Journal articles: 'Enzyme inhibition'

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Minchenko, O. H. "Inhibition of ERN1 signaling enzyme affects hypoxic regulation." Ukrainian Biochemical Journal 87, no. 2 (April 27, 2015): 76–87. http://dx.doi.org/10.15407/ubj87.02.076.

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Ismail, Muhammad, Javid Hussain, Arif-ullah Khan, Abdul Latif Khan, Liaqat Ali, Farman-ullah Khan, Amir Zada Khan, Uzma Niaz, and In-Jung Lee. "Antibacterial, Antifungal, Cytotoxic, Phytotoxic, Insecticidal, and Enzyme Inhibitory Activities ofGeranium wallichianum." Evidence-Based Complementary and Alternative Medicine 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/305906.

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The present study describes the phytochemical investigations of the crude extracts of rhizomes and leaves ofGeranium wallichianum. The crude extracts were fractionated to obtainn-hexane, ethyl acetate, andn-butanol fractions, which were subjected to different biological activities and enzyme inhibition assays to explore the therapeutic potential of this medicinally important herb. The results indicated that the crude extracts and different fractions of rhizomes and leaves showed varied degree of antimicrobial activities and enzyme inhibitions in different assays. Overall, the rhizome extract and its different fractions showed comparatively better activities in various assays. Furthermore, the purified constituents from the repeated chromatographic separations were also subjected to enzyme inhibition studies against three different enzymes. The results of these studies showed that lipoxygenase enzyme was significantly inhibited as compared to urease. In case of chemical constituents, the sterols (2–4) showed no inhibition, while ursolic acid (1) and benzoic ester (6) showed significant inhibition of urease enzymes.

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Ochs, Raymond S. "Understanding Enzyme Inhibition." Journal of Chemical Education 77, no. 11 (November 2000): 1453. http://dx.doi.org/10.1021/ed077p1453.

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Ault, Addison. "Understanding Enzyme Inhibition." Journal of Chemical Education 79, no. 3 (March 2002): 311. http://dx.doi.org/10.1021/ed079p311.1.

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Ochs, Raymond S. "Understanding Enzyme Inhibition." Journal of Chemical Education 79, no. 3 (March 2002): 311. http://dx.doi.org/10.1021/ed079p311.2.

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Wirasti, Wirasti, Titi Lestari, and Isyti'aroh Isyti'aroh. "Penghambatan Ekstrak Daun Kremah (Alternanthera sessilis) Terhadap Enzim α-amilase secara In-Vitro." Pharmacon: Jurnal Farmasi Indonesia 18, no. 1 (June 30, 2021): 68–74. http://dx.doi.org/10.23917/pharmacon.v18i01.14657.

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An important treatment for type 2 diabetes is controlling blood glucose levels. α-amylase enzyme in the body plays a role in breaking down carbohydrates into starch. Control of the amylase enzyme is needed in diabetes cases Kremah plant (Alternanthera sessillis) is a plant whose leaves can be used to lower blood glucose levels because it contains secondary metabolites, one of which is flavonoids which can inhibit the α-amylase enzyme. The purpose of this study was to determine the activity and inhibition value of kremah leaves against the α-amylase enzyme. The method used in this research is the enzymatic reaction by measuring the intensity of the color using UV-Vis spectrophotometry. The IC50 value obtained by α-amylase enzyme inhibition was 101.89±7,21 μg / ml while the IC50 acarbose value was 127.17±4,42 μg / ml. These results indicate that kremah leaf extract has activity (hyperglycemia) by inhibiting complex carbohydrate hydrolyzing enzymes such as the α-inhibition enzyme α-Amylase which is good compared to acarbose because the IC50 value of the extract is smaller, so that the leaves of kremah has inhibiting of the α-amylase enzyme.

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Rousdy, Diah Wulandari, and Elvi Rusmiyanto Wardoyo. "In Vitro Antiinflammatory Activity of Bajakah (Spatholobus littoralis) Stem Extract." Biosaintifika: Journal of Biology & Biology Education 15, no. 2 (August 16, 2023): 150–57. http://dx.doi.org/10.15294/biosaintifika.v15i2.36227.

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The plant of Bajakah tampala (Spatholobus littoralis Hassk) has been utilized in traditional medication. Previous studies have proven the existence of in vivo anti-inflammatory activities of Bajakah plant (S. littoralis) in lowering the degree of carrageenan-induced paw oedema in mice. This study aims to determine the anti-inflammatory mechanism of S. littoralis extract in vitro through an approach of enzyme inhibition involved in the inflammatory reaction. The concentration of ethanol extract of Bajakah used was 0.1; 0.2; 0.4; 0.8; 1.6 mg/ml. The parameters measured were lipoxygenase enzyme inhibition, protein denaturation inhibition, protease enzyme inhibition, as well as plasma membrane stabilization. The results of the study showed the potential of the ethanol extract of Bajakah stems in inhibiting the inflammatory process viewed from the ability to inhibit inflammation-related enzymes. S. littoralis extract concentration of 1.6 mg/ml showed the best inhibition of the protein denaturation process (75.9%), the inhibition of trypsin protease enzyme (26.1%) and the stability of erythrocyte membrane (93.7%). However, the extracts of S. littoralis did not provide inhibition for the lipoxygenase enzyme in the range of 0.2-3.8%. This study proves the role of S. littoralis extract in the anti-inflammatory mechanism. It has the potential to be developed into standardized herbs.

