Journal articles: 'Microbial enzymes'

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Liu, Chunhui, Jingyi Ma, Tingting Qu, Zhijing Xue, Xiaoyun Li, Qin Chen, Ning Wang, Zhengchao Zhou, and Shaoshan An. "Extracellular Enzyme Activity and Stoichiometry Reveal Nutrient Dynamics during Microbially-Mediated Plant Residue Transformation." Forests 14, no. 1 (December 24, 2022): 34. http://dx.doi.org/10.3390/f14010034.

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Extracellular enzymes are the major mediators of plant residue and organic matter decomposition in soil, frequently associated with microbial metabolic processes and the biochemical cycling of nutrients in soil ecosystems. However, the dynamic trends and driving factors of extracellular enzymes and their stoichiometry during plant residue transformation remain to be further studied. Here, we investigated the dynamics of extracellular enzymes and enzymatic stoichiometry in the “litter-soil” transformation interface soil (TIS) layer, an essential occurrence layer for microbially-mediated C transformation. The results indicated an unbalanced relationship between substrate resource supply and microbial metabolic demand. Microbial metabolism was limited by C (C/N-acquiring enzymes > 1) and P (N/P-acquiring enzymes < 1) throughout the observed stages of plant residue transformation. The initially higher extracellular enzyme activity reflected the availability of the active components (dissolved carbon (DC), nitrogen (DN), microbial biomass carbon (MBC), nitrogen (MBN), and phosphorus (MBP)) in the substrate and the higher intensity of microbial metabolism. With the transformation of plant residues, the active fraction ceased to be the predominant microbial C source, forcing the secretion of C-acquiring enzymes and N-acquiring enzymes to obtain C sources and N nutrients from refractory substrates. Moreover, C/N-acquiring enzymes decreased, while C/P-acquiring enzymes and N/P-acquiring enzymes subsequently increased, which suggested that the microbial demand for N gradually increased and for P relatively decreased. Soil microorganisms can be forced into dormancy or intracellular mineralization due to the lack of substrate resources, so microbial biomass and extracellular enzyme activities decreased significantly compared to initial values. In summary, the results indicated that soil nutrients indirectly contribute to extracellular enzymes and their stoichiometry by affecting microbial activities. Furthermore, extracellular enzymes and their stoichiometry were more sensitive to the response of soil microbial biomass carbon.

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Wackett, Lawrence P. "Microbial industrial enzymes." Microbial Biotechnology 12, no. 2 (February 25, 2019): 405–6. http://dx.doi.org/10.1111/1751-7915.13389.

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Wackett, Lawrence P. "Microbial industrial enzymes." Microbial Biotechnology 12, no. 5 (August 5, 2019): 1090–91. http://dx.doi.org/10.1111/1751-7915.13469.

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Wackett, Lawrence P. "Microbial commercial enzymes." Microbial Biotechnology 4, no. 4 (July 2011): 548–49. http://dx.doi.org/10.1111/j.1751-7915.2011.00274.x.

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Sihi, Debjani, Stefan Gerber, Patrick W. Inglett, and Kanika Sharma Inglett. "Comparing models of microbial–substrate interactions and their response to warming." Biogeosciences 13, no. 6 (March 21, 2016): 1733–52. http://dx.doi.org/10.5194/bg-13-1733-2016.

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Abstract. Recent developments in modelling soil organic carbon decomposition include the explicit incorporation of enzyme and microbial dynamics. A characteristic of these models is a positive feedback between substrate and consumers, which is absent in traditional first-order decay models. With sufficiently large substrate, this feedback allows an unconstrained growth of microbial biomass. We explore mechanisms that curb unrestricted microbial growth by including finite potential sites where enzymes can bind and by allowing microbial scavenging for enzymes. We further developed a model where enzyme synthesis is not scaled to microbial biomass but associated with a respiratory cost and microbial population adjusts enzyme production in order to optimise their growth. We then tested short- and long-term responses of these models to a step increase in temperature and find that these models differ in the long-term when short-term responses are harmonised. We show that several mechanisms, including substrate limitation, variable production of microbial enzymes, and microbes feeding on extracellular enzymes eliminate oscillations arising from a positive feedback between microbial biomass and depolymerisation. The model where enzyme production is optimised to yield maximum microbial growth shows the strongest reduction in soil organic carbon in response to warming, and the trajectory of soil carbon largely follows that of a first-order decomposition model. Modifications to separate growth and maintenance respiration generally yield short-term differences, but results converge over time because microbial biomass approaches a quasi-equilibrium with the new conditions of carbon supply and temperature.

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Baldrian, P. "Microbial enzyme-catalyzed processes in soils and their analysis." Plant, Soil and Environment 55, No. 9 (October 14, 2009): 370–78. http://dx.doi.org/10.17221/134/2009-pse.

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Currently, measuring enzyme activities in soils or other lignocellulose-based materials is technically feasible; this measurement is particularly suitable for evaluating soil processes of biopolymer (cellulose, hemicelluloses, lignin, chitin and others) degradation by microbes and for assessing cycling and mobilization of principal nutrients including nitrogen, phosphorus and sulfur. With some considerations, assay methods can provide reliable information on the concentration of enzymes in soil or the rates of enzyme-catalyzed processes. Enzyme analyses in recent studies demonstrated a high level of spatial variability of soil enzyme activity both in depth and in space. The vertical gradients of enzyme activities are most developed in forest soils. Furthermore, enzyme activity in soils is regulated by seasonally-dependent variables such as temperature, moisture and the input of fresh litter. While several enzymes are widely produced by different groups of soil microorganisms, some of them can be used as indicators of the presence or activity of specific microbial taxa.

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Singh, Ankita, PalakVarma .., Arpita Singh, Shuchi .., Anakshi .., Neha Sharma, Kajal Rawat, et al. "Applications of Microbial Enzymes: The Need of an Hour." Indian Journal of Genetics and Molecular Research 12, no. 2 (December 15, 2023): 19–32. http://dx.doi.org/10.21088/ijgmr.2319.4782.12223.3.

