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Journal articles on the topic 'Enzymes'

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Published: 4 June 2021

Last updated: 25 July 2025

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1

Stitt, M. "The Use of Transgenic Plants to Study the Regulation of Plant Carbohydrate Metabolism." Functional Plant Biology 22, no. 4 (1995): 635. http://dx.doi.org/10.1071/pp9950635.

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Transgenic plants with decreased expression of specific enzymes provide a powerful new tool to investigate metabolic regulation. Their use is discussed in the context of theories of metabolic regulation. It is argued that an enzyme is a key site for regulation, in the strict sense, when (i) natural mechanisms exist to alter the activity of the enzyme in vivo ('regulatability'), and (ii) a change in the activity of the enzyme is able to lead to a change in flux through the pathway ('regulatory capacity'). Previous approaches to the study of regulation allow the identification of enzymes with hi

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2

Christensen, Stefan Jarl, Silke Flindt Badino, Ana Mafalda Cavaleiro, Kim Borch, and Peter Westh. "Functional analysis of chimeric TrCel6A enzymes with different carbohydrate binding modules." Protein Engineering, Design and Selection 32, no. 9 (2019): 401–9. http://dx.doi.org/10.1093/protein/gzaa003.

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Abstract The glycoside hydrolase (GH) family 6 is an important group of enzymes that constitute an essential part of industrial enzyme cocktails used to convert lignocellulose into fermentable sugars. In nature, enzymes from this family often have a carbohydrate binding module (CBM) from the CBM family 1. These modules are known to promote adsorption to the cellulose surface and influence enzymatic activity. Here, we have investigated the functional diversity of CBMs found within the GH6 family. This was done by constructing five chimeric enzymes based on the model enzyme, TrCel6A, from the so

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3

Memon, Safyan Aman, Kinaan Aamir Khan, and Hammad Naveed. "HECNet: a hierarchical approach to enzyme function classification using a Siamese Triplet Network." Bioinformatics 36, no. 17 (2020): 4583–89. http://dx.doi.org/10.1093/bioinformatics/btaa536.

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Abstract Motivation Understanding an enzyme’s function is one of the most crucial problem domains in computational biology. Enzymes are a key component in all organisms and many industrial processes as they help in fighting diseases and speed up essential chemical reactions. They have wide applications and therefore, the discovery of new enzymatic proteins can accelerate biological research and commercial productivity. Biological experiments, to determine an enzyme’s function, are time-consuming and resource expensive. Results In this study, we propose a novel computational approach to predict

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4

Nixon, Andrew E., Marc Ostermeier, and Stephen J. Benkovic. "Hybrid enzymes: manipulating enzyme design." Trends in Biotechnology 16, no. 6 (1998): 258–64. http://dx.doi.org/10.1016/s0167-7799(98)01204-9.

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5

Cieśla, Joanna. "Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?" Acta Biochimica Polonica 53, no. 1 (2006): 11–32. http://dx.doi.org/10.18388/abp.2006_3360.

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Several enzymes that were originally characterized to have one defined function in intermediatory metabolism are now shown to participate in a number of other cellular processes. Multifunctional proteins may be crucial for building of the highly complex networks that maintain the function and structure in the eukaryotic cell possessing a relatively low number of protein-encoding genes. One facet of this phenomenon, on which I will focus in this review, is the interaction of metabolic enzymes with RNA. The list of such enzymes known to be associated with RNA is constantly expanding, but the mos

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Page, Michael I. "Past times: The efficiency of enzyme catalysis." Biochemist 25, no. 4 (2003): 52–53. http://dx.doi.org/10.1042/bio02504052.

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Understanding enzyme catalysis on a molecular and energetic basis has fascinated scientists for more than half a century. In addition to their obvious physiological involvement, the incredible efficiency of enzymes continues to intrigue us. In the absence of enzymes, many reactions of biological interest, e.g. the hydrolysis of proteins, carbohydrates and DNA, have half-lives of hundreds to millions of years. After a substrate is bound at an enzyme's active site, its halflife is usually milliseconds. The low concentration of enzymes in cells, which is often at or below the micromolar level, me

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Curtis, Nicole, Geordie Emberling, Alquama Lokhandwala, Mary Jo Ondrechen, and Constance Jeffery. "Metabolic Enzymes Moonlighting as RNA Binding Proteins." Structural Dynamics 12, no. 2_Supplement (2025): A345. https://doi.org/10.1063/4.0000651.

