Journal articles: 'Enzymes – Industrial applications'

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Ghaffari-Moghaddam, M., H. Eslahi, D. Omay, and E. Zakipour-Rahimabadi. "Industrial applications of enzymes." Review Journal of Chemistry 4, no. 4 (October 2014): 341–61. http://dx.doi.org/10.1134/s2079978014040037.

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Robic, Audrey, Christophe Ullmann, Pascal Auffray, Cécile Persillon, and Juliette Martin. "Enzymes for industrial applications." OCL 24, no. 4 (June 30, 2017): D404. http://dx.doi.org/10.1051/ocl/2017027.

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Demain, Arnold L., and Sergio Sánchez. "Enzymes of industrial interest." Mexican journal of biotechnology 2, no. 2 (July 1, 2017): 74–97. http://dx.doi.org/10.29267/mxjb.2017.2.2.74.

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For many years, industrial enzymes have played an important role in the benefit of our society due to their many useful properties and a wide range of applications. They are key elements in the progress of many industries including foods, beverages, pharmaceuticals, diagnostics, therapy, personal care, animal feed, detergents, pulp and paper, textiles, leather, chemicals and biofuels. During recent decades, microbial enzymes have replaced many plant and animal enzymes. This is because microbial enzymes are widely available and produced economically in short fermentations and inexpensive media. Screening is simple, and strain improvement for increased production has been very successful. The advances in recombinant DNA technology have had a major effect on production levels of enzymes and represent a way to overproduce industrially important microbial, plant and animal enzymes. It has been calculated that 50-60% of the world enzyme market is supplied with recombinant enzymes. Molecular methods, including genomics and metagenomics, are being used for the discovery of new enzymes from microbes. Also, directed evolution has allowed the design of enzyme specificities and better performance.

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Zamost, Bruce L., Henrik K. Nielsen, and Robert L. Starnes. "Thermostable enzymes for industrial applications." Journal of Industrial Microbiology 8, no. 2 (September 1991): 71–81. http://dx.doi.org/10.1007/bf01578757.

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Singh, Rajesh Kumar, Pratiksha Singh, Mohini Prabha Singh, Pooja Nikhanj, Param Pal Sahota, Wenxia Fang, and Yang Rui Li. "Yeast α-L-Rhamnosidase: Sources, Properties, and Industrial Applications." SDRP Journal of Food Science & Technology 6, no. 1 (2021): 313–24. http://dx.doi.org/10.25177/jfst.6.1.ra.10742.

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Yeasts have been used for the heterologous production of a range of enzymes. However, α-L-rhamnosidase production in yeasts as well as its vast potential for biotechnological processes is less reported. α-L-Rhamnosidase is one of the important biotechnologically attractive enzymes in several industrial and biotechnological processes. In food and agriculture industries, the enzyme catalyzes the hydrolysis of hesperidin to release L-rhamnose and hesperidin glucoside, industrial removal of bitterness from citrus juices caused by naringin, and enhancing aroma in grape juices and derived beverages. In pharmaceutical and chemical industries, this enzyme is used in the structural determination of polysaccharides, glycosides and glycolipids, metabolism of gellan, conversion of chloropolysporin B to chloropolysporin C, and production of prunin. Rhamnosidases are extensively distributed in fungi and bacteria while their production from yeast sources is less reported. Yeast rhamnosidase is very important as it is produced in short-duration fermentation, with enhanced shelf life, high thermal stability, capable of retaining juice flavor, and is non-toxic for human consumption. In this review, an attempt has been made to fill up this gap by focusing on production, purification, characterization, structural and molecular biological studies of yeast rhamnosidase and its potential biotechnological applications. Keywords: Industrial applications, Naringin, Rhamnosidase, Yeast

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Joshi, Ritika, and Arindam Kuila. "Lipase and their different industrial applications: A review." Brazilian Journal of Biological Sciences 5, no. 10 (2018): 237–47. http://dx.doi.org/10.21472/bjbs.051004.

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Enzymes are also known natural catalysts. Lipases are flexible enzymes that are mostly used. These enzymes are found extensively all over the animal and plant kingdoms, likewise in molds and bacteria. Among all identified enzymes, lipases have concerned the mainly biotechnological attention. This review paper discusses the characteristic, microbial origin and application of lipases. The present review discussed about different characteristics and sources (fungal, bacteria’s) of lipase. The present article also discussed about different bioreactors used for lipase production and different biotechnological applications (food, detergent, paper and pulp, biofuels etc) of lipases. An observation to considerate lipases and their applications as bulk enzymes and high-value of production, these enzymes are having huge impact in different bioprocesses.

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Littlechild, Jennifer A. "Archaeal Enzymes and Applications in Industrial Biocatalysts." Archaea 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/147671.

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Archaeal enzymes are playing an important role in industrial biotechnology. Many representatives of organisms living in “extreme” conditions, the so-called Extremophiles, belong to the archaeal kingdom of life. This paper will review studies carried by the Exeter group and others regarding archaeal enzymes that have important applications in commercial biocatalysis. Some of these biocatalysts are already being used in large scale industrial processes for the production of optically pure drug intermediates and amino acids and their analogues. Other enzymes have been characterised at laboratory scale regarding their substrate specificity and properties for potential industrial application. The increasing availability of DNA sequences from new archaeal species and metagenomes will provide a continuing resource to identify new enzymes of commercial interest using both bioinformatics and screening approaches.