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A growing need for sustainable solutions is one of the primary drivers of the demand for industrial enzymes. One of the most significant and beneficial sources of many enzymes has been and still is the microbial world. Numerous industrial procedures, such as chemical synthesis used to create chemicals and pharmaceuticals, have a number of drawbacks: Lack of enantiomeric specificity for chiral synthesis, low pH, high pressure, high temperature, and low catalytic efficiency. Enzyme research and interest are still advancing, which helps industrial biocatalysis succeed even more. There should be a lot of intriguing discoveries in the field of biotransformation over the coming years. The value of biotechnologically and industrially significant microbial enzymes is the main topic of this study, which comprises 44 papers, including research studies and review articles. Also, it offers novel insights into the micro-organisms that manufacture these enzymes as well as the procedures employed for their purification and separation.

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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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Wackett, Lawrence P. "Broad specificity microbial enzymes." Microbial Biotechnology 8, no. 1 (January 2015): 188–89. http://dx.doi.org/10.1111/1751-7915.12270.

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Wackett, Lawrence P. "Immobilization of microbial enzymes." Microbial Biotechnology 3, no. 6 (October 22, 2010): 729–30. http://dx.doi.org/10.1111/j.1751-7915.2010.00227.x.

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Mullen, W. H., and P. M. Vadgama. "Microbial enzymes in biosensors." Journal of Applied Bacteriology 61, no. 3 (September 1986): 181–93. http://dx.doi.org/10.1111/j.1365-2672.1986.tb04275.x.

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Staerck, Cindy, Amandine Gastebois, Patrick Vandeputte, Alphonse Calenda, Gérald Larcher, Louiza Gillmann, Nicolas Papon, Jean-Philippe Bouchara, and Maxime J. J. Fleury. "Microbial antioxidant defense enzymes." Microbial Pathogenesis 110 (September 2017): 56–65. http://dx.doi.org/10.1016/j.micpath.2017.06.015.

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Wackett, Lawrence P. "Evolution of microbial enzymes." Environmental Microbiology 9, no. 11 (November 2007): 2903–4. http://dx.doi.org/10.1111/j.1462-2920.2007.01463.x.

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Wackett, Lawrence P. "Microbial enzymes as sensors." Environmental Microbiology 11, no. 1 (January 2009): 277–78. http://dx.doi.org/10.1111/j.1462-2920.2008.01832.x.

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Lynd, Lee R., Paul J. Weimer, Willem H. van Zyl, and Isak S. Pretorius. "Microbial Cellulose Utilization: Fundamentals and Biotechnology." Microbiology and Molecular Biology Reviews 66, no. 3 (September 2002): 506–77. http://dx.doi.org/10.1128/mmbr.66.3.506-577.2002.

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SUMMARY Fundamental features of microbial cellulose utilization are examined at successively higher levels of aggregation encompassing the structure and composition of cellulosic biomass, taxonomic diversity, cellulase enzyme systems, molecular biology of cellulase enzymes, physiology of cellulolytic microorganisms, ecological aspects of cellulase-degrading communities, and rate-limiting factors in nature. The methodological basis for studying microbial cellulose utilization is considered relative to quantification of cells and enzymes in the presence of solid substrates as well as apparatus and analysis for cellulose-grown continuous cultures. Quantitative description of cellulose hydrolysis is addressed with respect to adsorption of cellulase enzymes, rates of enzymatic hydrolysis, bioenergetics of microbial cellulose utilization, kinetics of microbial cellulose utilization, and contrasting features compared to soluble substrate kinetics. A biological perspective on processing cellulosic biomass is presented, including features of pretreated substrates and alternative process configurations. Organism development is considered for “consolidated bioprocessing” (CBP), in which the production of cellulolytic enzymes, hydrolysis of biomass, and fermentation of resulting sugars to desired products occur in one step. Two organism development strategies for CBP are examined: (i) improve product yield and tolerance in microorganisms able to utilize cellulose, or (ii) express a heterologous system for cellulose hydrolysis and utilization in microorganisms that exhibit high product yield and tolerance. A concluding discussion identifies unresolved issues pertaining to microbial cellulose utilization, suggests approaches by which such issues might be resolved, and contrasts a microbially oriented cellulose hydrolysis paradigm to the more conventional enzymatically oriented paradigm in both fundamental and applied contexts.

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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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Zhang, Yuanye, Xia Wang, Yuxin Sun, Jinhong Wu, Tao Deng, Menghan Yuan, Wenhui Duan, and Yunfei Zhao. "Hydrolases Control Soil Carbon Sequestration in Alpine Grasslands in the Tibetan Plateau." Sustainability 16, no. 9 (April 23, 2024): 3508. http://dx.doi.org/10.3390/su16093508.

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Microbial-sourced carbon is an important component of soil organic carbon (SOC) and influences SOC’s size and turnover. Soil extracellular enzymes can participate in the degradation of plants in the soil to produce substances needed by microorganisms, which in turn affects microbial sources of carbon. Most of the current studies focus on the effects of soil extracellular enzymes on SOC pools, while there is a lack of clarity regarding the effects on microbial sources of carbon during SOC pool formation. In this paper, three typical grassland types (alpine meadow, alpine grassland, and desert grassland, respectively) on the Tibetan Plateau were selected as research objects to investigate the effects of grassland type and soil depth on microbial-sourced carbon (amino sugars) and soil extracellular enzymes (hydrolytic enzymes: β-glucosidase and cellulase; oxidative enzymes: peroxidase and polyphenol oxidase) in the soil profiles. Our study shows that the content of amino sugars in the three grassland types followed the order: alpine meadow > alpine grassland > desert grassland; the content of hydrolytic enzyme followed the order of alpine meadow > alpine grassland > desert grassland; the content of oxidative enzyme followed the order of desert grassland > alpine grassland > alpine meadow; amino sugars content showed a positive correlation with hydrolytic enzymes and a negative correlation with oxidative enzymes; and the hydrolytic enzyme was the main factor promoting the accumulation of amino sugars. The environmental conditions of alpine meadows and alpine grasslands are more favorable for the formation of microbial-derived carbon and have greater sequestration potential, while desert grasslands are not favorable for the formation of microbial-derived carbon. The results of this study provide a reference basis for exploring the model of organic carbon sequestration in the Tibetan Plateau.

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Cosme, Fernanda, António Inês, and Alice Vilela. "Microbial and Commercial Enzymes Applied in the Beverage Production Process." Fermentation 9, no. 4 (April 17, 2023): 385. http://dx.doi.org/10.3390/fermentation9040385.