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RNA binding proteins play key roles in many aspects of RNA metabolism and function, including splicing, translation, localization, stability and degradation. Within the past few years, proteomics studies have identified dozens of enzymes in intermediary metabolism that bind to RNA. The wide occurrence and conservation of RNA binding ability across distant branches of the evolutionary tree suggest that these moonlighting enzymes are involved in connections between intermediary metabolism and gene expression that comprise far more extensive regulatory networks than previously thought. The effect

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8

March, John B., and Jason Clark. "Enzymes by post—restriction enzyme stability." Nature Biotechnology 18, no. 3 (2000): 243. http://dx.doi.org/10.1038/73590.

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9

Städler, Brigitte, and Alexander N. Zelikin. "Enzyme prodrug therapies and therapeutic enzymes." Advanced Drug Delivery Reviews 118 (September 2017): 1. http://dx.doi.org/10.1016/j.addr.2017.10.006.

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10

Woggon, Wolf-Dietrich. "Lessons from Enzymes and Enzyme Models." CHIMIA 53, no. 5 (1999): 234. https://doi.org/10.2533/chimia.1999.234.

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Results from our laboratory are presented demonstrating the significance of synthetic active-site analogs of metalloproteins to accomplish catalytic enzyme-like reactions and to identify key intermediates of the reaction cycles.

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Howell, Matthew, Daniel G. Dumitrescu, Lauren R. Blankenship, Darby Herkert, and Stavroula K. Hatzios. "Functional characterization of a subtilisin-like serine protease from Vibrio cholerae." Journal of Biological Chemistry 294, no. 25 (2019): 9888–900. http://dx.doi.org/10.1074/jbc.ra119.007745.

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Vibrio cholerae, the causative agent of the human diarrheal disease cholera, exports numerous enzymes that facilitate its adaptation to both intestinal and aquatic niches. These secreted enzymes can mediate nutrient acquisition, biofilm assembly, and V. cholerae interactions with its host. We recently identified a V. cholerae-secreted serine protease, IvaP, that is active in V. cholerae-infected rabbits and human choleric stool. IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted V. cholerae proteases, decreases binding of intelectin, an inte

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Jimoh, Abdulhameed, and Job Atteh. "Improving the metabolisable energy value of brewers’ dried grains with enzyme cocktails in poultry nutrition." Journal of Agricultural Sciences, Belgrade 63, no. 4 (2018): 409–19. http://dx.doi.org/10.2298/jas1804409j.

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The determination of the positive effects of exogenous enzymes is essential to ensure their inclusion in poultry feed formulation. This study was conducted to determine the effect of enzymes on the apparent metabolisable energy (AME) value of brewers? dried grain (BDG). Xylanase, phytase and multipurpose enzymes were used in a completely randomised design to determine the effects of individual exogenous enzymes and their cocktails on poultry metabolisable energy using adult cockerels. There were eight treatments comprising a control and seven experimental treatments with BDG and one, two or th

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Høst, Amalie Vang, Roberto Morellon-Sterling, Diego Carballares, John M. Woodley, and Roberto Fernandez-Lafuente. "Co-Enzymes with Dissimilar Stabilities: A Discussion of the Likely Biocatalyst Performance Problems and Some Potential Solutions." Catalysts 12, no. 12 (2022): 1570. http://dx.doi.org/10.3390/catal12121570.

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Enzymes have several excellent catalytic features, and the last few years have seen a revolution in biocatalysis, which has grown from using one enzyme to using multiple enzymes in cascade reactions, where the product of one enzyme reaction is the substrate for the subsequent one. However, enzyme stability remains an issue despite the many benefits of using enzymes in a catalytic system. When enzymes are exposed to harsh process conditions, deactivation occurs, which changes the activity of the enzyme, leading to an increase in reaction time to achieve a given conversion. Immobilization is a w

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Aliyev, Tofiq, and Səbrin Abdullayeva. "The Role of Enzymes in Modern Medicine: Advances, Applications, and Future Directions." Luminis Applied Science and Engineering 2, no. 1 (2025): 72–76. https://doi.org/10.69760/lumin.20250001012.