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Masson, Patrick, and Aliya R. Mukhametgalieva. "Partial Reversible Inhibition of Enzymes and Its Metabolic and Pharmaco-Toxicological Implications." International Journal of Molecular Sciences 24, no. 16 (August 19, 2023): 12973. http://dx.doi.org/10.3390/ijms241612973.

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Partial reversible inhibition of enzymes, also called hyperbolic inhibition, is an uncommon mechanism of reversible inhibition, resulting from a productive enzyme–inhibitor complex. This type of inhibition can involve competitive, mixed, non-competitive and uncompetitive inhibitors. While full reversible inhibitors show linear plots for reciprocal enzyme initial velocity versus inhibitor concentration, partial inhibitors produce hyperbolic plots. Similarly, dose–response curves show residual fractional activity of enzymes at high doses. This article reviews the theory and methods of analysis and discusses the significance of this type of reversible enzyme inhibition in metabolic processes, and its implications in pharmacology and toxicology.

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AFFI, Sopi Thomas, Doh SORO, Souleymane COULIBALY, Bibata KONATE, and Nahossé ZIAO. "Modeling anticancer pharmacophore based on inhibition of HDAC7." SDRP Journal of Computational Chemistry & Molecular Modeling 5, no. 3 (2021): 657–63. http://dx.doi.org/10.25177/jccmm.5.3.ra.10776.

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Histone deacetylases (HDACs) are the target inhibition enzymes in cancer treatment via chemotherapy. Application of this therapeutic technique requires the use of drugs whose side effects are reduced and tiny with necessary safety. In this study, the methods and tools of pharmacophore modeling were used to investigate ten molecules known for their anticancer properties. Particular attention has been given to pinpoint a promising anti-cancer pharmacophore in order to lead new effective inhibitors. Using Discovery Studio 2.5 software, the ten compounds were docked within the active site of the HDAC7 enzyme. Analysis of the binding characteristics of all the compounds collected and tested in the model resulted in the characteristics produced by the 3D pharmacophore of the selected hypothesis. This led to note that the efficiency of any HDAC enzyme inhibitor was related to the characteristics of the designed pharmacophore. At the end, the pharmacophore hypothesis used here was presented as a useful basis for the development of anticancer compounds. Keywords: Pharmacophore, 3c0z, HDAC7, QSAR

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S, Iyswarya, Visweswaran S, Muthukumar N J, Tamilselvi S, and Mathukumar S. "Revealing Anti-diabetic potential of Siddha formulation Gandhaka Sarkkarai using alpha amylase and alpha glucosidase enzyme inhibition assay." International Journal of Ayurvedic Medicine 13, no. 2 (July 8, 2022): 515–19. http://dx.doi.org/10.47552/ijam.v13i2.2552.

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Background: Diabetes mellitus (DM) is a complex metabolic disorder which involves multiple pathology manifested with increased blood glucose, neural degeneration, chronic inflammation, organ dysfunction etc. Hyperactive metabolic enzymes like alpha amylase and alpha glucosidase that are involved in digestion of starch and sucrose further upswings the postprandial hyperglycaemia by rushing excess glucose moieties into the bloodstream. Drugs that effectively inhibit the action of these digestive enzymes may be expected to better regulate the post prandial blood glucose in the diabetic patients. Conventional anti-diabetic agents offer potential side effects upon long-term usage which includes vomiting, diarrhoea, pigmentation, GI disturbance, dark urination etc.The Siddha system of medicine has excelled in the art of treating human ailments for several centuries. Aim: Present investigation designed to investigate the anti-diabetic potential of siddha formulation Gandhaka sarkkarai (GS) using in-vitro alpha amylase and alpha glucosidase enzyme inhibition assay model. Results: It was evidenced from the outcome of the in-vitro data’s that the siddha formulation GS shown significant inhibition against alpha glucosidase enzyme with the maximum inhibition of about 50.44 % and the corresponding IC50 is 471.1 μg/ml, similar pattern of activity were observed against alpha amylase enzyme with the inhibition of 60.84 % (IC50 400.9 μg/ml). Conclusion: Our data concludes that siddha formulation GS possess significant anti-diabetic activity via inhibiting two major carbohydrate-digesting enzymes, further studies needs to extrapolated at pre-clinical level in order to ascertain the efficacy of the formulation. Key words: Diabetes mellitus, Alpha amylase, Alpha glucosidase, Siddha, Gandhaka sarkkarai, Enzyme inhibition assay, In-vitro, Anti-diabetic activity.

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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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12

Pasricha, Sharda, and Pragya Gahlot. "How Enzyme Inhibition Works!" Resonance 27, no. 5 (May 2022): 825–34. http://dx.doi.org/10.1007/s12045-022-1375-5.

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13

Hollenberg, Norman K. "Angiotensin-Converting Enzyme Inhibition." Journal of Cardiovascular Pharmacology 7, Supplement (1985): S45. http://dx.doi.org/10.1097/00005344-198500071-00009.

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Hollenberg, Norman K. "Angiotensin-Converting Enzyme Inhibition." Journal of Cardiovascular Pharmacology 7, Supplement 1 (1985): S40—S44. http://dx.doi.org/10.1097/00005344-198507001-00009.

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15

Bridges, Janis. "Angiotensin converting enzyme inhibition." Critical Care Nursing Quarterly 16, no. 2 (August 1993): 17–26. http://dx.doi.org/10.1097/00002727-199308000-00004.