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Enzymes are highly effective biocatalysts used in various industrial processes, playing a key role in winemaking and in other fermented beverages. Many of the enzymes used in fermentation processes have their origin in fruits, in the indigenous microbiota of the fruit, and in the microorganisms present during beverage processing. Besides naturally occurring enzymes, commercial preparations that usually blend different activities are used (glucosidases, glucanases, pectinases, and proteases, among others). Over the years, remarkable progress has been made in enhancing enzyme performance under operating conditions. The winemaking industry has observed a significant improvement in production levels, stimulating the introduction of technological innovations that aim to enhance efficiency and wine quality. Enzymes have traditionally been used in the beverage industry; however, others have been introduced more recently, with numerous studies aimed at optimizing their performance under processing conditions, including the use of immobilized enzymes. Therefore, one major goal of the current review is to give a detailed overview of the endogenous enzyme potential of wine microorganisms, as well as of enzymes obtained from grapes or even commercial preparations, studied and already in use in the beverage industry, and to present the future trends in enzyme production and application.

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Wu, Junyang, Zhongwei Wu, Evgenios Agathokleous, Yongli Zhu, Diwu Fan, and Jiangang Han. "Unveiling a New Perspective on Cadmium-Induced Hormesis in Soil Enzyme Activity: The Relative Importance of Enzymatic Reaction Kinetics and Microbial Communities." Agriculture 14, no. 6 (June 7, 2024): 904. http://dx.doi.org/10.3390/agriculture14060904.

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Hormesis in soil enzymes is well-established, yet the underlying mechanism remains elusive. In this novel study, we investigated the effects of low-dose Cd exposure (0, 0.03, 0.3, 3, and 30 mg·kg−1) in farmland soil within a typical constructed wetland environment. We assessed the activities of four soil enzymes (urease (URE), denitrification enzyme (DEA), dehydrogenase (DHA), and alkaline phosphatase (ALP)) at varying exposure durations (0 h, 24 h, and 48 h), evaluating hormetic characteristics across these time intervals. Additionally, we determined kinetic parameters, specifically the Michaelis constant (Km) and maximum reaction velocity (Vmax), for these enzymes while examining potential alterations in microbial community structure. Our findings revealed hormesis in all four soil enzymes at 24 h of exposure, with varying stimulus width and maximum hormesis rates. Interestingly, heavy metals did not significantly influence the diversity of soil microbial communities, but they did inhibit the ability of soil microbial communities to secrete extracellular enzymes. This resulted in a reduction in the soil enzyme pool and a consequential shift in overall soil enzyme activities. The conclusion of this study is that low-dose Cd primarily reduced extracellular enzyme secretion by soil microorganisms, leading to a reduction in the size of the soil enzyme pool and thereby inducing hormesis in soil enzyme activities.

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Zbar, Nedhaal Suhail. "Microbial enzymes: the role of enzyme in cancer therapy." International Journal of Research in Engineering and Innovation 06, no. 02 (2022): 104–16. http://dx.doi.org/10.36037/ijrei.2021.6204.

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One of the most important challenges of the 21st decade is cancer. Adequate therapy advances aren't meeting the growing quantity of sufferers. Therapies that are frequently utilized doesn't always achieve the expected outcomes. As a consequence, it's vital to take action. Identify innovative supplementary appropriate therapies. Immunology involves the utilization of certain kinds of microorganisms. It is perhaps of their most essential potentially fruitful pathway that, in some way, therapy is thought to increase intestinal response, allowing cancerous lymphocytes to be removed preferentially. These study results seem encouraging, proving that microbial activation creates a strong reaction engagement in the innate immunological responses. Also, microbes may be used for various methods depending on their special qualities, such as pathogenicity, anaerobic living, and binding compounds that may be transported to a particular region. This publication gives an analysis of a chosen listing of indigenous microorganisms, including their characterization, genetic encoding, enzymes associated with proteins, mechanisms, or action towards cancer. Things are still in the testing stage. The use of microorganisms for chemotherapy, unlike every medical treatment, has inherent drawbacks. Biotechnology makes use of a large variety of enzymes that are commercially manufactured using specially screening microbes. Several microbes have been studied, developed, or optimized to create large enzymatic preparations for commercial production. Because diverse businesses need enzymes for diverse objectives, microbiological enzymes have been researched for their unique properties that may be used in a variety of bioreactors.

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Maier, Robert, and Stéphane Benoit. "Role of Nickel in Microbial Pathogenesis." Inorganics 7, no. 7 (June 26, 2019): 80. http://dx.doi.org/10.3390/inorganics7070080.

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Nickel is an essential cofactor for some pathogen virulence factors. Due to its low availability in hosts, pathogens must efficiently transport the metal and then balance its ready intracellular availability for enzyme maturation with metal toxicity concerns. The most notable virulence-associated components are the Ni-enzymes hydrogenase and urease. Both enzymes, along with their associated nickel transporters, storage reservoirs, and maturation enzymes have been best-studied in the gastric pathogen Helicobacter pylori, a bacterium which depends heavily on nickel. Molecular hydrogen utilization is associated with efficient host colonization by the Helicobacters, which include both gastric and liver pathogens. Translocation of a H. pylori carcinogenic toxin into host epithelial cells is powered by H2 use. The multiple [NiFe] hydrogenases of Salmonella enterica Typhimurium are important in host colonization, while ureases play important roles in both prokaryotic (Proteus mirabilis and Staphylococcus spp.) and eukaryotic (Cryptoccoccus genus) pathogens associated with urinary tract infections. Other Ni-requiring enzymes, such as Ni-acireductone dioxygenase (ARD), Ni-superoxide dismutase (SOD), and Ni-glyoxalase I (GloI) play important metabolic or detoxifying roles in other pathogens. Nickel-requiring enzymes are likely important for virulence of at least 40 prokaryotic and nine eukaryotic pathogenic species, as described herein. The potential for pathogenic roles of many new Ni-binding components exists, based on recent experimental data and on the key roles that Ni enzymes play in a diverse array of pathogens.

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Drake, J. E., B. A. Darby, M. A. Giasson, M. A. Kramer, R. P. Phillips, and A. C. Finzi. "Stoichiometry constrains microbial response to root exudation – insights from a model and a field experiment in a temperate forest." Biogeosciences Discussions 9, no. 6 (June 13, 2012): 6899–945. http://dx.doi.org/10.5194/bgd-9-6899-2012.