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Enzymes play a critical role in modern medicine, serving as essential biological catalysts in therapeutic and diagnostic applications. This article explores the use of enzymes in enzyme replacement therapy (ERT), pharmaceutical drug development, and clinical diagnostics. The advancements in biotechnology have led to the development of engineered enzymes with improved stability and efficiency, addressing challenges such as enzyme degradation, immunogenicity, and production costs. Recent innovations, including enzyme immobilization, nanotechnology-based delivery systems, and CRISPR-engineered en

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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 (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 repea

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Liu, Jie, and Joseph Wang. "Remarkable thermostability of bioelectrodes based on enzymes immobilized within hydrophobic semi‐solid matrices." Biotechnology and Applied Biochemistry 30, no. 2 (1999): 177–83. http://dx.doi.org/10.1111/j.1470-8744.1999.tb00910.x.

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An enhanced resistance to thermal denaturation was investigated for enzymes immobilized within hydrophobic semi‐solid matrices compared with both free enzymes and polymer‐entrapped enzymes. The bioelectrodes based on the immobilization of glucose oxidase, lactate oxidase, alcohol oxidase, polyphenol oxidase, peroxidase and L‐amino acid oxidase within a carbon‐paste matrix were constructed to examine their thermal stabilitiy at 60 °C or 80 °C. The rhodium/glucose oxidase‐containing carbon‐paste electrode was found to offer a remarkable stability when incubated at 60 °C over a long period of 4 m

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Gaziola, S. A., C. M. Teixeira, A. Ando, L. Sodek, and R. A. Azevedo. "Enzyme isolation and regulation with lysine biosynthesis and degradation in developing seeds of rice." International Rice Research Notes 21, no. 1 (1996): 27–28. https://doi.org/10.5281/zenodo.6999483.

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This article 'Enzyme isolation and regulation with lysine biosynthesis and degradation in developing seeds of rice' appeared in the International Rice Research Notes series, created by the International Rice Research Institute (IRRI) to expedite communication among scientists concerned with the development of improved technology for rice and rice-based systems. The series is a mechanism to help scientists keep each other informed of current rice research findings. The concise scientific notes are meant to encourage rice scientists to communicate with one another to obtain details on the resear

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Vikhrova, А. O., S. L. Yuzkiv, I. R. Buchkevych, М. S. Kurka, and V. I. Lubenets. "USE OF ENZYMES AND ENZYME PREPARATIONS IN FOOD TECHNOLOGIES." Chemistry, Technology and Application of Substances 5, no. 2 (2022): 118–35. http://dx.doi.org/10.23939/ctas2022.02.118.

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The analysis of literature sources on the use of enzymes, enzyme preparations and immobilized enzymes, allowed to determine which enzymes are used in certain sectors of the food industry. It is established that the condition for the use of enzymes in the food industry is the availability, low cost and inertia relative to the target product. Examples of the wide use of enzymes, enzyme preparations and immobilized enzymes in the technological processes of the food industry are given, which contribute to improving the quality of food products and improving their storage conditions.

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Ioannou, Y. A., D. F. Bishop, and R. J. Desnick. "Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion." Journal of Cell Biology 119, no. 5 (1992): 1137–50. http://dx.doi.org/10.1083/jcb.119.5.1137.

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Human lysosomal alpha-galactosidase A (alpha-Gal A) was stably overexpressed in CHO cells and its biosynthesis and targeting were investigated. Clone AGA5.3-1000Mx, which was the highest enzyme overexpressor, produced intracellular alpha-Gal A levels of 20,900 U/mg (approximately 100 micrograms of enzyme/10(7) cells) and secreted approximately 13,000 U (or 75 micrograms/10(7) cells) per day. Ultrastructural examination of these cells revealed numerous 0.25-1.5 microns crystalline structures in dilated trans-Golgi network (TGN) and in lysosomes which stained with immunogold particles using affi

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Hochendoner, Philip, Curtis Ogle, and William H. Mather. "A queueing approach to multi-site enzyme kinetics." Interface Focus 4, no. 3 (2014): 20130077. http://dx.doi.org/10.1098/rsfs.2013.0077.