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Kleiner, Leslie. "Industrial applications of enzymes in Latin America." INFORM International News on Fats, Oils, and Related Materials 28, no. 8 (September 1, 2017): 38–39. http://dx.doi.org/10.21748/inform.09.2017.38.

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de Miguel Bouzas, Trinidad, Jorge Barros-Velazquez, and Tomas Gonzalez Villa. "Industrial Applications of Hyperthermophilic Enzymes: A Review." Protein & Peptide Letters 13, no. 7 (July 1, 2006): 645–51. http://dx.doi.org/10.2174/092986606777790548.

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Wackett, Lawrence P. "Industrial applications of microbial salt-tolerant enzymes." Microbial Biotechnology 5, no. 5 (August 24, 2012): 668–69. http://dx.doi.org/10.1111/j.1751-7915.2012.00355.x.

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Liese, Andreas, and Lutz Hilterhaus. "Evaluation of immobilized enzymes for industrial applications." Chemical Society Reviews 42, no. 15 (2013): 6236. http://dx.doi.org/10.1039/c3cs35511j.

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RAWLS, REBECCA. "Industrial applications open up for polymerlinked enzymes." Chemical & Engineering News 75, no. 17 (April 28, 1997): 27–28. http://dx.doi.org/10.1021/cen-v075n017.p027.

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Basso, Alessandra, and Simona Serban. "Industrial applications of immobilized enzymes—A review." Molecular Catalysis 479 (December 2019): 110607. http://dx.doi.org/10.1016/j.mcat.2019.110607.

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Alkorta, Itziar, Carlos Garbisu, María J. Llama, and Juan L. Serra. "Industrial applications of pectic enzymes: a review." Process Biochemistry 33, no. 1 (January 1998): 21–28. http://dx.doi.org/10.1016/s0032-9592(97)00046-0.

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Arshad, Hammad, SamrahTahir Khan, Ayesha Kanwal, and Imran Afzal. "Industrial Applications of Pectinases." Lahore Garrison University Journal of Life Sciences 1, no. 2 (May 5, 2020): 121–35. http://dx.doi.org/10.54692/lgujls.2017.010288.

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Application of pectinases in the commercial sector has been employed for nearly a century and due to the wide range of functions that these enzymes can work for, are making them critically important from industrial point of view. Pectinases are used in the industry on their role in the degradation of pectic substances aiding and enabling in overcoming the problems faced during the processing of purees, coffee and tea fermentation, fruit juices and in other food industry related manufacturing procedures. They break down the pectin content in the plants converting them to simpler molecules of galacturonic acid. The pectinases not only help in the food industry but also have remarkable applications in the textile, including retting, degumming, bio-scouring, maceration of plant tissues, paper making, and also has role in waste water treatment. Some of the roles of these pectinases solely and in conjunction with other enzymes e.g., amylases, xylanases, cellulases etc. have been comprehensively summarized in this review.

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Jujjavarapu, Satya Eswari, and Swasti Dhagat. "Evolutionary Trends in Industrial Production of α-amylase." Recent Patents on Biotechnology 13, no. 1 (February 1, 2019): 4–18. http://dx.doi.org/10.2174/2211550107666180816093436.

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Background: Amylase catalyzes the breakdown of long-chain carbohydrates to yield maltotriose, maltose, glucose and dextrin as end products. It is present in mammalian saliva and helps in digestion. Objective: Their applications in biotechnology include starch processing, biofuel, food, paper, textile and detergent industries, bioremediation of environmental pollutants and in clinical and medical applications. The commercial microbial strains for production of α-amylase are Bacillus subtilis, B. licheniformis, B. amyloliquefaciens and Aspergillus oryzae. Industrial production of enzymes requires high productivity and cannot use wild-type strains for enzyme production. The yield of enzyme from bacteria can be increased by varying the physiological and genetic properties of strains. Results: The genetic properties of a bacterium can be improved by enhancing the expression levels of the gene and secretion of the enzyme outside the cells, thereby improving the productivity by preventing degradation of enzymes. Overall, the strain for specific productivity should have the maximum ability for synthesis and secretion of an enzyme of interest. Genetic manipulation of α-amylase can also be used for the production of enzymes with different properties, for example, by recombinant DNA technology. Conclusion: This review summarizes different techniques in the production of recombinant α- amylases along with the patents in this arena. The washing out of enzymes in reactions became a limitation in utilization of these enzymes in industries and hence immobilization of these enzymes becomes important. This paper also discusses the immobilization techniques for used α-amylases.

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Mahnashi, Mater H., Uday M. Muddapur, Bhagya Turakani, Ibrahim Ahmed Shaikh, Ahmed Abdullah Al Awadh, Mohammed Merae Alshahrani, Ibrahim A. Almazni, et al. "A Review on Versatile Eco-Friendly Applications of Microbial Proteases in Biomedical and Industrial Applications." Science of Advanced Materials 14, no. 4 (April 1, 2022): 622–37. http://dx.doi.org/10.1166/sam.2022.4264.