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Abstract. Healthy plant roots release a wide range of chemicals into soils. This process, termed root exudation, is thought to increase the activity of microbes and the exo-enzymes they synthesize, leading to accelerated rates of carbon (C) mineralization and nutrient cycling in rhizosphere soils relative to bulk soils. The causal role of exudation, however, is difficult to isolate with in-situ observations, given the complex nature of the rhizosphere environment. We investigated the potential effects of root exudation on microbial and exo-enzyme activity using a theoretical model of decomposition and a field experiment, with a specific focus on the stoichiometric constraint of nitrogen (N) availability. The field experiment isolated the effect of exudation by pumping solutions of exudate mimics through microlysimeter "root simulators" into intact forest soils over two 50-day periods. Using a combined model-experiment approach, we tested two hypotheses: (1) exudation alone is sufficient to stimulate microbial and exo-enzyme activity in rhizosphere soils, and (2) microbial response to C-exudates (carbohydrates and organic acids) is constrained by N-limitation. Experimental delivery of exudate mimics containing C and N significantly increased microbial respiration, microbial biomass, and the activity of exo-enzymes that decompose labile components of soil organic matter (SOM, e.g., cellulose, amino sugars), while decreasing the activity of exo-enzymes that degrade recalcitrant SOM (e.g., polyphenols, lignin). However, delivery of C-only exudates had no effect on microbial biomass or overall exo-enzyme activity, and only increased microbial respiration. The theoretical decomposition model produced complementary results; the modeled microbial response to C-only exudates was constrained by limited N supply to support the synthesis of N-rich microbial biomass and exo-enzymes, while exuding C and N together elicited an increase in modeled microbial biomass, exo-enzyme activity, and decomposition. Thus, hypothesis (2) was supported, while hypothesis (1) was only supported when C and N compounds were exuded together. This study supports a cause-and-effect relationship between root exudation and enhanced microbial activity, and suggests that exudate stoichiometry is an important and underappreciated driver of microbial activity in rhizosphere soils.

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Wani, A. K., F. Rahayu, F. T. Kadarwati, C. Suhara, R. Singh, D. S. Dhanjal, N. Akhtar, T. G. Mir, and C. Chopra. "Metagenomic screening strategies for bioprospecting enzymes from environmental samples." IOP Conference Series: Earth and Environmental Science 974, no. 1 (January 1, 2022): 012003. http://dx.doi.org/10.1088/1755-1315/974/1/012003.

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Abstract Globally, there is a growing demand for biocatalysts because of the associated efficacy and efficiency. The applications of enzymes in food, paper, pulp, textile, and chemical industries have prompted enzyme exploration. Microbes, being the natural reservoirs of enzymes, have gained researchers’ attention, and the quest for microbial enzymes has increased in past years. This review provides insights about metagenomics techniques and their applicability in obtaining microbial-origin enzymes from diverse environmental samples besides highlighting their importance. The metagenomic approach has emerged as a promising way towards replacing conventional microbial techniques with culture-independent methods involving direct isolation of DNA environmental samples. There are two primary methodologies, i.e., functional-based and sequence-based, to identify and characterize industrially valuable biocatalysts from the environmental microcosms. Many of the obtained enzymes are successfully used in diverse food, cosmetics, and pharmaceutical industries. However, there are some complications associated with it that can be minimized only by further investigations. The paper focuses on the advancement of metagenomics for bioprospecting to stress on its significance in microbial characterization and exploration. This will also ensure the in-depth analysis of several unexplored and unknown microbial communities and/or members from complex niches.

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Sihi, D., S. Gerber, P. W. Inglett, and K. S. Inglett. "Comparing models of microbial-substrate interactions and their response to warming." Biogeosciences Discussions 12, no. 13 (July 10, 2015): 10857–97. http://dx.doi.org/10.5194/bgd-12-10857-2015.

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Abstract. Recent developments in modelling soil organic carbon decomposition include the explicit incorporation of enzyme and microbial dynamics. A characteristic of these models is a positive feedback between substrate and consumers which is absent in traditional first order decay models. Under sufficient large substrate, this new feedback allows an unconstrained growth of microbial biomass. A second phenomenon incorporated in the microbial decomposition models is decreased carbon use efficiency (CUE) with increasing temperature. Here, first we analyse microbial decomposition models by parameterising changes in CUE based on the differentiation between growth and maintenance respiration. We then explore mechanisms that curb unrestricted microbial growth by including finite potential sites where enzymes can bind and by allowing microbial scavenging for enzymes. Finally, we propose a model where enzyme synthesis is associated with a respiratory cost and microbial population adjusts enzyme production in order to optimise their growth. When applying a step increase in temperature, we find fast responses that reflect adjustments to enzyme dynamics and maintenance respiration, a short-term adjustment in microbial growth, and the long-term change in carbon storage. We find that mechanisms that prevent unrestricted microbial growth lead to a similar response to warming as traditional first order decomposition models.

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Niyongabo Niyonzima, Francois. "Production of Microbial Industrial Enzymes." Acta Scientific Microbiology 2, no. 12 (November 11, 2019): 75–89. http://dx.doi.org/10.31080/asmi.2019.02.0434.

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Bhandari, Sobika, Darbin Kumar Poudel, Rishab Marahatha, Sonika Dawadi, Karan Khadayat, Sitaram Phuyal, Shreesti Shrestha, et al. "Microbial Enzymes Used in Bioremediation." Journal of Chemistry 2021 (February 8, 2021): 1–17. http://dx.doi.org/10.1155/2021/8849512.

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Emerging pollutants in nature are linked to various acute and chronic detriments in biotic components and subsequently deteriorate the ecosystem with serious hazards. Conventional methods for removing pollutants are not efficient; instead, they end up with the formation of secondary pollutants. Significant destructive impacts of pollutants are perinatal disorders, mortality, respiratory disorders, allergy, cancer, cardiovascular and mental disorders, and other harmful effects. The pollutant substrate can recognize different microbial enzymes at optimum conditions (temperature/pH/contact time/concentration) to efficiently transform them into other rather unharmful products. The most representative enzymes involved in bioremediation include cytochrome P450s, laccases, hydrolases, dehalogenases, dehydrogenases, proteases, and lipases, which have shown promising potential degradation of polymers, aromatic hydrocarbons, halogenated compounds, dyes, detergents, agrochemical compounds, etc. Such bioremediation is favored by various mechanisms such as oxidation, reduction, elimination, and ring-opening. The significant degradation of pollutants can be upgraded utilizing genetically engineered microorganisms that produce many recombinant enzymes through eco-friendly new technology. So far, few microbial enzymes have been exploited, and vast microbial diversity is still unexplored. This review would also be useful for further research to enhance the efficiency of degradation of xenobiotic pollutants, including agrochemical, microplastic, polyhalogenated compounds, and other hydrocarbons.