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Multi-site enzymes, defined as where multiple substrate molecules can bind simultaneously to the same enzyme molecule, play a key role in a number of biological networks, with the Escherichia coli protease ClpXP a well-studied example. These enzymes can form a low latency ‘waiting line’ of substrate to the enzyme's catalytic core, such that the enzyme molecule can continue to collect substrate even when the catalytic core is occupied. To understand multi-site enzyme kinetics, we study a discrete stochastic model that includes a single catalytic core fed by a fixed number of substrate binding s

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Hemalatha.V, Kalyani.P Chandana Vineela.K Hemalatha.K.P.J*. "METHODS, APPLICATIONS OF IMMOBILIZED ENZYMES-A MINI REVIEW." INTERNATIONAL JOURNAL OF ENGINEERING SCIENCES & RESEARCH TECHNOLOGY 5, no. 11 (2016): 523–26. https://doi.org/10.5281/zenodo.168439.

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Reports on chemical immobilization of proteins and enzymes first appeared in the 1960s. Since then, immobilized proteins and enzymes have been widely used in the processing of variety of products and increasingly used in the field of medicine. Here, we present a review of recent developments in immobilized enzyme use in medicine. Immobilized enzymes are widely used for variety of applications. Based on the type of application, the method of immobilization and support material can be selected. The immobilized enzymes can be separated from the reaction mixture and reused and also immobilized in

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P, Keerthi, Lathif AK, and Nesaghi Amuthavel. "Enzyme Technology for Drug Discovery." Journal of Chemical Engineering & Process Technology 14, no. 14 (2023): 8. https://doi.org/10.35248/2157-7048.23.14.471.

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Enzymes are biochemical catalysts that facilitate chemical reactions under Physiological conditions. Currently enzymes are being employed in industrial biotechnology for numerous purposes for the production of novel and sustainable products at a speedy rate. Enzyme technology is the change of an enzyme's structure or catalytic activity in order to produce new metabolites or participate in new reaction pathways. Simultaneously, significant technical advancements are encouraging the chemical and pharmaceutical sectors to embrace enzyme technology, a movement fueled by worries about health, energ

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23

O'Keefe, S. J., W. M. Bennet, A. R. Zinsmeister, and M. W. Haymond. "Pancreatic enzyme synthesis and turnover in human subjects." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 5 (1994): G816—G821. http://dx.doi.org/10.1152/ajpgi.1994.266.5.g816.

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Animal studies have shown that pancreatic enzyme secretion is independent of enzyme synthesis. To investigate this relationship in humans, we have coinfused 14C-labeled leucine tracer with cholecystokinin octapeptide in nine healthy adults for 4 h and measured the rate of appearance of secreted and newly labeled enzymes in the duodenum. Enzyme secretion was well maintained throughout, but newly labeled enzymes only appeared in juice between 75 and 101 min (median time, 86 min), indicating that initial secretion was dependent on the release of zymogen stores and that the median production time

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Siregar, Benedicta Lamria, Rexi Sebastian Siallagan, Suwarnita Butar Butar, Bambang Mahmudi, and Elisabeth Sri Pujiastuti. "The Nutrient Content of Eco-enzymes from Mixture of Various Fruit Peels." Agro Bali : Agricultural Journal 7, no. 2 (2024): 475–87. http://dx.doi.org/10.37637/ab.v7i2.1646.

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Today, many institutions and individuals are paying attention to the development of technologies used in sustainable agriculture. One of the technologies is eco-enzyme that can be used as organic fertilizer. Several researchers have studied the use of eco-enzymes in agriculture, but studies on the nutrient content of eco-enzymes are still very limited. This research was conducted to investigate the nutrient content of two eco-enzyme preparations. The eco-enzymes were produced through the fermentation process of water, fruit peels, and molasses with a weight ratio of 10 : 3 : 1. Fruit peels use

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Wu, Zhuofu, Linjuan Shi, Xiaoxiao Yu, Sitong Zhang, and Guang Chen. "Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran." Molecules 24, no. 20 (2019): 3648. http://dx.doi.org/10.3390/molecules24203648.

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Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address th

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Dima, Lintang A. M., Andriani Rafael, Sonya T. M. Nge, Ocky K. Radjasa, Tiodor S. J. Manalu, and James Ngginak. "Isolation and Selection of Extracellular Enzymes in Sponge Symbiont Bacteria (Porifera: Demospongiae) from Tablolong Beach." JURNAL PEMBELAJARAN DAN BIOLOGI NUKLEUS 9, no. 3 (2023): 727–42. http://dx.doi.org/10.36987/jpbn.v9i3.5222.