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Enzymes are the keystone for metabolism or the chemical reactions in biological systems. They help to build certain substances and break others down. Enzymes play a critical role in our bodies, industries and corporate sectors. Protease is an enzyme that helps break the peptide bonds present in the protein and separates the amino acids. Microbial proteases are the ones where the bacteria can produce the protease enzyme. Among many industrial enzymes, microbial protease has a versatile role in many fields like laundry, leather preparation, feather degradation, detergent preparation, biocontrol agents, optical lens cleaners, tannery, deproteinization of prawn shell, prevention of putrefaction of cutting oil, food preservatives, chelating agents, fodder additives, removal and degradation of polymeric substances (EPS), removal of hairs in buffalo hide, waste treatment, bioremediation process, reduction of waste-activated sludge and biofilm formation, degumming of silk, cosmetics (to remove glabellar-frown lines), cheese making, Meat tenderization, rehydration of goat skins and reduced water quantity, fibrin degradation, photographic, silver recovery from X-ray films, dairy industry, control harmful nematodes, fruit juice, and bakery, soybean paste, and sauce industry, pulp mills, alcohol production, fish processing wastes, prion degradation. Microbial protease is popularly used in the detergent industry, leather industry, textile industry, food industry, dairy industry, meat processing industry, bakery industry, pharmaceutical industry, etc.

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Ahmad, M. A., U. Isah, I. A. Raubilu, S. I. Muhammad, and D. Ibrahim. "An overview of the enzyme: Amylase and its industrial potentials." Bayero Journal of Pure and Applied Sciences 12, no. 1 (April 15, 2020): 352–58. http://dx.doi.org/10.4314/bajopas.v12i1.53s.

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Amylases are group of enzymes produced by plants, animals and microorganisms, the enzyme has the ability to hydrolyze or degrade starch molecules into polymers containing units of glucose, thus, it is one of the most useful enzymes used by industries dependent on starch in their production processes. The enzyme has varying applications in food, fermentation, textile, pharmaceutical industries among others. Generally, amylase from microbial sources (i.e. fungal and bacterial origin) has over shadowed others in industrial usage. As such, this Paper aimed at reviewing amylase enzyme as a whole and some of its common industrial applications. The review visited the types of amylase based on hydrolases classification, its sources with emphasis to microorganisms, methods of production as well as effects of some chemical and physical parameters. The review also discusses some of the most common industrial application or uses of amylase enzyme in food, brewing, chemicals, paper, pharmaceutical, textile industries to mention but few. In conclusion, the reviewers suggest the use of microbial amylase due to it easy and simple technique in production, lower capital investment, lower energy requirement and high yield during production, exploration of more microbes with enzyme production potentials as well as improved industrial Scale production of the amylase for the betterment of the economy and improved industrial production of products. Key: Amylase, Application, Enzyme, Industry, Microbes and Starch.

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S. Borkar, Sucharitha, Mithali Shetty, Aravind Pai, K. S. Chandrashekar, H. N. Aswatha Ram, Kiran Kumar Kolathur, Venkatesh Kamath B., and Kanav Khera. "TREASURE WRAPPED IN AN ENIGMA: CHEMISTRY AND INDUSTRIAL RELEVANCE OF ENZYMES FROM RARE ACTINOMYCETES." RASAYAN Journal of Chemistry 15, no. 04 (2022): 2493–501. http://dx.doi.org/10.31788/rjc.2022.1546997.

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Microbial enzymes are known for their versatile catalytic property. With the advent of enzyme engineering, stringent environmental rules restraining the use of toxic chemicals, and need for the sustainable resource, there is a mounting demand for the utilization of these enzymes. Classified under Gram-positive filamentous bacteria, actinomycetes are ubiquitous and are one of the major sources of enzymes, antibiotics, and various such bioactive molecules. Rare actinomycetes are a less explored genera of actinomycetes. However, they are also a potential source of a diverse spectrum of enzymes that are principal of commercial importance. Enzymes produced by rare actinomycetes have a wide array of applications ranging from bioremediation techniques to the estimation of serum cholesterol levels. This untapped resource is industrially as well as biotechnologically valuable. Oxidative enzymes and esterases are two very important classes of enzymes produced by rare actinomycetes. The fundamental principles of catalysis applied by the organic catalysts are also relevant to the enzymes. This review highlights how this unexploited resource could be effectively exploited for various commercial applications and gives an overview of the industrial and biochemical applications of oxidative enzymes and esterases produced by rare actinomycetes. Protein engineering and modern biotechnology have been capable of manipulating the enzyme design making it a more stable and efficient asset to the industries

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Silva, Allison R. M., Jeferson Y. N. H. Alexandre, José E. S. Souza, José G. Lima Neto, Paulo G. de Sousa Júnior, Maria V. P. Rocha, and José C. S. dos Santos. "The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems." Molecules 27, no. 14 (July 15, 2022): 4529. http://dx.doi.org/10.3390/molecules27144529.

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Enzymatic biocatalysis is a sustainable technology. Enzymes are versatile and highly efficient biocatalysts, and have been widely employed due to their biodegradable nature. However, because the three-dimensional structure of these enzymes is predominantly maintained by weaker non-covalent interactions, external conditions, such as temperature and pH variations, as well as the presence of chemical compounds, can modify or even neutralize their biological activity. The enablement of this category of processes is the result of the several advances in the areas of molecular biology and biotechnology achieved over the past two decades. In this scenario, metal–organic frameworks (MOFs) are highlighted as efficient supports for enzyme immobilization. They can be used to ‘house’ a specific enzyme, providing it with protection from environmental influences. This review discusses MOFs as structures; emphasizes their synthesis strategies, properties, and applications; explores the existing methods of using immobilization processes of various enzymes; and lists their possible chemical modifications and combinations with other compounds to formulate the ideal supports for a given application.

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Cavalcante, Francisco T. T., Antônio L. G. Cavalcante, Isamayra G. de Sousa, Francisco S. Neto, and José C. S. dos Santos. "Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization." Catalysts 11, no. 10 (October 11, 2021): 1222. http://dx.doi.org/10.3390/catal11101222.

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The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level.

