyme does not completely unfold even at 95°C. Both enzymes, however, show similar unfolding behavior in urea, and the Rhodococcus enzyme is only slightly more tolerant to unfolding by guanidine hydrochloride. Structure analysis suggests that the higher thermostability of the Rhodococcus enzyme may be attributed to a larger buried surface area and extra salt bridge networks between the α and β subunits in the Rhodococcus enzyme.
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Pratiwi, Nurma, and Sigit Ardiansyah. "UTILIZATION OF AGRICULTURAL WASTE AS A SUBSTRATE FOR PRODUCING CELLULASE ENZYME BY ASPERGILLUS NIGER." Jurnal Pengembangan Agroindustri Terapan 1, no. 1 (September 12, 2022): 23–30. http://dx.doi.org/10.25181/jupiter.v1i1.2655.
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Fresh Fruit Bunches (FFB) of oil palm, bran, straw, and bagasse are agricultural wastes whose availability is very abundant in Indonesia. The agricultural waste is lignocellulosic waste which still has economic value if further processing is carried out, namely as a substrate in the production of cellulase enzymes. Cellulase enzymes are commonly used in various industries such as food biotechnology, textiles, animal feed, paper, and agriculture to degrade cellulose with its main products, namely glucose, cellobiose, and cellooligosaccharides. In producing cellulase enzymes, it is necessary to have microorganisms that have a high ability to produce enzymes, one of which is Aspergillus niger. The purpose of this study was to determine the activity of crude cellulase enzyme, protein content, and specific activity of cellulase enzyme from agricultural waste which includes FFB, bran, straw, and bagasse. The research methods included preparation of Aspergillus niger culture, delignification, basal medium preparation, cellulase enzyme production, enzyme extraction, crude cellulase enzyme activity test (CMC-ase), lowry method protein content test, and determination of cellulase enzyme specific activity. The study showed that the highest crude cellulase enzyme activity in bran was 26.83 U/ml, the highest protein content in bagasse was 63.42 g/ml, and the highest specific activity of cellulase enzyme in straw was 0.9818 U/ml. The high enzyme activity is influenced by the cellulose content in the material, type of substrate, media, substrate concentration, pH, and temperature.
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Lin, Peng, Hui Yang, Eiji Nakata, and Takashi Morii. "Mechanistic Aspects for the Modulation of Enzyme Reactions on the DNA Scaffold." Molecules 27, no. 19 (September 24, 2022): 6309. http://dx.doi.org/10.3390/molecules27196309.
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Cells have developed intelligent systems to implement the complex and efficient enzyme cascade reactions via the strategies of organelles, bacterial microcompartments and enzyme complexes. The scaffolds such as the membrane or protein in the cell are believed to assist the co-localization of enzymes and enhance the enzymatic reactions. Inspired by nature, enzymes have been located on a wide variety of carriers, among which DNA scaffolds attract great interest for their programmability and addressability. Integrating these properties with the versatile DNA–protein conjugation methods enables the spatial arrangement of enzymes on the DNA scaffold with precise control over the interenzyme distance and enzyme stoichiometry. In this review, we survey the reactions of a single type of enzyme on the DNA scaffold and discuss the proposed mechanisms for the catalytic enhancement of DNA-scaffolded enzymes. We also review the current progress of enzyme cascade reactions on the DNA scaffold and discuss the factors enhancing the enzyme cascade reaction efficiency. This review highlights the mechanistic aspects for the modulation of enzymatic reactions on the DNA scaffold.
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Lee, Sun Hyung, Ji Sook Lim, and Han Seung Kim. "Decomposition of Chlorinated Hydrocarbons Using the Biocatalyst Immobilized by Clay Minerals." Advanced Materials Research 356-360 (October 2011): 1089–92. http://dx.doi.org/10.4028/www.scientific.net/amr.356-360.1089.
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Biochemical decomposition of catechol and 4-chlorocatechol, degradation intermediate products of 4-chlorophenol, was investigated using enzymes and their immobilized forms by clay minerals. An oxygenase that can initiate oxidative ring-fission of aromatic compounds was obtained via cloning of its gene (cphA-1) encoding hydroxyquinol dioxygenase contained in Arthrobacter chlorophenolicus A6 and overexpression and purification of the enzyme. The enzyme expressed in vitro was then immobilized onto the clay mineral (montmorillonite). Michaelis-Menten kinetic analysis was conducted to compare the expressed enzymes and the immobilized biocatalysts with regard to their degradation activity and capability to sustain activities under severe environments. Vmax values for the immobilized enzymes were smaller than those for the originally cloned enzymes, indicating that loss of enzyme activity was accompanied in the enzyme immobilization process. However, the immobilized enzyme demonstrated far more stable degrading activity in response to wide environmental changes such as marked variation of pH, temperature, and ionic strength. This supported that the enzyme immobilization can provide great advantages for its field application and also should be useful for establishing the concept of ecological green U-City.
