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Journal articles on the topic 'Microbial enzymes Biotechnology'

Author: Grafiati

Published: 11 December 2022

Last updated: 25 January 2023

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1

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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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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3

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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4

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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Pécs, Miklós, Martin Eggert, and Karl Schügerl. "Affinity precipitation of extracellular microbial enzymes." Journal of Biotechnology 21, no. 1-2 (November 1991): 137–42. http://dx.doi.org/10.1016/0168-1656(91)90266-x.

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6

Kotb, Essam. "Activity assessment of microbial fibrinolytic enzymes." Applied Microbiology and Biotechnology 97, no. 15 (June 29, 2013): 6647–65. http://dx.doi.org/10.1007/s00253-013-5052-1.

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7

Di Gennaro, Patrizia, Anna Bargna, and Guido Sello. "Microbial enzymes for aromatic compound hydroxylation." Applied Microbiology and Biotechnology 90, no. 6 (April 27, 2011): 1817–27. http://dx.doi.org/10.1007/s00253-011-3285-4.

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8

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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9

Xia, Wei, Kang Zhang, Lingqia Su, and Jing Wu. "Microbial starch debranching enzymes: Developments and applications." Biotechnology Advances 50 (September 2021): 107786. http://dx.doi.org/10.1016/j.biotechadv.2021.107786.

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10

Atomi, Haruyuki. "Microbial enzymes involved in carbon dioxide fixation." Journal of Bioscience and Bioengineering 94, no. 6 (December 2002): 497–505. http://dx.doi.org/10.1016/s1389-1723(02)80186-4.

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11

ATOMI, HARUYUKI. "Microbial Enzymes Involved in Carbon Dioxide Fixation." Journal of Bioscience and Bioengineering 94, no. 6 (2002): 497–505. http://dx.doi.org/10.1263/jbb.94.497.

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12

Girvan, Hazel M., and Andrew W. Munro. "Applications of microbial cytochrome P450 enzymes in biotechnology and synthetic biology." Current Opinion in Chemical Biology 31 (April 2016): 136–45. http://dx.doi.org/10.1016/j.cbpa.2016.02.018.

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13

Vachher, Meenakshi, Aparajita Sen, Rachna Kapila, and Arti Nigam. "Microbial therapeutic enzymes: A promising area of biopharmaceuticals." Current Research in Biotechnology 3 (2021): 195–208. http://dx.doi.org/10.1016/j.crbiot.2021.05.006.

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14

Du, Jikun, Li Li, and Shining Zhou. "Microbial production of cyanophycin: From enzymes to biopolymers." Biotechnology Advances 37, no. 7 (November 2019): 107400. http://dx.doi.org/10.1016/j.biotechadv.2019.05.006.

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15

Qiu, Jingwen, Casper Wilkens, Kristian Barrett, and Anne S. Meyer. "Microbial enzymes catalyzing keratin degradation: Classification, structure, function." Biotechnology Advances 44 (November 2020): 107607. http://dx.doi.org/10.1016/j.biotechadv.2020.107607.

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16

Sariaslani, F. Sima, and Howard Dalton. "Microbial Enzymes for Oxidation of Organic Molecules." Critical Reviews in Biotechnology 9, no. 3 (January 1989): 171–257. http://dx.doi.org/10.3109/07388558909036736.

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17

Fabara, Andrea N., and Marco W. Fraaije. "An overview of microbial indigo-forming enzymes." Applied Microbiology and Biotechnology 104, no. 3 (December 13, 2019): 925–33. http://dx.doi.org/10.1007/s00253-019-10292-5.

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AbstractIndigo is one of the oldest textile dyes and was originally prepared from plant material. Nowadays, indigo is chemically synthesized at a large scale to satisfy the demand for dyeing jeans. The current indigo production processes are based on fossil feedstocks; therefore, it is highly attractive to develop a more sustainable and environmentally friendly biotechnological process for the production of this popular dye. In the past decades, a number of natural and engineered enzymes have been identified that can be used for the synthesis of indigo. This mini-review provides an overview of the various microbial enzymes which are able to produce indigo and discusses the advantages and disadvantages of each biocatalytic system.

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18

Thuku, R. N., D. Brady, M. J. Benedik, and B. T. Sewell. "Microbial nitrilases: versatile, spiral forming, industrial enzymes." Journal of Applied Microbiology 106, no. 3 (March 2009): 703–27. http://dx.doi.org/10.1111/j.1365-2672.2008.03941.x.

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19

Theriot, Casey M., and Amy M. Grunden. "Hydrolysis of organophosphorus compounds by microbial enzymes." Applied Microbiology and Biotechnology 89, no. 1 (October 2, 2010): 35–43. http://dx.doi.org/10.1007/s00253-010-2807-9.

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20

Chaudhry, A. S. "Biotechnology and Ruminant Nutrition (Jerry Hughes Scholarship)." Proceedings of the British Society of Animal Production (1972) 1994 (March 1994): 90. http://dx.doi.org/10.1017/s0308229600026374.