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Puntambekar, Ashwini, and Manjusha Dake. "Microbial Proteases: Potential Tools for Industrial Applications." Research Journal of Biotechnology 18, no. 2 (January 15, 2023): 159–71. http://dx.doi.org/10.25303/1802rjbt1590171.

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The use of enzymes in applied biotechnology has progressively increased in both industrial processes, products and in medical field. Proteolytic enzymes play an important regulatory role in many physiological processes and also represent a therapeutic target for several diseases including cancer, hypertension, blood clotting disorders, respiratory and viral infection. Proteases, a largest and ubiquitous class of enzymes, have a divergent role in biomedical field. The current review includes the basic information about the protease classification and optimized growth parameters to maximize the production of alkaline proteases and applications of proteases in a wide variety of industries including leather, textile, food manufacturing, pharmaceutical, detergent and waste management. The review also implicates the importance of genetic tools to obtain the novel engineered protease with improved catalytic performance and stability, pH and thermal tolerance.

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Sher, Hassan, Muhammad Faheem, Abdul Ghani, Rashid Mehmood, Hamza Rehman, and Syed A. I. Bokhari. "OPTIMIZATION OF CELLULASE ENZYME PRODUCTION FROM Aspergillus oryzae FOR INDUSTRIAL APPLICATIONS." World Journal of Biology and Biotechnology 2, no. 2 (August 15, 2017): 155. http://dx.doi.org/10.33865/wjb.002.02.0088.

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Cellulases are the hydrolytic group of enzymes, responsible for release of sugars in the bioconversion of the cellulosic biomass into a variety of value added industrial products. Fungal isolated cellulases are well studied and playing a significant role in various industrial processes. Enzymatic depolymerisation of cellulosic material has been done by the various fungal isolated enzymes. In the present study, the cultivation conditions for cellulase production from Aspergillus species were optimized. Optimization of scarification conditions such as time course, inoculum size, carbon source and concentration, nitrogen source, various pH levels were performed for the production of extracellular carboxymethyl cellulase and endoglucanase enzyme. The result exhibited, 15 % inoculums size, corncobs 2 % concentration, Urea and medium pH 7 at 30oC supported high yield of carboxymethyl cellulase (38.80 U/ml/min) and exoglucanase enzyme (10.94 U/ml/min) through a submerged fermentation (SmF). In future biotechnological applications in cellulase enzyme production attain a vital role to obtain high degradable yield.

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Parvizpour, Sepideh, Nurulfarhana Hussin, Mohd Shahir Shamsir, and Jafar Razmara. "Psychrophilic enzymes: structural adaptation, pharmaceutical and industrial applications." Applied Microbiology and Biotechnology 105, no. 3 (January 11, 2021): 899–907. http://dx.doi.org/10.1007/s00253-020-11074-0.

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Sette, Lara D., Valéria M. de Oliveira, and Maria Filomena A. Rodrigues. "Microbial lignocellulolytic enzymes: industrial applications and future perspectives." Microbiology Australia 29, no. 1 (2008): 18. http://dx.doi.org/10.1071/ma08018.

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The demand for microbial industrial enzymes is ever increasing due to their use in a wide variety of processes. Lignocellulolytic enzymes have potential applications in a large number of fields, including the chemical, fuel, food, agricultural, paper, textile and cosmetic industrial sectors. Lignocellulosic biomass is an abundant renewable resource composed of cellulose (a polymer of glucose that represents the major fraction of lignocellulose), hemicellulose (also a sugar polymer) and lignin (a complex phenylpropane polymer). Lignocellulosic material can be broken down by microorganisms into its sugar components, thereby providing a readily fermentable substrate. One of the most significant potential applications of lignocellulolytic enzymes is fuel production from agricultural and forest wastes as an alternative renewable energy resource. The need to reduce carbon dioxide emissions provides an additional incentive for the development of processes for production of fuels from lignocellulosic biomass and has attracted the interest of biotechnologists and microbiologists in recent decades.

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Rigoldi, Federica, Stefano Donini, Alberto Redaelli, Emilio Parisini, and Alfonso Gautieri. "Review: Engineering of thermostable enzymes for industrial applications." APL Bioengineering 2, no. 1 (March 2018): 011501. http://dx.doi.org/10.1063/1.4997367.

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Bhat, M. K., and S. Bhat. "Cellulose degrading enzymes and their potential industrial applications." Biotechnology Advances 15, no. 3-4 (January 1997): 583–620. http://dx.doi.org/10.1016/s0734-9750(97)00006-2.

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Houben, J. "Industrial applications of natural, modified and artificial enzymes." Journal of Biotechnology 24, no. 2 (June 15, 1992): v. http://dx.doi.org/10.1016/0168-1656(92)90115-p.

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Estell, David A. "Engineering enzymes for improved performance in industrial applications." Journal of Biotechnology 28, no. 1 (March 1993): 25–30. http://dx.doi.org/10.1016/0168-1656(93)90122-4.

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Robinson, Peter K. "Enzymes: principles and biotechnological applications." Essays in Biochemistry 59 (October 26, 2015): 1–41. http://dx.doi.org/10.1042/bse0590001.

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Enzymes are biological catalysts (also known as biocatalysts) that speed up biochemical reactions in living organisms, and which can be extracted from cells and then used to catalyse a wide range of commercially important processes. This chapter covers the basic principles of enzymology, such as classification, structure, kinetics and inhibition, and also provides an overview of industrial applications. In addition, techniques for the purification of enzymes are discussed.