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Waeber, Bernard, Jürg Nussberger, Lucienne Juillerat, and Hans R. Brunner. "Angiotensin Converting Enzyme Inhibition." Journal of Cardiovascular Pharmacology 14, no. 4 (January 1989): S53—S59. http://dx.doi.org/10.1097/00005344-198900000-00012.

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Waeber, Bernard, Jürg Nussberger, Lucienne Juillerat, and Hans R. Brunner. "Angiotensin Converting Enzyme Inhibition." Journal of Cardiovascular Pharmacology 14 (1989): S53—S59. http://dx.doi.org/10.1097/00005344-198906144-00012.

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Jackson, B., Mendelsohn, and C. I. Johnston. "Angiotensin-Converting Enzyme Inhibition." Journal of Cardiovascular Pharmacology 18, no. 7 (1991): S4–8. http://dx.doi.org/10.1097/00005344-199100180-00003.

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Giudicelli, Jean-François, Christine Richer, Christian Richard, Christian Thuillez, and Christine Capdeville. "Angiotensin Converting Enzyme Inhibition." American Journal of Hypertension 4, no. 3_Pt_2 (March 1991): 258S—262S. http://dx.doi.org/10.1093/ajh/4.3.258s.

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DiBianco, Robert. "Angiotensin converting enzyme inhibition." Postgraduate Medicine 78, no. 5 (October 1985): 229–48. http://dx.doi.org/10.1080/00325481.1985.11699167.

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Williams, John. "Enzyme inhibition and induction." Anaesthesia & Intensive Care Medicine 9, no. 4 (April 2008): 165–66. http://dx.doi.org/10.1016/j.mpaic.2008.02.004.

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Jackson, B., Mendelsohn, and C. I. Johnston. "Angiotensin-Converting Enzyme Inhibition." Journal of Cardiovascular Pharmacology 18 (1991): S4–8. http://dx.doi.org/10.1097/00005344-199106187-00003.

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23

Barry, M., and J. Feely. "Enzyme induction and inhibition." Pharmacology & Therapeutics 48, no. 1 (January 1990): 71–94. http://dx.doi.org/10.1016/0163-7258(90)90019-x.

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Nussberger, Jürg, Bernard Waeber, and Hans R. Brunner. "Angiotensin converting enzyme inhibition and renin inhibition." Journal of Hypertension 7 (April 1989): S75—S79. http://dx.doi.org/10.1097/00004872-198904002-00016.

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Pratasik, Veronika, Revolson Mege, and Mokosuli Semuel Yermia. "In Vitro Antidiabetic Activity Of Apis dorsata Binghami Nest Extract." JURNAL PEMBELAJARAN DAN BIOLOGI NUKLEUS 8, no. 3 (November 25, 2022): 733–43. http://dx.doi.org/10.36987/jpbn.v8i3.3196.

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Indonesia is ranked 7th out of 10 countries with the highest number of people with diabetes mellitus, which is estimated to increase every year.α -amylase is an enzyme that catalyzes the hydrolysis of α-1,4 glycosidic bonds of polysaccharides to produce dextrins, oligosaccharides, maltose and D-glucose. Apis dorsata Binghami honeycomb contains secondary metabolites that have antidiabetic potential, including inhibiting the action of the α-amylase enzyme. The purpose of this study was to determine the in vitro antidiabetic potential of Apis dorsata binghami nest extract. This study uses a descriptive research method where the research data are obtained through laboratory experiments. Honeycomb extraction using maceration method. Analysis of total flavonoid content using UV-Vis spectrophotometric method. Antidiabetic potency test using -amylase enzyme inhibition method. The results of the extraction study showed that the % yield of the extract was 11.82% with a brownish yellow color. Analysis of the total flavonoid content showed the results of 3.33 mgQE/g. The inhibitory activity of the -amylase enzyme, the IC50 value of the extract obtained was 158.48±7.42 g/mL, the acarbose value was 165.96±7.08 g/mL. These results indicate that the extract of A.dorsata Binghami nest has hyperglycemic activity by inhibiting complex carbohydrate hydrolyzing enzymes such as inhibition of the -amylase enzyme which is better than acarbose because the IC50 value of the extract is smaller. If the IC50 value is smaller then the enzyme inhibition is stronger. For further research, it is recommended to use a more specific enzyme, namely the -glucosidase enzyme.

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Rosyida, Risya, Mintarto Martosudiro, and Anton Muhibuddin. "Analysis of Chitinase Enzyme Trichoderma sp. in Degrading Fusarium oxysporum." Research Journal of Life Science 9, no. 3 (December 1, 2022): 131–45. http://dx.doi.org/10.21776/ub.rjls.2022.009.03.5.

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The chitinase enzyme in Trichoderma sp. play an important role in pathogen control. This is because chitin is the main component of the fungal cell wall which the chitinase enzyme can degrade. One Trichoderma sp. isolate was obtained (UBPK6) with the highest percentage of inhibition against Fusarium oxysporum, 76.71%. In addition, UBPK6 isolates also showed the highest bromocresol purple reagent test results (indicating the presence of chitinase enzymes). Chitinase enzyme activity was measured for Trichoderma asperellum isolates. The results showed that the optimum incubation period for enzyme production was the 4th day, with an enzyme activity value of 4.05 U/mL. It indicates that this time is the right time for harvesting enzymes. Furthermore, the effect of pH on the chitinase enzyme activity of Trichoderma asperellum fungus. The test results showed that the optimum value was produced at pH 5 with a value of 3.4 U/mL and decreased afterward. The pH five treatment was the best in inhibiting the growth of pathogens, with an inhibition value of 60.63%. The higher the content of the chitinase enzyme, the higher its ability to degrade damage to the germination of pathogenic spores, thus causing the growth of the pathogen to be inhibited.