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Marine biota has many benefits for human life. Sponges are a species of marine biota that can be used as a producer of antimicrobial compounds. The bacteria found in sponges have an important role in the continuity of life in the sea. The symbiotic lifestyle that occurs in bacteria and sponges has the opportunity to form substitutions for the content of secondary metabolites and enzymes, especially extracellular enzymes (amylase, protease, cellulose and lipase). This study aims to determine how to isolate sponge symbiotic bacteria and identify spongy symbiotic bacteria. The method used is purp

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Elnashar, Magdy M. M., and Mohamed E. Hassan. "Novel Epoxy Activated Hydrogels for Solving Lactose Intolerance." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/817985.

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“Lactose intolerance” is a medical problem for almost 70% of the world population. Milk and dairy products contain 5–10% w/v lactose. Hydrolysis of lactose by immobilized lactase is an industrial solution. In this work, we succeeded to increase the lactase loading capacity to more than 3-fold to 36.3 U/g gel using epoxy activated hydrogels compared to 11 U/g gel using aldehyde activated carrageenan. The hydrogel’s mode of interaction was proven by FTIR, DSC, and TGA. The high activity of the epoxy group was regarded to its ability to attach to the enzyme’s –SH, –NH, and –OH groups, whereas the

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Yalcinkaya, Zeki, Hakan Turan, and Halit Demir. "Importance of enzyme immobilization for human health." Medical Science and Discovery 4, no. 9 (2017): 69–71. https://doi.org/10.36472/msd.v4i9.194.

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In this review, we aimed to emphasize the importance of immobilized enzymes for human health in shed light on recent literature. In addition to our clinical experiences, some literature studies on immobilized enzymes were evaluated. The immobilized enzymes bind to a specific region physically by using mediator enzymes and shows catalytic activities repeatedly and continuously without losing their catalytic activities. In other words, enzyme immobilization is the trapping or binding of the insoluble form of the enzyme or the carrier agent to itself. Compared to free enzymes in solution, immobil

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Wang, Sheng-Wei, and Tian-Yi Wang. "Study on Antibacterial Activity and Structure of Chemically Modified Lysozyme." Molecules 28, no. 1 (2022): 95. http://dx.doi.org/10.3390/molecules28010095.

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Lysozyme is a natural protein with a good bacteriostatic effect, but its poor inhibition of Gram-negative bacteria limits its development potential as a natural preservative. Therefore, the modification of natural lysozyme to expand the antimicrobial spectrum become the focus of lysozyme study. Egg white lysozyme has low cost, rich content in nature, is easy to obtain, strong stability, and high enzyme activity, so it can be applied in the modification of lysozyme. Egg white lysozyme was modified by chemical methods using organic acids. Caffeic acid and p-coumaric acid in organic acids were us

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Ali, Hala M., and Ghazi M. Aziz. "Purification and characterization of amylase from local isolate Pseudomonas sp.SPH4." Journal of Biotechnology Research Center 6, no. 1 (2012): 69–79. http://dx.doi.org/10.24126/jobrc.2012.6.1.205.

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The amylase produced from local isolate Pseudomonas sp. SPH4 was purified by precipitation with 30% saturation ammonium sulphate, followed by ion-exchange chromotography using DEAE-cellulose column, and Gel filtration using Sephacryl S-300 column.The two iso-enzymes (a, b) were purified to (2.83, 3.47) times in the last step with an enzymes yields of (32.36, 76.34)% respectively. Enzyme characterization of the two iso-enzymes indicated that the optimum pH for the two iso-enzymes a and b were (7, 7.5) respectively, while the optimum pH for the iso-enzymes stability were (6.5, 7) respectively. T

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Su, Xiaoyun, Yejun Han, Dylan Dodd, et al. "Reconstitution of a Thermostable Xylan-Degrading Enzyme Mixture from the Bacterium Caldicellulosiruptor bescii." Applied and Environmental Microbiology 79, no. 5 (2012): 1481–90. http://dx.doi.org/10.1128/aem.03265-12.