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Wackett, Lawrence P. "Chiral transformations by microbial enzymes." Microbial Biotechnology 1, no. 1 (December 12, 2007): 94–95. http://dx.doi.org/10.1111/j.1751-7915.2007.00019.x.

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Böttcher, Dominique, and Uwe T. Bornscheuer. "Protein engineering of microbial enzymes." Current Opinion in Microbiology 13, no. 3 (June 2010): 274–82. http://dx.doi.org/10.1016/j.mib.2010.01.010.

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Urlacher, V. B., S. Lutz-Wahl, and R. D. Schmid. "Microbial P450 enzymes in biotechnology." Applied Microbiology and Biotechnology 64, no. 3 (April 1, 2004): 317–25. http://dx.doi.org/10.1007/s00253-003-1514-1.

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Wackett, Lawrence P. "Microbial extracellular enzymes used industrially." Environmental Microbiology 16, no. 5 (April 22, 2014): 1452–53. http://dx.doi.org/10.1111/1462-2920.12473.

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TSURU, Daisuke. "Microbial Enzymes and Their Inhibitors." YAKUGAKU ZASSHI 113, no. 10 (1993): 683–97. http://dx.doi.org/10.1248/yakushi1947.113.10_683.

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Jayani, Ranveer Singh, Shivalika Saxena, and Reena Gupta. "Microbial pectinolytic enzymes: A review." Process Biochemistry 40, no. 9 (September 2005): 2931–44. http://dx.doi.org/10.1016/j.procbio.2005.03.026.

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Gari, Jiregna, and Rahma Abdella. "Degradation of zearalenone by microorganisms and enzymes." PeerJ 11 (August 14, 2023): e15808. http://dx.doi.org/10.7717/peerj.15808.

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Mycotoxins are toxic metabolites produced by fungi that may cause serious health problems in humans and animals. Zearalenone is a secondary metabolite produced by fungi of the genus Fusarium, widely exists in animal feed and human food. One concern with the use of microbial strains and their enzyme derivatives for zearalenone degradation is the potential variability in the effectiveness of the degradation process. The efficiency of degradation may depend on various factors such as the type and concentration of zearalenone, the properties of the microbial strains and enzymes, and the environmental conditions. Therefore, it is important to carefully evaluate the efficacy of these methods under different conditions and ensure their reproducibility. Another important consideration is the safety and potential side effects of using microbial strains and enzymes for zearalenone degradation. It is necessary to evaluate the potential risks associated with the use of genetically modified microorganisms or recombinant enzymes, including their potential impact on the environment and non-target organisms. Additionally, it is important to ensure that the degradation products are indeed harmless and do not pose any health risks to humans or animals. Furthermore, while the use of microbial strains and enzymes may offer an environmentally friendly and cost-effective solution for zearalenone degradation, it is important to explore other methods such as physical or chemical treatments as well. These methods may offer complementary approaches for zearalenone detoxification, and their combination with microbial or enzyme-based methods may improve overall efficacy. Overall, the research on the biodegradation of zearalenone using microorganisms and enzyme derivatives is promising, but there are important considerations that need to be addressed to ensure the safety and effectiveness of these methods. Development of recombinant enzymes improves enzymatic detoxification of zearalenone to a non-toxic product without damaging the nutritional content. This review summarizes biodegradation of zearalenone using microorganisms and enzyme derivatives to nontoxic products. Further research is needed to fully evaluate the potential of these methods for mitigating the impact of mycotoxins in food and feed.

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Subathra, Devi C., Naine S. Jemimah, Keziah S. Merlyn, and V. Mohanasrinivasan. "A brief review on conventional methods for screening, product development, downstream and evaluation of fibrinolytic enzymes from marine microbes." Research Journal of Chemistry and Environment 25, no. 7 (June 25, 2021): 194–201. http://dx.doi.org/10.25303/257rjce19421.

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The ocean is a great reservoir of biodiversity and microbial metabolites. Enzymes from marine source have recently gained considerable attention as they have lower side effects and more potency when compared to other existing sources. Fibrinolytic enzymes from microbial sources possess ability to dissolve clots and help to circumvent cardiovascular problems in more efficient and safer way. The complexity of the marine environment involves high salinity, high pressure, low temperature, special lighting conditions. This contributes to the significant differences between the enzymes generated by marine microorganisms and homologous enzymes from terrestrial microorganisms leading to the boosted marine microbial enzyme technology. Further, it is believed that sea water, which is saline in nature and chemically closer to the human blood plasma, could provide biomolecules, in particular enzymes that could have lower or no toxicity or side effects when used for therapeutic applications. However, only a small proportion of fibrinolytic enzymes from marine microbiota has been examined and an even smaller proportion has been exploited. Therefore, much work needs to be done intensively and extensively in terms of potent fibrinolytic enzymes from marine resources.

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Alves, Priscila Divina Diniz, Flávia de Faria Siqueira, Susanne Facchin, Carolina Campolina Rebello Horta, Júnia Maria Netto Victória, and Evanguedes Kalapothakis. "Survey of Microbial Enzymes in Soil, Water, and Plant Microenvironments." Open Microbiology Journal 8, no. 1 (April 4, 2014): 25–31. http://dx.doi.org/10.2174/1874285801408010025.

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Detection of microbial enzymes in natural environments is important to understand biochemical activities and to verify the biotechnological potential of the microorganisms. In the present report, 346 isolates from soil, water, and plants were screened for enzyme production (caseinase, gelatinase, amylase, carboxymethyl cellulase, and esterase). Our results showed that 89.6% of isolates produced at least one tested enzyme. A predominance of amylase in soil samples, carboxymethyl cellulase in plants, as well as esterase and gelatinase in water was observed. Interesting enzymatic profiles were found in some microenvironments, suggesting specificity of available nutrients and/or natural selection. This study revealed the potential of microorganisms present in water, soil, and plant to produce important enzymes for biotechnological exploration. A predominance of certain enzymes was found, depending on the type of environmental sample. The distribution of microbial enzymes in soil, water and plants has been little exploited in previous reports.