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Godfrey, Wesley H., Kaho Cho, Shruthi Shanmukha, Jodie Deng, and Michael Kornberg. "Inhibition of distinct glycolytic enzymes produces differential effects on CD4 T cell function." Journal of Immunology 210, no. 1_Supplement (May 1, 2023): 148.12. http://dx.doi.org/10.4049/jimmunol.210.supp.148.12.

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Abstract Introduction: When T cells are activated, they upregulate glycolysis and take on a requisite Warburg phenotype. In this study, we evaluated the effect of inhibiting two distinct glycolytic enzymes, GAPDH and PGAM, on CD4 T cell differentiation. Methods/Results: Using the GAPDH inhibitor heptelidic acid, we found that GAPDH inhibition produces a potent anti-inflammatory phenotype in Th1 cells, significantly reducing IFNγ expression. We further showed that GAPDH inhibition produces the anti-inflammatory metabolite methylglyoxal, which is necessary for its anti-inflammatory effect. GAPDH inhibition also produced anti-inflammatory effects in vivo, as heptelidic acid significantly reduced disease severity and altered immune subsets in a therapeutic treatment paradigm in the MOG 35–55EAE model of multiple sclerosis. Furthermore, we showed that GAPDH inhibition enhances Treg polarization, while inhibiting PGAM, a downstream glycolytic enzyme, potently blocked Treg polarization. Additionally, we found that inhibition of PGAM increases serine biosynthesis and subsequently alters 1-carbon metabolism. We also found that PGAM gene expression is associated with Treg differentiation and response to immunotherapy in lung cancer patients. Conclusion: Overall, our in vitroand in vivoresults indicate that targeting the glycolytic enzyme GAPDH produces an anti-inflammatory phenotype via the methylglyoxal pathway, while targeting the downstream enzyme PGAM produces an opposite effect via regulation of serine synthesis. Our findings suggest that the functional consequences of glycolysis inhibition depend on the specific enzymes targeted, which represent promising novel therapeutic targets for immunological disease. This work was supported by NIH/NINDS grant K08NS104266 and Conrad N. Hilton Foundation Marilyn Hilton Bridging Award for Physician Scientists grant 17316 to MDK. WHG was supported by NIH MSTP Grant T32 GM136577 and the American Association of Immunologists’ Careers in Immunology Fellowship Program.

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Lim, Wen Xin Janice, Cheryl S. Gammon, Pamela von Hurst, Lynne Chepulis, and Rachel A. Page. "The Inhibitory Effects of New Zealand Pine Bark (Enzogenol®) on α-Amylase, α-Glucosidase, and Dipeptidyl Peptidase-4 (DPP-4) Enzymes." Nutrients 14, no. 8 (April 12, 2022): 1596. http://dx.doi.org/10.3390/nu14081596.

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The New Zealand pine bark extract (Enzogenol®) has previously been shown to elicit acute hypoglycaemic effects in humans. The present study investigated the underlying mechanisms of Enzogenol® in reducing postprandial glucose in humans. The potential inhibitory action of Enzogenol® against digestive enzymes: α-amylase and α-glucosidase, and dipeptidyl peptidase-4 (DPP-4) enzyme was determined. Enzogenol® demonstrated the ability to inhibit all three enzymes: α-amylase enzyme activity (IC50 3.98 ± 0.11 mg/mL), α-glucosidase enzyme activity (IC50 13.02 ± 0.28 μg/mL), and DPP-4 enzyme activity (IC50 2.51 ± 0.04 mg/mL). The present findings indicate the potential for Enzogenol® to improve postprandial glycaemia by delaying carbohydrate digestion via the inhibition of digestive enzymes (α-amylase and α-glucosidase), and enhancing the incretin effect via inhibiting the dipeptidyl-peptidase-4 enzyme. The inhibitory actions of Enzogenol® on enzymes should therefore be further validated in humans for its potential use in type 2 diabetes mellitus prevention and management.

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Demir, Yeliz, Cüneyt Türkeş, and Şükrü Beydemir. "Molecular Docking Studies and Inhibition Properties of Some Antineoplastic Agents against Paraoxonase-I." Anti-Cancer Agents in Medicinal Chemistry 20, no. 7 (July 3, 2020): 887–96. http://dx.doi.org/10.2174/1871520620666200218110645.

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Background: Currently, most of the drugs used in clinical applications show their pharmacological influences by inhibiting or activating enzymes. Therefore, enzyme inhibitors have an essential place in the drug design for many diseases. Objective: The current study aimed to contribute to this growing drug design field (i.e., medicine discovery and development) by analyzing enzyme-drug interactions. Methods: For this reason, Paraoxonase-I (PON1) enzyme was purified from fresh human serum by using rapid chromatographic techniques. Additionally, the inhibition effects of some antineoplastic agents were researched on the PON1. Results: The enzyme was obtained with a specific activity of 2603.57 EU/mg protein. IC50 values for pemetrexed disodium, irinotecan hydrochloride, dacarbazine, and azacitidine were determined to be 9.63μM, 30.13μM, 53.31μM, and 21.00mM, respectively. These agents found to strongly inhibit PON1, with Ki constants ranging from 8.29±1.47μM to 23.34±2.71mM. Dacarbazine and azacitidine showed non-competitive inhibition, while other drugs showed competitive inhibition. Furthermore, molecular docking was performed using maestro for these agents. Among these, irinotecan hydrochloride and pemetrexed disodium possess the binding energy of -5.46 and -8.43 kcal/mol, respectively. Conclusion: The interaction studies indicated that these agents with the PON1 possess binding affinity.