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ABSTRACTXylose, the major constituent of xylans, as well as the side chain sugars, such as arabinose, can be metabolized by engineered yeasts into ethanol. Therefore, xylan-degrading enzymes that efficiently hydrolyze xylans will add value to cellulases used in hydrolysis of plant cell wall polysaccharides for conversion to biofuels. Heterogeneous xylan is a complex substrate, and it requires multiple enzymes to release its constituent sugars. However, the components of xylan-degrading enzymes are often individually characterized, leading to a dearth of research that analyzes synergistic actio

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Mao, Shucan, Jiawen Jiang, Ke Xiong, et al. "Enzyme Engineering: Performance Optimization, Novel Sources, and Applications in the Food Industry." Foods 13, no. 23 (2024): 3846. http://dx.doi.org/10.3390/foods13233846.

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This review summarizes the latest progress in enzyme preparation, including enzyme design and modification technology, exploration of new enzyme sources, and application of enzyme preparation in food processing, detection, and preservation. The directed evolution technology improved the stability and catalytic efficiency of enzymes, while enzyme immobilization technology enhanced reusability and industrial applicability. Extremozymes and biomimetic enzymes exhibit excellent performance under harsh conditions. In food processing, enzyme preparation can improve food quality and flavor. In food d

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Khudhair, Saad Hussein, Melad Khalaf Mohammed, and Ahmed Darweesh Jabbar. "Immobilization of lipase enzyme extracted from thermophilic Bacillus licheniformis 14T local isolate." Advancements in Life Sciences 11, no. 2 (2024): 362. http://dx.doi.org/10.62940/als.v11i2.2251.

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Background: Currently, lipase enzymes are considered important bio-catalysts in many industries due to their unique properties in catalyzing various types of reactions in aqueous solutions. By targeting hydrocarbons in the oil, lipase enzymes contribute to the breakdown of hydrocarbons, reducing the environmental impact of oil spills and facilitating the remediation of contaminated areas.Methods: A thermostable lipase from local isolate Bacillus licheniformis 14T has been immobilized on four different supports that include the inactivated chitosan beads, activated chitosan beads with glutarald

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Daris, Ummi Syahda, Ummi Halimah Rahmatika, and Angel Kurnilah Fitri. "The potential of plant protease enzymes as rennet alternatives for developing halal cheese product: A review." Journal of Halal Science and Research 5, no. 1 (2024): 60–70. http://dx.doi.org/10.12928/jhsr.v5i1.9524.

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Cheese, a derivative of dairy products made using the enzyme rennet, has received full attention because of the critical point for halalness from the milk coagulation process, which uses the rennet enzyme. Rennet enzymes can be obtained from the stomachs of animals such as cows, pigs, and goats, and they can also be produced from microbes. This very high risk of haram sources or unclean contamination has led to the development of cheese products using plant protease enzymes as a substitute for rennet enzymes. This study aims to highlight plant protease enzymes, characterize the enzymes produce

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Liu, Ziyi, and Stephen R. Smith. "Cross-Linked Enzyme Aggregate (CLEA) Preparation from Waste Activated Sludge." Microorganisms 11, no. 8 (2023): 1902. http://dx.doi.org/10.3390/microorganisms11081902.

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Enzymes are used extensively as industrial bio-catalysts in various manufacturing and processing sectors. However, commercial enzymes are expensive in part due to the high cost of the nutrient medium for the biomass culture. Activated sludge (AS) is a waste product of biological wastewater treatment and consists of microbial biomass that degrades organic matter by producing substantial quantities of hydrolytic enzymes. Recovering enzymes from AS therefore offers a potential alternative to conventional production techniques. A carrier-free, cross-linked enzyme aggregate (CLEA) was produced from

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Rinaldo, Serena, Giorgio Giardina, Nicoletta Castiglione, Valentina Stelitano, and Francesca Cutruzzolà. "The catalytic mechanism of Pseudomonas aeruginosa cd1 nitrite reductase." Biochemical Society Transactions 39, no. 1 (2011): 195–200. http://dx.doi.org/10.1042/bst0390195.

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The cd1 NiRs (nitrite reductases) are enzymes catalysing the reduction of nitrite to NO (nitric oxide) in the bacterial energy conversion denitrification process. These enzymes contain two distinct redox centres: one covalently bound c-haem, which is reduced by external electron donors, and another peculiar porphyrin, the d1-haem (3,8-dioxo-17-acrylate-porphyrindione), where nitrite is reduced to NO. In the present paper, we summarize the most recent results on the mechanism of nitrite reduction by the cd1 NiR from Pseudomonas aeruginosa. We discuss the essential catalytic features of this enz

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R, Kumaravelrajan, Swetha M та Suba V. "Characterization of Immobilized β-Amylase Enzyme Isolated from Sweet Potato and prepared by Entrapment Method". International Journal of Pharmaceutical Sciences and Nanotechnology(IJPSN) 15, № 6 (2022): 6196–203. http://dx.doi.org/10.37285/ijpsn.2022.15.6.2.