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Diwan, Deepti, Zeba Usmani, Minaxi Sharma, James W. Nelson, Vijay Kumar Thakur, Graham Christie, Gustavo Molina, and Vijai Kumar Gupta. "Thrombolytic Enzymes of Microbial Origin: A Review." International Journal of Molecular Sciences 22, no. 19 (September 28, 2021): 10468. http://dx.doi.org/10.3390/ijms221910468.

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Enzyme therapies are attracting significant attention as thrombolytic drugs during the current scenario owing to their great affinity, specificity, catalytic activity, and stability. Among various sources, the application of microbial-derived thrombolytic and fibrinolytic enzymes to prevent and treat vascular occlusion is promising due to their advantageous cost–benefit ratio and large-scale production. Thrombotic complications such as stroke, myocardial infarction, pulmonary embolism, deep venous thrombosis, and peripheral occlusive diseases resulting from blood vessel blockage are the major cause of poor prognosis and mortality. Given the ability of microbial thrombolytic enzymes to dissolve blood clots and prevent any adverse effects, their use as a potential thrombolytic therapy has attracted great interest. A better understanding of the hemostasis and fibrinolytic system may aid in improving the efficacy and safety of this treatment approach over classical thrombolytic agents. Here, we concisely discuss the physiological mechanism of thrombus formation, thrombo-, and fibrinolysis, thrombolytic and fibrinolytic agents isolated from bacteria, fungi, and algae along with their mode of action and the potential application of microbial enzymes in thrombosis therapy.

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Borzova, N. V. "MICROBIAL α-L-RHAMNOSIDASES: CLASSIFICATION, DISTRIBUTION, PROPERTIES AND PRACTICAL APPLICATION." Biotechnologia Acta 16, no. 4 (August 31, 2023): 5–21. http://dx.doi.org/10.15407/biotech16.04.005.

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One of the important problems of current biotechnology is the usage of enzymes of microbial origin for destruction of poorly soluble compounds and synthesis of new drugs. In recent years a great deal of researchers’ attention has been given to such technologically promising carbohydrases as O-glycosylhydrolases catalyzing the hydrolysis of O-glycoside links in glycosides, oligo- and polysaccharides, glycolipids, and other glycoconjugates. Aim. The review provides data on the position of α-L-rhamnosidases in the modern hierarchical classification of glycosidases and presents data available in the literature on the features of the enzyme structure in various microorganisms. Methods. The publications from the following databases were analyzed: PubMed (https://pubmed.nsbi.nlm.nih.gov/), the Carbohydrate-Active enZYmes (http://www.cazy.org/), the BRENDA Enzyme Database (https://www.brenda-enzymes.org/). Results. Data on the physicochemical, catalytic, and kinetic properties of α-L-rhamnosidases in microorganisms of different taxonomic groups have been systematized. The peculiarities of the substrate specificity of the enzyme depending on the nature of the protein and the growing conditions of the producer are characterized. Conclusions. Functional properties and specificity action of microbial α-L-rhamnosidases suggest their broad-range applicability for food and animal feed processing, as well as obtaining biologically active compounds for the pharmaceutical industry and medicine.

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Morgan, J. Alun W., and Roger W. Pickup. "Activity of microbial peptidases, oxidases, and esterases in lake waters of varying trophic status." Canadian Journal of Microbiology 39, no. 8 (August 1, 1993): 795–803. http://dx.doi.org/10.1139/m93-117.

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The range and activities of microbial enzymes present in lake water were assessed directly in cells concentrated by tangential flow filtration. A total of 108 enzymes were assayed in this study, which included tests for 60 peptidases, 20 oxidases, and 10 esterases, and 18 miscellaneous tests. In general, no trends in the range of enzymes were associated with trophic status of the lakes. However, one lake that was hypereutrophic had a greater range of enzymes than the other lakes tested. An increase in total enzyme activity (activity/mL) was recorded with an increase in trophic status of the water. The relationship between the physical and chemical attributes of each lake and microbial enzyme activities was investigated by principal component analysis. Quantitative changes between lakes in 11 of the 21 variables were shown to be closely related to changes in the enzyme activities of the lakes; total organic carbon, particulate carbon, particulate nitrogen, pH, and chlorophyll a showed the closest relationships.Key words: lake water, enzyme activity, trophic status.

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Sartaj, Km, Alok Patel, Leonidas Matsakas, and Ramasare Prasad. "Unravelling Metagenomics Approach for Microbial Biofuel Production." Genes 13, no. 11 (October 25, 2022): 1942. http://dx.doi.org/10.3390/genes13111942.

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Renewable biofuels, such as biodiesel, bioethanol, and biobutanol, serve as long-term solutions to fossil fuel depletion. A sustainable approach feedstock for their production is plant biomass, which is degraded to sugars with the aid of microbes-derived enzymes, followed by microbial conversion of those sugars to biofuels. Considering their global demand, additional efforts have been made for their large-scale production, which is ultimately leading breakthrough research in biomass energy. Metagenomics is a powerful tool allowing for functional gene analysis and new enzyme discovery. Thus, the present article summarizes the revolutionary advances of metagenomics in the biofuel industry and enlightens the importance of unexplored habitats for novel gene or enzyme mining. Moreover, it also accentuates metagenomics potentials to explore uncultivable microbiomes as well as enzymes associated with them.

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Latip, Wahhida, Victor Feizal Knight, Norhana Abdul Halim, Keat Khim Ong, Noor Azilah Mohd Kassim, Wan Md Zin Wan Yunus, Siti Aminah Mohd Noor, and Mohd Shukuri Mohamad Ali. "Microbial Phosphotriesterase: Structure, Function, and Biotechnological Applications." Catalysts 9, no. 8 (August 7, 2019): 671. http://dx.doi.org/10.3390/catal9080671.