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OLUBISOLA ARIKE AFOLAYAN, FAWAZ ISSHAK, CYRIL CHIDIEBERE OKPARA, DAVID ONWUKA EME, and GODSLOVE OZURUMBA. "In vitro studies of magnesium oxide nano-particles of Saccharum officinarum root extract: Evaluation of the antidiabetic effect using alpha-glucosidase enzyme." World Journal of Biology Pharmacy and Health Sciences 16, no. 1 (October 30, 2023): 117–22. http://dx.doi.org/10.30574/wjbphs.2023.16.1.0357.

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Objective: Magnesium oxide nanoparticle green synthesis is said to have a wide range of biomedical uses. Inhibiting the activity of pancreatic enzymes is one method for treating diabetes. The goal of this study was to show in-vitro evidence that Saccharum officinarum magnesium oxide nanoparticles may inhibit the activity of the enzyme α-glucosidase. This study had a therapeutic focus as this could be emerging candidates of new drugs for controlling hyperglycemia. Materials and Procedures: Saccharum officinarum root extract was used to create magnesium oxide nanoparticles, which were then examined for bioactive components and tested for α-glucosidase inhibition. When the enzyme substrate solution was incubated with various doses of the grass-root Magnesium oxide nanoparticles, the activity of the enzyme was monitored to identify the kind of inhibition. Result: Magnesium oxide nanoparticles synthesized from Saccharum officinarum root extract showed concentration and time-dependent inhibition of α-glucosidase. An 85% inhibition was observed with 0.6 mg/ml of the synthesized nanoparticles. Conclusion: The results showed that the ethanolic extract of MgO nanoparticles synthesized by Saccharum officinarum exhibited effective antidiabetic activity, supporting its use in the treatment and control of diabetes.

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Demirci, Fatih, Ayşe Esra Karadağ, Sevde Nur Biltekin, and Betül Demirci. "In Vitro ACE2 and 5-LOX Enzyme Inhibition by Menthol and Three Different Mint Essential Oils." Natural Product Communications 16, no. 11 (November 2021): 1934578X2110550. http://dx.doi.org/10.1177/1934578x211055014.

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Mentha arvensis L., M. citrata L., and M. spicata L. (family Lamiaceae) essential oils, and their characteristic constituent, menthol, were evaluated in vitro for angiotensin converting enzyme 2 (ACE2) and 5-lipoxygenase (5-LOX) enzyme inhibitory activity. The chemical compositions of M. arvensis, M. citrata, and M. spicata essential oils were analysed both by GC-FID, and GC/MS; 82.0%, 38.1%, and 0.4% menthol were identified, respectively. M. spicata essential oil contained 88.2% carvone as its major component. The enzyme inhibitory activities of the essential oils were evaluated using a fluorometric multiplate based enzyme inhibition kit; the ACE2 inhibitions produced by M. arvensis, M. citrata, and M. spicata essential oils were 33%, 22%, and 73%, while the 5-LOX inhibitions were 84%, 79%, and 70%, respectively. In addition, menthol also showed remarkable ACE2 inhibition of 99.8%, whereas the 5-LOX inhibition was 79.9%. As a result, menthol and the three different mint essential oils may have antiviral potential applications against coronaviruses due to their ACE2 enzyme inhibition and anti-inflammatory features. However, further in vivo studies are needed to confirm the safety and efficacy.

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Dreshaj, Arber, Altin Dreshaj, Driton Sinanaj, Evetar Morina, and Shefket Dehari. "Main consequences of enzymatic induction and inhibition during the interaction of drugs and the role of CYP3A4, CYP3A45 enzymes." Current Issues in Pharmacy and Medical Sciences 37, no. 1 (March 1, 2024): 1–6. http://dx.doi.org/10.2478/cipms-2024-0001.

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Abstract The microsomal enzyme system is responsible for the metabolism of pollutants, toxic agents and drugs. With regards to drug metabolism, the activity of the constituent microsomal enzymes results in the reduction of pharmacological and toxicological activity through conversion of hydrophilic (water soluble) compounds to allow urinary excretion. Microsomal enzymes oxidize drugs and steroid hormones in reactions that require adenine nucleotide diphosphate (NADPH). Reversible inhibition reduces enzyme activity through reversible interaction. A covalent bond between the inhibitor and the enzyme can promote the destruction of essential functional groups of the enzyme. Enzyme induction and inhibition are problematic in drug polytherapy. Often the lack of effect of a drug or the side effects that a certain drug exhibits are problems of interaction of drugs with each other in that individually they inhibit or stimulate enzyme activity.

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Zaporozhets, T. S., I. D. Makarenkova, I. Y. Bakunina, Y. V. Burtseva, M. I. Kusaykin, L. A. Balabanova, T. N. Zvyagintseva, N. N. Besednova, and V. A. Rasskazov. "Inhibition of adherence of corynebacterium diphtheriae to human buccal epitelium by glycoside hydrolases of marine hydrobiontes." Biomeditsinskaya Khimiya 56, no. 3 (2010): 350–58. http://dx.doi.org/10.18097/pbmc20105603350.