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Mokhtar, Nur Fathiah, Raja Noor Zaliha Raja Abd. Rahman, Noor Dina Muhd Noor, Fairolniza Mohd Shariff, and Mohd Shukuri Mohamad Ali. "The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method." Catalysts 10, no. 7 (July 4, 2020): 744. http://dx.doi.org/10.3390/catal10070744.

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Four major enzymes commonly used in the market are lipases, proteases, amylases, and cellulases. For instance, in both academic and industrial levels, microbial lipases have been well studied for industrial and biotechnological applications compared to others. Immobilization is done to minimize the cost. The improvement of enzyme properties enables the reusability of enzymes and facilitates enzymes used in a continuous process. Immobilized enzymes are enzymes physically confined in a particularly defined region with retention to their catalytic activities. Immobilized enzymes can be used repeatedly compared to free enzymes, which are unable to catalyze reactions continuously in the system. Immobilization also provides a higher pH value and thermal stability for enzymes toward synthesis. The main parameter influencing the immobilization is the support used to immobilize the enzyme. The support should have a large surface area, high rigidity, suitable shape and particle size, reusability, and resistance to microbial attachment, which will enhance the stability of the enzyme. The diffusion of the substrate in the carrier is more favorable on hydrophobic supports instead of hydrophilic supports. The methods used for enzyme immobilization also play a crucial role in immobilization performance. The combination of immobilization methods will increase the binding force between enzymes and the support, thus reducing the leakage of the enzymes from the support. The adsorption of lipase on a hydrophobic support causes the interfacial activation of lipase during immobilization. The adsorption method also causes less or no change in enzyme conformation, especially on the active site of the enzyme. Thus, this method is the most used in the immobilization process for industrial applications.

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Yamaguchi, Hiroshi, Yuhei Kiyota, and Masaya Miyazaki. "Techniques for Preparation of Cross-Linked Enzyme Aggregates and Their Applications in Bioconversions." Catalysts 8, no. 5 (April 24, 2018): 174. http://dx.doi.org/10.3390/catal8050174.

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Enzymes are biocatalysts. They are useful in environmentally friendly production processes and have high potential for industrial applications. However, because of problems with operational stability, cost, and catalytic efficiency, many enzymatic processes have limited applications. The use of cross-linked enzyme aggregates (CLEAs) has been introduced as an effective carrier-free immobilization method. This immobilization method is attractive because it is simple and robust, and unpurified enzymes can be used. Coimmobilization of different enzymes can be achieved. CLEAs generally show high catalytic activities, good storage and operational stabilities, and good reusability. In this review, we summarize techniques for the preparation of CLEAs for use as biocatalysts. Some important applications of these techniques in chemical synthesis and environmental applications are also included. CLEAs provide feasible and efficient techniques for improving the properties of immobilized enzymes for use in industrial applications.

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Vingiani, Giorgio Maria, Pasquale De Luca, Adrianna Ianora, Alan D. W. Dobson, and Chiara Lauritano. "Microalgal Enzymes with Biotechnological Applications." Marine Drugs 17, no. 8 (August 5, 2019): 459. http://dx.doi.org/10.3390/md17080459.

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Enzymes are essential components of biological reactions and play important roles in the scaling and optimization of many industrial processes. Due to the growing commercial demand for new and more efficient enzymes to help further optimize these processes, many studies are now focusing their attention on more renewable and environmentally sustainable sources for the production of these enzymes. Microalgae are very promising from this perspective since they can be cultivated in photobioreactors, allowing the production of high biomass levels in a cost-efficient manner. This is reflected in the increased number of publications in this area, especially in the use of microalgae as a source of novel enzymes. In particular, various microalgal enzymes with different industrial applications (e.g., lipids and biofuel production, healthcare, and bioremediation) have been studied to date, and the modification of enzymatic sequences involved in lipid and carotenoid production has resulted in promising results. However, the entire biosynthetic pathways/systems leading to synthesis of potentially important bioactive compounds have in many cases yet to be fully characterized (e.g., for the synthesis of polyketides). Nonetheless, with recent advances in microalgal genomics and transcriptomic approaches, it is becoming easier to identify sequences encoding targeted enzymes, increasing the likelihood of the identification, heterologous expression, and characterization of these enzymes of interest. This review provides an overview of the state of the art in marine and freshwater microalgal enzymes with potential biotechnological applications and provides future perspectives for this field.

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Schiraldi, Chiara, Mariateresa Giuliano, and Mario De Rosa. "Perspectives on biotechnological applications of archaea." Archaea 1, no. 2 (2002): 75–86. http://dx.doi.org/10.1155/2002/436561.

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Many archaea colonize extreme environments. They include hyperthermophiles, sulfur-metabolizing thermophiles, extreme halophiles and methanogens. Because extremophilic microorganisms have unusual properties, they are a potentially valuable resource in the development of novel biotechnological processes. Despite extensive research, however, there are few existing industrial applications of either archaeal biomass or archaeal enzymes. This review summarizes current knowledge about the biotechnological uses of archaea and archaeal enzymes with special attention to potential applications that are the subject of current experimental evaluation. Topics covered include cultivation methods, recent achievements in genomics, which are of key importance for the development of new biotechnological tools, and the application of wild-type biomasses, engineered microorganisms, enzymes and specific metabolites in particular bioprocesses of industrial interest.

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Xu, Anming, Xiaoxiao Zhang, Shilei Wu, Ning Xu, Yan Huang, Xin Yan, Jie Zhou, Zhongli Cui, and Weiliang Dong. "Pollutant Degrading Enzyme: Catalytic Mechanisms and Their Expanded Applications." Molecules 26, no. 16 (August 6, 2021): 4751. http://dx.doi.org/10.3390/molecules26164751.