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The role of phosphotriesterase as an enzyme which is able to hydrolyze organophosphate compounds cannot be disputed. Contamination by organophosphate (OP) compounds in the environment is alarming, and even more worrying is the toxicity of this compound, which affects the nervous system. Thus, it is important to find a safer way to detoxify, detect and recuperate from the toxicity effects of this compound. Phosphotriesterases (PTEs) are mostly isolated from soil bacteria and are classified as metalloenzymes or metal-dependent enzymes that contain bimetals at the active site. There are three separate pockets to accommodate the substrate into the active site of each PTE. This enzyme generally shows a high catalytic activity towards phosphotriesters. These microbial enzymes are robust and easy to manipulate. Currently, PTEs are widely studied for the detection, detoxification, and enzyme therapies for OP compound poisoning incidents. The discovery and understanding of PTEs would pave ways for greener approaches in biotechnological applications and to solve environmental issues relating to OP contamination.

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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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Shomar, Helena, and Gregory Bokinsky. "Towards a Synthetic Biology Toolset for Metallocluster Enzymes in Biosynthetic Pathways: What We Know and What We Need." Molecules 26, no. 22 (November 17, 2021): 6930. http://dx.doi.org/10.3390/molecules26226930.

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Microbes are routinely engineered to synthesize high-value chemicals from renewable materials through synthetic biology and metabolic engineering. Microbial biosynthesis often relies on expression of heterologous biosynthetic pathways, i.e., enzymes transplanted from foreign organisms. Metallocluster enzymes are one of the most ubiquitous family of enzymes involved in natural product biosynthesis and are of great biotechnological importance. However, the functional expression of recombinant metallocluster enzymes in live cells is often challenging and represents a major bottleneck. The activity of metallocluster enzymes requires essential supporting pathways, involved in protein maturation, electron supply, and/or enzyme stability. Proper function of these supporting pathways involves specific protein–protein interactions that remain poorly characterized and are often overlooked by traditional synthetic biology approaches. Consequently, engineering approaches that focus on enzymatic expression and carbon flux alone often overlook the particular needs of metallocluster enzymes. This review highlights the biotechnological relevance of metallocluster enzymes and discusses novel synthetic biology strategies to advance their industrial application, with a particular focus on iron-sulfur cluster enzymes. Strategies to enable functional heterologous expression and enhance recombinant metallocluster enzyme activity in industrial hosts include: (1) optimizing specific maturation pathways; (2) improving catalytic stability; and (3) enhancing electron transfer. In addition, we suggest future directions for developing microbial cell factories that rely on metallocluster enzyme catalysis.

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KUMARI, JYOTSNA, and CHETNA RAJAS. "OPTIMIZATION OF PHYSICAL PARAMETERS FOR PRODUCTION OF AMYLASES AND PROTEASES FROM SOIL BACTERIA." Asian Journal of Microbiology, Biotechnology & Environmental Sciences 25, no. 02 (2023): 232–36. http://dx.doi.org/10.53550/ajmbes.2023.v25i02.008.

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Enzymes are biomolecules present in the cells of living organisms in minute amounts and are capable of speeding up chemical reactions, without being altered and utilized in the reaction. Microbial enzymes are preferred than both plant and animal sources because they are cost effective with respect to production, more predictable, controllable and reliable. These naturally occurring enzymes are quite often not readily available in sufficient quantities for food applications or industrial use. However, by isolating microbial strains that produce the desired enzyme and optimizing the conditions for growth, commercial quantities can be obtained. Our study aimed at isolating and identifying the bacterial strains from soil which produce extracellular proteases and amylases and the optimization of physical conditions for maximum enzyme production.

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Gurung, Neelam, Sumanta Ray, Sutapa Bose, and Vivek Rai. "A Broader View: Microbial Enzymes and Their Relevance in Industries, Medicine, and Beyond." BioMed Research International 2013 (2013): 1–18. http://dx.doi.org/10.1155/2013/329121.

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Enzymes are the large biomolecules that are required for the numerous chemical interconversions that sustain life. They accelerate all the metabolic processes in the body and carry out a specific task. Enzymes are highly efficient, which can increase reaction rates by 100 million to 10 billion times faster than any normal chemical reaction. Due to development in recombinant technology and protein engineering, enzymes have evolved as an important molecule that has been widely used in different industrial and therapeutical purposes. Microbial enzymes are currently acquiring much attention with rapid development of enzyme technology. Microbial enzymes are preferred due to their economic feasibility, high yields, consistency, ease of product modification and optimization, regular supply due to absence of seasonal fluctuations, rapid growth of microbes on inexpensive media, stability, and greater catalytic activity. Microbial enzymes play a major role in the diagnosis, treatment, biochemical investigation, and monitoring of various dreaded diseases. Amylase and lipase are two very important enzymes that have been vastly studied and have great importance in different industries and therapeutic industry. In this review, an approach has been made to highlight the importance of different enzymes with special emphasis on amylase and lipase in the different industrial and medical fields.

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Elbanna, Khaled, Atheer Alshareef, Leena A. Neyaz, Mahmoud Z. El-Readi, and Hussein H. Abulreesh. "Microbial Uricase and its Unique Potential Applications." Advancements of Microbiology 63, no. 2 (June 1, 2024): 81–91. http://dx.doi.org/10.2478/am-2024-0007.

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Abstract The uricase enzyme yields allantoin, hydrogen peroxide, and carbon dioxide by catalyzing the oxidative opening of the purine ring in the urate pathway. This enzyme is important for biochemical diagnosis and reduces toxic urate accumulation during various diseases (hyperuricemia, gout, and bedwetting). Direct urate oxidase injection is recommended in renal complications-associated gout and to prevent chemotherapy-linked hyperuricemia disorders. Thus, uricase is a promising enzyme with diverse applications in medicine. Microbial production of uricase is featured by high growth rates, cost-effective bioprocessing, and easy optimization of the medium. Microbes produce the enzyme extracellular or intracellular. Extracellular uricase is preferred for biotechnological applications as it minimizes time, effort, and purification processes. This review provides insights into uricase-producing microbes, bacterial uric acid degradation pathways, degrading enzymes, and uricase-encoding genes. Furthermore, aspects influencing the microorganisms’ production of the uricase enzyme, its activity, and its purification procedure are also emphasized. Cell disruption is mandatory for intercellular uricase production, which elevates production costs. Therefore, extracellular uricase-producing microbial strains should be investigated, and production factors should be optimized. Future techniques for obtaining extracellular enzymes should feature reduced time and effort, as well as a simple purification methodology. Furthermore, uricase gene-carrying recombinant probiotic microorganisms could become an effective tool for gout treatment.