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A possibility of adhesion inhibition of Corynebacterium diphtheriae to human buccal epithelium by glycoside hydrolases of marine hydrobiontes was investigated using α-galactosidase from marine bacterium Pseudoalteromonas sp. КММ 701, total enzyme preparation and β-1,3-glucanase from marine fungi Chaetomium, total enzyme preparation and β-1,3-glucanase from marine mollusk Littorina kurila, and total enzyme preparation from crystalline style of marine mollusk Spisula sachalinensis were used. The enzymes were added to test-tubes containing buccal epithelial cells and/or the toxigenic bacterial strain C. diphtheriae №1129, v. gravis. All the investigated enzymes were able to abort C. diphtheriae adherence to human buccal epithelocytes. Inhibition of adhesion was more pronounced in the case of treatment of epithelocytes with highly purified enzymes of marine hydrobiontes in comparison with total enzyme preparations. The significant inhibition of C. diphtheriae adhesion was observed when the enzymes were added to the epithelocytes with the attached microorganisms.The results obtained show that glycoside hydrolases of marine hydrobiontes degrade any carbohydrates expressed on cell surface of bacterium or human buccal epithelocytes, impair unique lectin-carbohydrate interaction and prevent the adhesion.

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Setiawan, Fery, Arif Rahman Nurdianto, Heribertus Agustinus B. Tena, Ahmad Yudianto, Jenny Sunariani, Achmad Basori, and Acrivida Mega Charisma. "Molecular Toxicology of Organophosphate Poisoning." Jurnal Ilmiah Kedokteran Wijaya Kusuma 11, no. 1 (April 12, 2022): 87. http://dx.doi.org/10.30742/jikw.v11i1.1596.

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The use of organophosphates (pesticides and other compounds to eradicate pests), currently, to increase the fulfillment of the population's consumption needs has a double-edged sword effect, on the one hand it can increase the need for food to be consumed by the population. The negative effect that can arise is the safety of organophosphate drugs which can contaminate the soil and water sources around the place where organophosphate drugs are used. The negative effects of organophosphates are associated with the effects of xenobiotics on humans who consume them. Xenobiotics are associated with toxicdynamic effects where organophosphates cause irreversible inhibition of the enzyme acetylcholinesterase (ACh). ACh is one of the main enzymes in the nervous system that terminates impulse conduction through the hydrolysis process of acetylcholine enzymes. Acetylcholinesterase is a specific molecular target of organophosphate pesticides. The inhibition of the Ach enzyme causes the inhibition of the acetylcholine enzyme which is normally always hydrolyzed by the Ach enzyme and is a specific biological marker of pesticide poisoning. Inhibition of ACh will cause the accumulation of the enzyme acetylcholine, resulting in negative effects of organophosphate poisoning which can lead to death. In this paper, the authors collect from various sources related to the study of molecular toxicology toxidynamic effects of drug safety and organophosphate poisoning. The results of this review article show that organophosphate poisoning is associated with irreversible inhibition of the acetylcholinesterase enzyme which results in death in the individual concerned.

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35

Arribas, Laura, and Carlos Vicente. "Enzyme Inhibition by Usnic Acids." Current Enzyme Inhibition 4, no. 4 (December 1, 2008): 180–85. http://dx.doi.org/10.2174/157340808786733622.

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36

Westley, Aiko M., and John Westley. "Enzyme Inhibition in Open Systems." Journal of Biological Chemistry 271, no. 10 (March 8, 1996): 5347–52. http://dx.doi.org/10.1074/jbc.271.10.5347.

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Ahmad, Bashir, S. M. Mukarram Shah, Haroon Khan, and S. M. Hassan Shah. "Enzyme inhibition activities ofteucrium royleanum." Journal of Enzyme Inhibition and Medicinal Chemistry 22, no. 6 (January 2007): 730–32. http://dx.doi.org/10.1080/14756360701306271.

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38

Ochs, Raymond S. "Correction to Understanding Enzyme Inhibition." Journal of Chemical Education 78, no. 1 (January 2001): 32. http://dx.doi.org/10.1021/ed078p32.2.

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Abeles, R. H., and T. A. Alston. "Enzyme inhibition by fluoro compounds." Journal of Biological Chemistry 265, no. 28 (October 1990): 16705–8. http://dx.doi.org/10.1016/s0021-9258(17)44813-7.

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40

Daigle, F., F. Trudeau, G. Robinson, M. R. Smyth, and D. Leech. "Mediated reagentless enzyme inhibition electrodes." Biosensors and Bioelectronics 13, no. 3-4 (March 1998): 417–25. http://dx.doi.org/10.1016/s0956-5663(97)00140-1.

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Schullek, John R., and Irwin B. Wilson. "Angiotensin converting enzyme: Substrate inhibition." Peptides 10, no. 2 (March 1989): 431–34. http://dx.doi.org/10.1016/0196-9781(89)90054-5.

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Butler, Anthony R., Adrianne M. Calsy, and Ian L. Johnson. "Enzyme inhibition by sodium nitroprusside." Polyhedron 9, no. 7 (January 1990): 913–19. http://dx.doi.org/10.1016/s0277-5387(00)84291-6.