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The treatment of environmental pollution by microorganisms and their enzymes is an innovative and socially acceptable alternative to traditional remediation approaches. Microbial biodegradation is often characterized with high efficiency as this process is catalyzed via degrading enzymes. Various naturally isolated microorganisms were demonstrated to have considerable ability to mitigate many environmental pollutants without external intervention. However, only a small fraction of these strains are studied in detail to reveal the mechanisms at the enzyme level, which strictly limited the enhancement of the degradation efficiency. Accordingly, this review will comprehensively summarize the function of various degrading enzymes with an emphasis on catalytic mechanisms. We also inspect the expanded applications of these pollutant-degrading enzymes in industrial processes. An in-depth understanding of the catalytic mechanism of enzymes will be beneficial for exploring and exploiting more degrading enzyme resources and thus ameliorate concerns associated with the ineffective biodegradation of recalcitrant and xenobiotic contaminants with the help of gene-editing technology and synthetic biology.

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Shakya, Akhilesh Kumar, and Kutty Selva Nandakumar. "An update on smart biocatalysts for industrial and biomedical applications." Journal of The Royal Society Interface 15, no. 139 (February 2018): 20180062. http://dx.doi.org/10.1098/rsif.2018.0062.

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Recently, smart biocatalysts, where enzymes are conjugated to stimuli-responsive (smart) polymers, have gained significant attention. Based on the presence or absence of external stimuli, the polymer attached to the enzyme changes its conformation to protect the enzyme from the external environment and regulate the enzyme activity, thus acting as a molecular switch. Owing to this behaviour, smart biocatalysts can be separated easily from a reaction mixture and re-used several times. Several such smart polymer-based biocatalysts have been developed for industrial and biomedical applications. In addition, they have been used in biosensors, biometrics and nano-electronic devices. This review article covers recent advances in developing different kinds of stimuli-responsive enzyme bioconjugates, including conjugation strategies, and their applications.

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Xu, Meng-Qiu, Shuang-Shuang Wang, Li-Na Li, Jian Gao, and Ye-Wang Zhang. "Combined Cross-Linked Enzyme Aggregates as Biocatalysts." Catalysts 8, no. 10 (October 17, 2018): 460. http://dx.doi.org/10.3390/catal8100460.

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Enzymes are efficient biocatalysts providing an important tool in many industrial biocatalytic processes. Currently, the immobilized enzymes prepared by the cross-linked enzyme aggregates (CLEAs) have drawn much attention due to their simple preparation and high catalytic efficiency. Combined cross-linked enzyme aggregates (combi-CLEAs) including multiple enzymes have significant advantages for practical applications. In this review, the conditions or factors for the preparation of combi-CLEAs such as the proportion of enzymes, the type of cross-linker, and coupling temperature were discussed based on the reaction mechanism. The recent applications of combi-CLEAs were also reviewed.

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Petrila, Larisa-Maria, Vasile Robert Grădinaru, Florin Bucatariu, and Marcela Mihai. "Polymer/Enzyme Composite Materials—Versatile Catalysts with Multiple Applications." Chemistry 4, no. 4 (October 19, 2022): 1312–38. http://dx.doi.org/10.3390/chemistry4040087.

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A significant interest was granted lately to enzymes, which are versatile catalysts characterized by natural origin, with high specificity and selectivity for particular substrates. Additionally, some enzymes are involved in the production of high-valuable products, such as antibiotics, while others are known for their ability to transform emerging contaminates, such as dyes and pesticides, to simpler molecules with a lower environmental impact. Nevertheless, the use of enzymes in industrial applications is limited by their reduced stability in extreme conditions and by their difficult recovery and reusability. Rationally, enzyme immobilization on organic or inorganic matrices proved to be one of the most successful innovative approaches to increase the stability of enzymatic catalysts. By the immobilization of enzymes on support materials, composite biocatalysts are obtained that pose an improved stability, preserving the enzymatic activity and some of the support material’s properties. Of high interest are the polymer/enzyme composites, which are obtained by the chemical or physical attachment of enzymes on polymer matrices. This review highlights some of the latest findings in the field of polymer/enzyme composites, classified according to the morphology of the resulting materials, following their most important applications.

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Chapman, Jordan, Ahmed Ismail, and Cerasela Dinu. "Industrial Applications of Enzymes: Recent Advances, Techniques, and Outlooks." Catalysts 8, no. 6 (June 5, 2018): 238. http://dx.doi.org/10.3390/catal8060238.

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Ogawa, J. "Microbial enzymes: new industrial applications from traditional screening methods." Trends in Biotechnology 17, no. 1 (January 1, 1999): 13–20. http://dx.doi.org/10.1016/s0167-7799(98)01227-x.

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Shimizu, Sakayu. "Screening of novel microbial enzymes and their industrial applications." Journal of Biotechnology 136 (October 2008): S278. http://dx.doi.org/10.1016/j.jbiotec.2008.07.596.

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Liese, Andreas, and Lutz Hilterhaus. "ChemInform Abstract: Evaluation of Immobilized Enzymes for Industrial Applications." ChemInform 44, no. 38 (August 30, 2013): no. http://dx.doi.org/10.1002/chin.201338268.

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Hamid, Burhan, Zaffar Bashir, Ali Mohd Yatoo, Fayaz Mohiddin, Neesa Majeed, Monika Bansal, Peter Poczai, et al. "Cold-Active Enzymes and Their Potential Industrial Applications—A Review." Molecules 27, no. 18 (September 10, 2022): 5885. http://dx.doi.org/10.3390/molecules27185885.