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Schauer, Roland, Ulf Sommer, Dorothea Krüger, Henrieke van Unen, and Christina Traving. "The Terminal Enzymes of Sialic Acid Metabolism: Acylneuraminate Pyruvate-Lyases." Bioscience Reports 19, no. 5 (October 1, 1999): 373–83. http://dx.doi.org/10.1023/a:1020256004616.

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The acylneuraminate pyruvate-lyase gene from Clostridium perfringens was sequenced and found to be most similar to the lyase gene from Haemophilus influenzae. Both the recombinant clostridial enzyme and the native enzyme from pig kidney were purified in larger amounts and characterized. The properties of the porcine lyase are similar to the microbial ones. However, the much higher degree of similarity in comparison to the microbial enzymes that was found between porcine lyase peptides and two putative mammalian lyase sequences show that the latter form an own group apart from the microbial lyases. Actual models of the acylneuraminate pyruvate-lyase reaction are discussed.

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Ai, Dongmei, Hongfei Pan, Xiaoxin Li, Min Wu, and Li C. Xia. "Association network analysis identifies enzymatic components of gut microbiota that significantly differ between colorectal cancer patients and healthy controls." PeerJ 7 (July 29, 2019): e7315. http://dx.doi.org/10.7717/peerj.7315.

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The human gut microbiota plays a major role in maintaining human health and was recently recognized as a promising target for disease prevention and treatment. Many diseases are traceable to microbiota dysbiosis, implicating altered gut microbial ecosystems, or, in many cases, disrupted microbial enzymes carrying out essential physio-biochemical reactions. Thus, the changes of essential microbial enzyme levels may predict human disorders. With the rapid development of high-throughput sequencing technologies, metagenomics analysis has emerged as an important method to explore the microbial communities in the human body, as well as their functionalities. In this study, we analyzed 156 gut metagenomics samples from patients with colorectal cancer (CRC) and adenoma, as well as that from healthy controls. We estimated the abundance of microbial enzymes using the HMP Unified Metabolic Analysis Network method and identified the differentially abundant enzymes between CRCs and controls. We constructed enzymatic association networks using the extended local similarity analysis algorithm. We identified CRC-associated enzymic changes by analyzing the topological features of the enzymatic association networks, including the clustering coefficient, the betweenness centrality, and the closeness centrality of network nodes. The network topology of enzymatic association network exhibited a difference between the healthy and the CRC environments. The ABC (ATP binding cassette) transporter and small subunit ribosomal protein S19 enzymes, had the highest clustering coefficient in the healthy enzymatic networks. In contrast, the Adenosylhomocysteinase enzyme had the highest clustering coefficient in the CRC enzymatic networks. These enzymic and metabolic differences may serve as risk predictors for CRCs and are worthy of further research.

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Hu, Zhiyuan, Jiating Li, Kangwei Shi, Guangqian Ren, Zhicong Dai, Jianfan Sun, Xiaojun Zheng, et al. "Effects of Canada Goldenrod Invasion on Soil Extracellular Enzyme Activities and Ecoenzymatic Stoichiometry." Sustainability 13, no. 7 (March 29, 2021): 3768. http://dx.doi.org/10.3390/su13073768.

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The rapid expansion of Canada goldenrod (Solidago canadensis L.) in China has drawn considerable attention as it may not only decrease vegetation diversity but also alter soil nutrient cycling in the affected ecosystems. Soil extracellular enzymes mediate nutrient cycling by catalyzing the organic matter decomposition; however, the mechanisms by which alien plant invasion may affect soil extracellular enzymes remain unclear. The objective of this study was to investigate the responses of soil extracellular enzyme activities and ecoenzymatic stoichiometry to S. canadensis invasion. Several extracellular enzymatic activities related to carbon, nitrogen, and phosphorus cycling were measured using a fluorometric method. Ecoenzymatic stoichiometry was used as a proxy of soil microbial metabolic limitations. S. canadensis invasion appeared to be associated with decreased activities of enzymes and with substantial conversions of microbial metabolic carbon and nitrogen limitations. The changes in the activities of extracellular enzymes and the limitations of microbial metabolism were correlated with the alterations in the nutrient availability and resource stoichiometry in the soil. These findings reveal that the alterations in soil available nutrients associated with S. canadensis invasion may regulate extracellular enzymatic activities and cause microbial metabolic limitations, suggesting that S. canadensis invasion considerably affects biogeochemical cycling processes.

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Cerdobbel, An, Erick J. Vandamme, and Wim Soetaert. "Towards a ‘tailor made’ biocatalysis." Microbiology Australia 29, no. 1 (2008): 38. http://dx.doi.org/10.1071/ma08038.

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Microbial enzymes are used today in the most diverse industrial sectors. However, it is only in recent years that fundamental knowledge has been acquired that allows for a rational ? rather than an empirical ? development and application of microbial enzyme processes. These enzymes are primarily used as an end product or a processing aid in the agricultural sector, food and feed industry, the detergent sector, the textile industry and health care sector. In these sectors they replace or adjust the familiar (bio)chemical processes, or plant or animal enzymes. But they can also perform totally new ?chemical? reactions, with the principal aim of ?improving? and/or modifying the ?substrate?.

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Jacobs, J. L., and A. B. McAllan. "Duodenal Nitrogenous Constituent Flow in Growing Steers Fed Silages Prepared with Formic Acid and Enzyme Additives." Proceedings of the British Society of Animal Production (1972) 1988 (March 1988): 146. http://dx.doi.org/10.1017/s0308229600017827.

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The addition to grass during ensiling of enzymes capable of hydrolysing forage polysaccharides has been shown to result in increased fermentation of dry matter within the silo (Jacobs & McAllan, 1987). Thus it appears that the enzymes promoted cellular breakdown within the silo. It is also possible that the enzymes may also have made available greater amounts of structural carbohydrate for utilisation within the rumen. Such an increase in available energy may be reflected in improved microbial activity in the rumen resulting in increased microbial protein synthesis. The present experiment examines the effects of enzyme treated silages on the flow of nitrogenous constituents at the duodenum of growing steers.

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Journal articles on the topic 'Microbial enzymes'

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