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Aim: This study attempted to isolate β-amylase from sweet potato and enzyme immobilized by encapsulation method, and characterized with various parameters.  Methods: The enzyme β-amylase was isolated with phosphate-buffered saline and purified by centrifugation with ammonium sulfate. The purified enzyme was immobilized on chitosan (0.25 g) and sodium alginate (0.25 g) polymers by entrapment method in the presence of calcium chloride (0.5 M). The immobilized enzyme was characterized by a starch hydrolysis test, the optimal pH and temperature were studied and the stability of the immobiliz

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Yang, Seung O., Joseph P. Talley, Gregory H. Nielsen, Kristen M. Wilding, and Bradley C. Bundy. "Streamlined Production, Protection, and Purification of Enzyme Biocatalysts Using Virus-like Particles and a Cell-Free Protein Synthesis System." SynBio 3, no. 1 (2025): 5. https://doi.org/10.3390/synbio3010005.

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Enzymes play an essential role in many different industries; however, their operating conditions are limited due to the loss of enzyme activity in the presence of proteases and at temperatures significantly above physiological conditions. One way to improve the stability of these enzymes against high temperatures and proteases is to encapsulate them in protective shells or virus-like particles. This work presents a streamlined, three-step, cell-free protein synthesis (CFPS) procedure that enables rapid in vitro enzyme production, targeted encapsulation in protective virus-like particles (VLPs)

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Galperin, Michael Y., D. Roland Walker, and Eugene V. Koonin. "Analogous Enzymes: Independent Inventions in Enzyme Evolution." Genome Research 8, no. 8 (1998): 779–90. http://dx.doi.org/10.1101/gr.8.8.779.

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Lieberman, Jack. "Enzymes in Sarcoidosis: Angiotensin-Converting-Enzyme (ACE)." Clinics in Laboratory Medicine 9, no. 4 (1989): 745–56. http://dx.doi.org/10.1016/s0272-2712(18)30602-4.

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Maeda, Masako. "New label enzymes for bioluminescent enzyme immunoassay." Journal of Pharmaceutical and Biomedical Analysis 30, no. 6 (2003): 1725–34. http://dx.doi.org/10.1016/s0731-7085(02)00514-9.

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Sree Kumar, K., Yashesh N. Vaishnav, and Joseph F. Weiss. "Radioprotection by antioxidant enzymes and enzyme mimetics." Pharmacology & Therapeutics 39, no. 1-3 (1988): 301–9. http://dx.doi.org/10.1016/0163-7258(88)90076-9.

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Mebs, D., S. Mieseler, U. Rimpau, C. Vossius, B. König, and S. Benesch. "Enzymes and enzyme inhibitors from marine sponges." Toxicon 33, no. 3 (1995): 304. http://dx.doi.org/10.1016/0041-0101(95)99364-9.

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Jovov, B., N. K. Wills, P. J. Donaldson, and S. A. Lewis. "Vectorial secretion of a kallikrein-like enzyme by cultured renal cells. I. General properties." American Journal of Physiology-Cell Physiology 259, no. 6 (1990): C869—C882. http://dx.doi.org/10.1152/ajpcell.1990.259.6.c869.

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Urinary kallikreins are proteolytic enzymes known to be secreted by distal nephron tubules. In this study, we demonstrate (using the chromogenic tripeptide substrate S 2266) that the renal cell line A6 from Xenopus laevis secretes a kallikrein-like enzyme. Secretion is present only when the cells are grown on filters, and enzyme is secreted only into the apical membrane bathing solution. Enzyme secretion consists of two components, one soybean trypsin inhibitor (SBTI) sensitive (SSBTI) and the other insensitive to SBTI (ISBTI). Both enzymes were inhibited by aprotinin, a kallikrein-like enzyme

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Almulaiky, Yaaser Q., J. Alkabli та Reda M. El-Shishtawy. "Sustainable Immobilization of β-Glucosidase onto Silver Ions and AgNPs-Loaded Acrylic Fabric with Enhanced Stability and Reusability". Polymers 15, № 22 (2023): 4361. http://dx.doi.org/10.3390/polym15224361.