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More than 70% of our planet is covered by extremely cold environments, nourishing a broad diversity of microbial life. Temperature is the most significant parameter that plays a key role in the distribution of microorganisms on our planet. Psychrophilic microorganisms are the most prominent inhabitants of the cold ecosystems, and they possess potential cold-active enzymes with diverse uses in the research and commercial sectors. Psychrophiles are modified to nurture, replicate, and retain their active metabolic activities in low temperatures. Their enzymes possess characteristics of maximal activity at low to adequate temperatures; this feature makes them more appealing and attractive in biotechnology. The high enzymatic activity of psychrozymes at low temperatures implies an important feature for energy saving. These enzymes have proven more advantageous than their mesophilic and thermophilic counterparts. Therefore, it is very important to explore the efficiency and utility of different psychrozymes in food processing, pharmaceuticals, brewing, bioremediation, and molecular biology. In this review, we focused on the properties of cold-active enzymes and their diverse uses in different industries and research areas. This review will provide insight into the areas and characteristics to be improved in cold-active enzymes so that potential and desired enzymes can be made available for commercial purposes.

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Johansen, Katja S. "Discovery and industrial applications of lytic polysaccharide mono-oxygenases." Biochemical Society Transactions 44, no. 1 (February 9, 2016): 143–49. http://dx.doi.org/10.1042/bst20150204.

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The recent discovery of copper-dependent lytic polysaccharide mono-oxygenases (LPMOs) has opened up a vast area of research covering several fields of application. The biotech company Novozymes A/S holds patents on the use of these enzymes for the conversion of steam-pre-treated plant residues such as straw to free sugars. These patents predate the correct classification of LPMOs and the striking synergistic effect of fungal LPMOs when combined with canonical cellulases was discovered when fractions of fungal secretomes were evaluated in industrially relevant enzyme performance assays. Today, LPMOs are a central component in the Cellic CTec enzyme products which are used in several large-scale plants for the industrial production of lignocellulosic ethanol. LPMOs are characterized by an N-terminal histidine residue which, together with an internal histidine and a tyrosine residue, co-ordinates a single copper atom in a so-called histidine brace. The mechanism by which oxygen binds to the reduced copper atom has been reported and the general mechanism of copper–oxygen-mediated activation of carbon is being investigated in the light of these discoveries. LPMOs are widespread in both the fungal and the bacterial kingdoms, although the range of action of these enzymes remains to be elucidated. However, based on the high abundance of LPMOs expressed by microbes involved in the decomposition of organic matter, the importance of LPMOs in the natural carbon-cycle is predicted to be significant. In addition, it has been suggested that LPMOs play a role in the pathology of infectious diseases such as cholera and to thus be relevant in the field of medicine.

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Manas Ranjan, Aashi Thakur, Chirag Chopra, and Reena Singh. "Microbial Oxidoreductases: Biotechnological and Synthetic Applications." International Journal of Research in Pharmaceutical Sciences 11, no. 4 (October 27, 2020): 6526–31. http://dx.doi.org/10.26452/ijrps.v11i4.3535.

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Enzymes are biocatalysts responsible for driving all biochemical reactions in the cells. The enzymes determine the physiology of a cell and together regulate the growth and proliferation of cells in response to various environmental signals. The ability of cells to adapt and respond to environmental conditions can be utilized for industrial applications. Hydrolases and oxidoreductases are the most common classes of enzymes used in various industries such as pharmaceutical, food and beverages, bioremediation and biofuels, among others. Oxidoreductases are the EC1 class enzymes that catalyze the biological oxidation and reduction reactions. They transfer electrons from one molecule (reductant that donates electron) to other molecules (oxidants those accept electron). Usually, the enzymes of this class are NAD+ (Nicotinamide Adenine Dinucleotide) or NADP (Nicotinamide Adenine Dinucleotide Phosphate)-dependent. The oxidoreductases are a diverse class of enzymes responsible for catalyzing highly stereo selective and regioselective reactions, because of which they are the enzymes of choice for synthesis of optically-active compounds. Alcohol dehydrogenase (ADH) is one of the most studied oxidoreductases. Generally, ADHs have narrow specificity towards their substrates. Here we are looking for ADH having high/ broad specificity towards the substrate. This review discusses the enzyme oxidoreductase, synthetic transformation with oxidoreductase and application of oxidoreductase in bioremediation.

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Tuan, Le Quang Anh. "Rational protein design for enhancing thermal stability of industrial enzymes." ENGINEERING AND TECHNOLOGY 8, no. 1 (August 17, 2020): 3–17. http://dx.doi.org/10.46223/hcmcoujs.tech.en.8.1.340.2018.

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Enzymes possessing many excellent properties such as high selectivity, consuming less energy, and producing less side products or waste have been widely applied as biocatalysts in pharmaceutical production and many industries such as biofuel, biomaterials, biosensor, food, and environmental treatment. Although enzymes have shown its potential as biocatalysts for many industrial applications, natural enzymes were not originated for manufacturing process which requires harsh reaction conditions such as high temperature, alkaline pH, and organics solvents. It was reported that reduction of final conversion of several enzymatic reactions was declined at high temperature. Protein engineering to improve the enzymes’ thermostability is crucial to extend the use of the industrial enzymes and maximize effectiveness of the enzyme-based procesess. Various industrial enzymes with improved thermostability were produced through rational protein engineering using different strategies. This review is not aimed to cover all successful rational protein engineering studies. The review focuses on some effective strategies which have widely used to increase the thermostability of several industrial enzymes through introduction of disulfide bonds and introduction of proline.