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43

Abbas, Ghulam, Muhammad Abdullah Albroumi, Najeeb Ur Rehman, Hidayat Hussain, and Ahmed Sulaiman Al-Harrasi. "Evaluation of essential oils from Boswellia sacra and Teucrium mascatense against acetyl cholinesterase enzyme and urease enzyme." International Journal of Phytomedicine 8, no. 4 (February 18, 2017): 500. http://dx.doi.org/10.5138/09750185.1901.

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Enzyme inhibition is one of the most important areas of pharmaceutical research which resulted in the discoveries of several useful drugs. The prime aim of this study is to identify effective natural inhibitors against pharmacologically important enzymes such as acetylcholinesterase enzyme and urease enzyme. In present study, we evaluated the essential oils extracted from medicinally important plants including Boswellia sacra Flückiger (frankincense) and Teucrium mascatense Boiss. Two major constituents of frankincense essential oil including (+)-α-pinene and (R)-+-limonene were also investigated against these enzymes. The essential oils were extracted from Boswellia sacra and Teucrium mascatense which are native plants to the southern and northern areas of Oman, respectively. In this study, the essential oil of frankincense exhibited significant inhibition with IC50 value of 0.043±0.02 mg/mL, against acetylcholinesterase enzyme while against urease enzyme it has shown good inhibition with IC50 value of 0.17 ± 0.05 mg/mL. The essential oil obtained from the Teucrium mascatense was found to be in active against both the enzymes. On acetylcholinesterase enzyme inhibition assay, the (+)-α- pinene exhibited significant inhibition (IC50 = 0.094±0.01 mg/mL) while (R)-+- limonene was found to be inactive on this assay. Against urease enzyme (+)-α- pinene and (R)-+- limonene showed moderate activity 40.06±1.03 % and 19.5±1.00 %, respectively. Interestingly, the mixture of equal concentration of (+)-α- pinene and (R)-+- limonene exhibited 70% inhibition with IC50 value of (0.195 ± 0.10 mg/mL) which shows the synergistic relationship between them. Promising inhibitory potential of frankincense essential oil and (+)-α-pinene, against acetylcholinesterase enzyme and urease enzyme indicated their potential therapeutic role to manage Alzheimer’s disease and stomach ulcers, respectively.

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Esimbekova, Elena N., Anastasia A. Asanova, and Valentina A. Kratasyuk. "Alternative Enzyme Inhibition Assay for Safety Evaluation of Food Preservatives." Life 13, no. 6 (May 24, 2023): 1243. http://dx.doi.org/10.3390/life13061243.

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While food additives are widely used in the modern food industry and generally are important in maintaining the ability to provide food for the increasing world population, the progress occurring in this field is much ahead of the evaluation of their possible consequences for human health. The present study suggests a set of single- and multi-enzyme assay systems for revealing toxic effects of the most widely spread food preservatives, such as sorbic acid (E200), potassium sorbate (E202), and sodium benzoate (E211) at the primary molecular level of their interaction with enzymes. The assay is based on the inhibition of enzyme activity by toxic substances proportional to the amount of the toxicants in the sample. The single-enzyme assay system based on NAD(P)H:FMN oxidoreductase (Red) proved to be most sensitive to the impact of food additives, with the IC50 values being 29, 14, and 0.02 mg/L for sodium benzoate, potassium sorbate, and sorbic acid, respectively, which is considerably lower than their acceptable daily intake (ADI). No reliable change in the degree of inhibition of the enzyme assay systems by food preservatives was observed upon elongating the series of coupled redox reactions. However, the inhibition of activity of the multi-enzyme systems by 50% was found at a preservative concentration below the maximum permissible level for food. The inhibition effect of food preservatives on the activity of butyrylcholinesterase (BChE), lactate dehydrogenase (LDH), and alcohol dehydrogenase (ADH) was either absent or found in the presence of food preservatives at concentrations significantly exceeding their ADI. Among the preservatives under study, sodium benzoate is considered to be the safest in terms of the inhibiting effect on the enzyme activity. The results show that the negative effect of the food preservatives at the molecular level of organization of living things is highly pronounced, while at the organismal level it may not be obvious.

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Buneeva, O. A., L. N. Aksenova, and A. E. Medvedev. "A Simple Approach for Pilot Analysis of Time-dependent Enzyme Inhibition: Discrimination Between Mechanism-based Inactivation and Tight Binding Inhibitor Behavior." Biomedical Chemistry: Research and Methods 3, no. 1 (2020): e00115. http://dx.doi.org/10.18097/bmcrm00115.

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The increase in enzyme inhibition developed during prolonged incubation of an enzyme preparation with a chemical substance may be associated with both the non-covalent and also with covalent enzyme-inhibitor complex formation. The latter case involves catalytic conversion of a mechanism-based irreversible inhibitor (a poor substrate) into a reactive species forming covalent adduct(s) with the enzyme and thus irreversibly inactivating the enzyme molecule. Using a simple approach, based on comparison of enzyme inhibition after preincubation with a potential inhibitor at 4ºC or 37ºC we have analyzed inhibition of monoamine oxidase A (MAO A) by known MAO inhibitors pargyline and pirlindole (pyrazidol). MAO A inhibitory activity of pirlindole (reversible tight binding inhibitor of MAO A) assayed after mitochondrial wash was basically the same for the incubation at both 4ºC and 37ºC. In contrast to pirlindole, the effect of pargyline (mechanism based irreversible MAO inhibitor) strongly depended on the temperature of the incubation medium. At 37ºC the residual activity MAO A in the mitochondrial fraction after washing was significantly lower than in the mitochondrial samples incubated with pargyline at 4ºC. Results of this study suggest that using analysis of both time- and temperature-dependence of inhibition it is possible to discriminate mechanism-based irreversible inhibition and reversible tight binding inhibition of target enzym

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Abell, Lynn M. "Biochemical Approaches to Herbicide Discovery: Advances in Enzyme Target Identification and Inhibitor Design." Weed Science 44, no. 3 (September 1996): 734–42. http://dx.doi.org/10.1017/s0043174500094613.