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Oro, Carolina E. Demaman, Bruna M. Saorin Puton, Luciana D. Venquiaruto, Rogério Marcos Dallago, and Marcus V. Tres. "Immobilization of Enzymes in Polymeric Materials Based on Polyamide: A Review." Processes 13, no. 1 (January 13, 2025): 200. https://doi.org/10.3390/pr13010200.
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The immobilization of enzymes in polyamide-based polymeric materials through covalent bonding is an established technique to stabilize and reuse biocatalysts in industrial processes. Traditionally, enzymes are immobilized using crosslinking agents that activate functional groups on both the support and the enzyme, creating strong bonds that securely anchor the enzyme to the surface. While effective for maintaining enzyme activity over multiple cycles, this method can reduce catalytic efficiency due to rigid binding and involves complex activation steps. Recently, in situ immobilization approaches have emerged as promising alternatives. In this method, enzymes are directly entrapped within the polymer matrix during the synthesis of the polyamide support, such as nylon, simplifying the process and offering enhanced control over enzyme distribution. For instance, studies have demonstrated that in situ immobilization can improve enzyme stability by protecting it within the polymeric network, while reducing production costs and waste. This review explores the ability of polyamide as a support material for immobilization of enzymes, analyzing key techniques, performance across applications, and future strategies to optimize polymer-enzyme interactions for industrial use.
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Vanderstocken, Gilles, Nicholas L. Woolf, Giuseppe Trigiante, Jessica Jackson, and Rory McGoldrick. "Harnessing the Potential of Enzymes as Inhaled Therapeutics in Respiratory Tract Diseases: A Review of the Literature." Biomedicines 10, no. 6 (June 17, 2022): 1440. http://dx.doi.org/10.3390/biomedicines10061440.
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Respiratory tract diseases (RTDs) are a global cause of mortality and affect patient well-being and quality of life. Specifically, there is a high unmet need concerning respiratory tract infections (RTIs) due to limitations of vaccines and increased antibiotic resistance. Enzyme therapeutics, and in particular plant-based enzymes, represent an underutilised resource in drug development warranting further attention. This literature review aims to summarise the current state of enzyme therapeutics in medical applications, with a focus on their potential to improve outcomes in RTDs, including RTIs. We used a narrative review approach, searching PubMed and clinicaltrials.gov with search terms including: enzyme therapeutics, enzyme therapy, inhaled therapeutics, botanical enzyme therapeutics, plant enzymes, and herbal extracts. Here, we discuss the advantages and challenges of enzyme therapeutics in the setting of RTDs and identify and describe several enzyme therapeutics currently used in the respiratory field. In addition, the review includes recent developments concerning enzyme therapies and plant enzymes in (pre-)clinical stages. The global coronavirus disease 2019 (COVID-19) pandemic has sparked development of several promising new enzyme therapeutics for use in the respiratory setting, and therefore, it is timely to provide a summary of recent developments, particularly as these therapeutics may also prove beneficial in other RTDs.
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O'Keefe, S. J., W. M. Bennet, A. R. Zinsmeister, and M. W. Haymond. "Pancreatic enzyme synthesis and turnover in human subjects." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 5 (May 1, 1994): G816—G821. http://dx.doi.org/10.1152/ajpgi.1994.266.5.g816.
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Animal studies have shown that pancreatic enzyme secretion is independent of enzyme synthesis. To investigate this relationship in humans, we have coinfused 14C-labeled leucine tracer with cholecystokinin octapeptide in nine healthy adults for 4 h and measured the rate of appearance of secreted and newly labeled enzymes in the duodenum. Enzyme secretion was well maintained throughout, but newly labeled enzymes only appeared in juice between 75 and 101 min (median time, 86 min), indicating that initial secretion was dependent on the release of zymogen stores and that the median production time for new enzymes was 86 min. Between 85 and 225 min there was a curvilinear increase in the enrichment of secreted enzymes with newly synthesized enzymes, suggesting a median turnover rate of zymogen stores of 29%/h (range 12-47%/h). In conclusion, our results suggest that in healthy humans, postprandial pancreatic enzyme secretion is maintained by the export of a large stored pool and is not rate limited by enzyme synthesis, since it takes approximately 86 min for newly synthesized enzymes to take part in the digestive process.