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Sohail, Muhammad, Noora Barzkar, Philippe Michaud, Saeid Tamadoni Jahromi, Olga Babich, Stanislav Sukhikh, Rakesh Das, and Reza Nahavandi. "Cellulolytic and Xylanolytic Enzymes from Yeasts: Properties and Industrial Applications." Molecules 27, no. 12 (June 12, 2022): 3783. http://dx.doi.org/10.3390/molecules27123783.

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Lignocellulose, the main component of plant cell walls, comprises polyaromatic lignin and fermentable materials, cellulose and hemicellulose. It is a plentiful and renewable feedstock for chemicals and energy. It can serve as a raw material for the production of various value-added products, including cellulase and xylanase. Cellulase is essentially required in lignocellulose-based biorefineries and is applied in many commercial processes. Likewise, xylanases are industrially important enzymes applied in papermaking and in the manufacture of prebiotics and pharmaceuticals. Owing to the widespread application of these enzymes, many prokaryotes and eukaryotes have been exploited to produce cellulase and xylanases in good yields, yet yeasts have rarely been explored for their plant-cell-wall-degrading activities. This review is focused on summarizing reports about cellulolytic and xylanolytic yeasts, their properties, and their biotechnological applications.

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Santos, Myllena R., Daniela B. Hirata, and Joelise A. F. Angelotti. "Lipases: Sources of Acquisition, Ways of Production, and Recent Applications." Catalysis Research 2, no. 2 (February 16, 2022): 1. http://dx.doi.org/10.21926/cr.2202013.

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Enzymes are extensively used in biotechnological processes in several areas of industry. They are sustainable and safe, and their specificity is another characteristic that improves the performance in the process. Among enzymes, lipase is relevant due to the ability to play different roles in the industry and the possibility of collecting them from microbial sources that are found in industrial residues. This can reduce the costs of enzyme production. In relation to that, lipase immobilization is an interesting process that allows the enzymes to be reused and improves enzyme robustness. Among them, the cross-linked enzyme aggregates (CLEAs) methodology is attractive due to its simplicity, low cost (given the absence of support), and greater interaction with the substrate. Thus, in this review, we discussed the potential of lipase. We reviewed the traditional and new sources of obtaining lipases, along with the ways of improving production, activity, and application in the industry.

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Poria, Vikram, Anuj Rana, Arti Kumari, Jasneet Grewal, Kumar Pranaw, and Surender Singh. "Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications." Biology 10, no. 12 (December 12, 2021): 1319. http://dx.doi.org/10.3390/biology10121319.

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Chitinases are a large and diversified category of enzymes that break down chitin, the world’s second most prevalent polymer after cellulose. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase (GH) families. Most of the distinct GH families, as well as the unique structural and catalytic features of various chitinolytic enzymes, have been thoroughly explored to demonstrate their use in the development of tailor-made chitinases by protein engineering. Although chitin-degrading enzymes may be found in plants and other organisms, such as arthropods, mollusks, protozoans, and nematodes, microbial chitinases are a promising and sustainable option for industrial production. Despite this, the inducible nature, low titer, high production expenses, and susceptibility to severe environments are barriers to upscaling microbial chitinase production. The goal of this study is to address all of the elements that influence microbial fermentation for chitinase production, as well as the purifying procedures for attaining high-quality yield and purity.

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Campbell, G. L., and M. R. Bedford. "Enzyme applications for monogastric feeds: A review." Canadian Journal of Animal Science 72, no. 3 (September 1, 1992): 449–66. http://dx.doi.org/10.4141/cjas92-058.

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The potential for industrial enzyme products as animal feed additives has attracted substantial interest from feed manufacturers as a novel means of improving animal performance. Enzyme manufacturers have also targeted feed as an alternate outlet for their products, which have primarily been in the food, beverage, and detergent industries. Despite a history dating back 35 years or more, only recently has enzyme application been extensive and efforts in research intensified. The use of enzymes that degrade polysaccharides of the endosperm cell wall has become most prominent. The major cell wall polysaccharides are the β-glucans in barley and oats and arabinoxylans (pentosans) in rye, wheat, and triticale. In barley and rye particularly, the cell wall carbohydrates are prone to solubilization. The major enzymes are endolytic and achieve their beneficial effects by removal of diffusion constraints that interfere with nutrient absorption. Although most nutrients are affected, fat malabsorption may be severe in chicks fed unsupplemented diets containing barley or rye. Young chicks give the greatest response to enzyme-induced viscosity reduction; the response is much less evident in older birds or in swine. In addition to carbohydrases, renewed research in dietary phytase has occurred with the realization that phytases provide a cost-effective alternative to inorganic phosphorous in regions with dense populations and intensive livestock production, where excessive phosphorus in animal wastes is a national concern. Other enzymes may also be beneficial, including supplementary α-amylase (in young animals) and oligosaccharidases for feeds high in oligosaccharides; however, this has not been shown conclusively. Enzymes with desired activity and stability characteristics for feed applications will continue to be developed. Future directions for enzyme research may also involve genetic manipulation of the substrate to facilitate more complete enzyme degradation, as in the case of the fiber components of rye. Key words: Dietary enzymes, β-glucanase, pentosanase, phytase, feed, β-glucan, pentosan, phytate

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Journal articles on the topic 'Enzymes – Industrial applications'

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