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This paper focuses primarily on the means by which biochemical information can be used to identify enzymes which, upon inhibition, produce lethal phenotypes and the enzyme inhibitor design strategies that have the highest probability of not only inhibiting the enzyme but also translating that inhibition into herbicidal efficacy. The identification of an exquisitely lethal target site is the key initial component to this approach and has often been one of the most difficult steps because the attributes of a lethal site have, at best, been ill-defined. An examination of the characteristics of known targets provides some insight as to the definition of a lethal target. Recently, antisense RNA suppression of enzyme translation has been used to determine the extent of inhibition required for toxicity and offers potential as a strategy for identifying lethal target sites. After identification of a lethal target, detailed knowledge of the enzyme's chemical and kinetic mechanism as well as the protein's structure may be used to design potent inhibitors. Various types of inhibitors may be designed for a given enzyme. The advantages and disadvantages of a given type with respect to in vivo efficacy as well as the probability of herbicide resistance development will be discussed.

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Mole, Simon, and Peter G. Waterman. "Tannic acid and proteolytic enzymes: Enzyme inhibition or substrate deprivation?" Phytochemistry 26, no. 1 (December 1986): 99–102. http://dx.doi.org/10.1016/s0031-9422(00)81490-9.

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Babatunde, Oluwatoyin, Shehryar Hameed, Kingsley Mbachu, Faiza Saleem, Sridevi Chigurupati, Abdul Wadood, Rehman Ur, et al. "Evaluation of derivatives of 2,3-dihydroquinazolin-4(1H)-one as inhibitors of cholinesterases and their antioxidant activity: In vitro, in silico, and kinetics studies." Journal of the Serbian Chemical Society, no. 00 (2023): 5. http://dx.doi.org/10.2298/jsc211106005b.

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In search of potent inhibitors of cholinesterase enzymes and antioxidant agents, synthetic derivatives dihydroquinazolin-4(1H)-one 1-38 were evaluated as potential anti-Alzheimer agents through in vitro acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitions and radical (DPPH and ABTS) scavenging activities. The (SAR) was mainly based on the different substituents at the aryl part which showed a significant effect on the inhibitory potential of enzymes and radical scavenging activities. The kinetic studies of most active compounds showed a noncompetitive mode of inhibition for AChE and a competitive mode of inhibition for the BChE enzyme. Additionally, molecular modeling studies were carried out to investigate the possible binding interactions of quinazolinone derivatives with the active site of both enzymes.

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Fu, Ruimin, Hong Zhang, Wei Tang, Xue Yang, Ding Wang, and Wuling Chen. "Study on the effect of fengycin on the respiration and metabolic mechanism of Penicillium expansum." Materials Express 11, no. 12 (December 1, 2021): 2047–51. http://dx.doi.org/10.1166/mex.2021.2114.

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This study investigate the inhibiting effect of fengycin on respiration and nutrient utilization of Penicillium expansum. The respiratory inhibition rate of the P. expansum was determined by the test of dissolved oxygen fengycin, The effect of fengycin treatment on the activity of P. expansum mitochondrial complex enzyme was detected by mitochondrial enzyme activity assay. The ability of fengycin treatment to P. expansum the utilization of total sugar and total protein was determined by DNS colorimetric method and biuret method. After fengycin treatments, the TCA pathway of respiratory metabolism in P. expansum was inhibited. Besides, fengycin could block the gene expression in P. expansum by binding P. expansum mitochondrial complex enzyme II and III related genes. Therefore, the activity of mitochondrial enzymes was affected. With the increasement of fengycin concentration, the absorption and utilization capacity of P. expansum to total sugar and total protein decreased significantly. Fengycin could inhibit the respiratory metabolism and reduce the biochemical metabolism level in P. expansum and finally caused the growth inhibition.

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Ren, Jie, Chuan Shan Zhao, and Dong Mei Yu. "Research on the Technology and Mechanism of Inhibiting Stickies of Blanket by Enzyme Treatment." Advanced Materials Research 750-752 (August 2013): 1373–76. http://dx.doi.org/10.4028/www.scientific.net/amr.750-752.1373.

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The stickies in pulp and paper machinery especially in the blankets will cause a lot of problems such as paper defects, increasing the time of machine shut down . Therefore, Inhibiting the Stickies of blanket is very important to regular production. In this study,we mainly studied on the inhibition of Stickies in the blanket with enzyme. The processed blanket was treated by several kinds of enzymes. The results showed that the optimum enzyme treatment conditions were obtained as followings:PH of 7, temperature of 50°C, 2×104U/g of cellulose enzyme, 2×103U/g of amylase and 104U/g of lipase. The blankets obtained better cleaning situation under this conditions.

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Journal articles on the topic 'Enzyme inhibition'

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