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Modified polymer design has attracted significant attention for enzyme immobilization, offering promising applications. In this study, amine-terminated polymers were synthesized by incorporating functional groups into polyacrylonitrile using hexamethylenediamine. This work highlights the successful enzyme immobilization strategy using modified polymers, offering improved stability and expanded operational conditions for potential biotechnological applications. The resulting amino groups were utilized to capture silver ions, which were subsequently converted to silver nanoparticles (AgNPs). The

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Gupta, Supriya, Aiman Tanveer, Shruti Dwivedi, Kanchan Yadav, Vivek Kumar Morya, and Dinesh Yadav. "Isolation and Characterization of Aeromonas taiwanensis Strain for Simultaneous Production of Cellulase, Amylase, Pectinase, and Protease Enzymes." Biosciences Biotechnology Research Asia 21, no. 2 (2024): 655–70. http://dx.doi.org/10.13005/bbra/3254.

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ABSTRACT: A study was conducted to discover a novel microorganism capable of producing multiple enzymes with industrial applications. Bacterial isolates were screened from a soil sample collected from a wood-decaying area, and their ability to produce various enzymes of industrial significance was evaluated. Among the 100 screened bacterial isolates, the strain GCEL-BGb85 was identified as Aeromonas taiwanensis through 16s RNA sequencing. Further screening revealed that this microorganism could produce cellulase, pectinase, protease, and amylase enzymes. The strain was set up for enzyme produc

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Suresh, Harsha Garadi, Aline Xavier da Silveira dos Santos, Wanda Kukulski, et al. "Prolonged starvation drives reversible sequestration of lipid biosynthetic enzymes and organelle reorganization in Saccharomyces cerevisiae." Molecular Biology of the Cell 26, no. 9 (2015): 1601–15. http://dx.doi.org/10.1091/mbc.e14-11-1559.

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Cells adapt to changing nutrient availability by modulating a variety of processes, including the spatial sequestration of enzymes, the physiological significance of which remains controversial. These enzyme deposits are claimed to represent aggregates of misfolded proteins, protein storage, or complexes with superior enzymatic activity. We monitored spatial distribution of lipid biosynthetic enzymes upon glucose depletion in Saccharomyces cerevisiae. Several different cytosolic-, endoplasmic reticulum–, and mitochondria-localized lipid biosynthetic enzymes sequester into distinct foci. Using

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Ainscough, R. J., J. M. McGree, M. J. Callaghan, and R. E. Speight. "Effective incorporation of xylanase and phytase in lick blocks for grazing livestock." Animal Production Science 59, no. 9 (2019): 1762. http://dx.doi.org/10.1071/an18424.

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The addition of feed enzymes to livestock diets has contributed to significant increases in productivity over recent decades. The use of enzymes has been the most common in systems where enzyme delivery and diets can be easily managed, such as for poultry and pigs. Lick blocks supplement the forage diets of ruminants with nitrogen and minerals but not enzymes, due in part to concerns that block manufacturing temperatures would lead to unacceptable levels of enzyme degradation. The nutritional value of low quality pasture could be improved using enzyme supplemented lick blocks if enzymes remain

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Demain, Arnold L., and Sergio Sánchez. "Enzymes of industrial interest." Mexican journal of biotechnology 2, no. 2 (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.

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SAITO, AKINOBU, and RYO HONDO. "Genome Variation among Listeria monocytogenes Isolates Derived from Epidemiologically Related Raw Milk and Other Strains." Journal of Food Protection 59, no. 9 (1996): 998–1002. http://dx.doi.org/10.4315/0362-028x-59.9.998.

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Listeria monocytogenes strains were examined by restriction-enzyme analysis of chromosomal DNA using a total of 18 restriction enzymes. Ten of the 6-base restriction enzymes and one 8-base restriction enzyme produced distinguishable fragments among these strains. Six strains (serotype 1/2a) recovered from raw milk suspected of the same contaminant were compared with seven epidemiologically unrelated strains (serotype 1/2a) using 10 of the 6-base restriction enzymes. The restriction enzyme patterns of the six raw milk isolates were identical to each other, but differed from those of the other s

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