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Biotechnology is the application of biological procedures and processes to manufacture and service industries (Armstrong, 1988). Any processes which require microorganisms (natural or genetically modified) or biological extracts should be related to biotechnology. Biotechnology has played a vital role in the production of novel products using a variety of microbes. These products have immense potential in improving not only the nutritive quality of crops (Chaudhry and Miller, 1994) but also utilization of food by animals. One such product is recombinant DNA-derived bovine somatotrophin (BST) which has been widely used for years to stimulate milk yield in dairy cows. However, its prolonged use adversely affects health, reproduction and birth weight and skeletal size of the offspring (Dr. Robert Cook, personal communication). Other products of importance are microbial cultures and purified enzymes. The cultures or enzymes are generally mixed with diets to enhance digestive efficiency of livestock by altering microbial activities in the rumen or gastrointestinal tract. They are safe to handle and kind to animals and environment (Dawson, 1992). Whilst biotechnology has a wide range of applications for livestock industry its role in ruminant nutrition is particularly emphasized.

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21

Karimi, S., and O. P. Ward. "Comparative study of some microbial arabinan-degrading enzymes." Journal of Industrial Microbiology 4, no. 3 (May 1989): 173–80. http://dx.doi.org/10.1007/bf01574074.

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22

Brennan, YaLi, Walter N. Callen, Leif Christoffersen, Paul Dupree, Florence Goubet, Shaun Healey, Myrian HernÃ¯Â¿Â½ndez, et al. "Unusual Microbial Xylanases from Insect Guts." Applied and Environmental Microbiology 70, no. 6 (June 2004): 3609–17. http://dx.doi.org/10.1128/aem.70.6.3609-3617.2004.

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ABSTRACT Recombinant DNA technologies enable the direct isolation and expression of novel genes from biotopes containing complex consortia of uncultured microorganisms. In this study, genomic libraries were constructed from microbial DNA isolated from insect intestinal tracts from the orders Isoptera (termites) and Lepidoptera (moths). Using a targeted functional assay, these environmental DNA libraries were screened for genes that encode proteins with xylanase activity. Several novel xylanase enzymes with unusual primary sequences and novel domains of unknown function were discovered. Phylogenetic analysis demonstrated remarkable distance between the sequences of these enzymes and other known xylanases. Biochemical analysis confirmed that these enzymes are true xylanases, which catalyze the hydrolysis of a variety of substituted β-1,4-linked xylose oligomeric and polymeric substrates and produce unique hydrolysis products. From detailed polyacrylamide carbohydrate electrophoresis analysis of substrate cleavage patterns, the xylan polymer binding sites of these enzymes are proposed.

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23

Gunam, I. B. W., I. G. A. Sujana, I. M. M. Wijaya, Y. Setiyo, I. W. W. P. Putra, and L. Suriati. "Isolation and selection of amylase-producing microbes isolated from ragi tape and cassava tape available on the markets." IOP Conference Series: Earth and Environmental Science 913, no. 1 (November 1, 2021): 012041. http://dx.doi.org/10.1088/1755-1315/913/1/012041.

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Abstract Amylase has an important role in biotechnology development and occupies an important position in the world enzyme market, as a biocatalyst in various industrial fields. This study has the goal to find microbial isolates that have the ability to produce amylase enzymes. The study was conducted in two stages, namely: 1) Isolation and selection of microbes that can produce amylase enzymes using starch as substrate, was incubated for 4-7 days at 30°C. Microbial isolates that can produce amylase enzymes are characterized by the presence of clear zones around the colony after the addition of an iodine solution of 1% in the overgrown media of microbes, 2) Test the activity of amylase enzymes using a dinitrosalicylic acid reagent test. The activity of the amylase enzyme is determined by measurement using a spectrophotometer at a wavelength of 540 nm. The sample used comprised of 7 types of ragi tape and 2 samples from cassava tape that has been fermented for 5-7 days. The results obtained in the first stage were 65 microbial isolates, 16 of which had clear zones, consisting of 7 isolates from ragi tape samples and 9 isolates from cassava tape samples. In the enzyme activity test, there are several isolates that have the potential to produce amylase enzymes, these include R5I4 (0.897 ± 0.018 U/mL), R2I5.1 (0.814 ± 0.011 U/mL), R5I3 (0.727 ± 0,042 U/mL) (derived from cassava ragi tape samples) and T2I2.2 (0.812 ± 0.013 U/mL), T2I6.1 (0.817 ± 0.010 U/mL), T2I2.1 (0.735 ± 0.023 U/mL), T1I4 (0.755 ± 0.020 U/mL) (derived from cassava tape samples). The isolate with the highest enzyme activity is the R5I4 which has the value enzyme activity of 0.897 ± 0.018 U/mL and with a fairly high or moderate category, while the lowest enzyme activity is the T1I1.1 isolate of 0.284 ± 0.020 U/mL.

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24

Karigar, Chandrakant S., and Shwetha S. Rao. "Role of Microbial Enzymes in the Bioremediation of Pollutants: A Review." Enzyme Research 2011 (September 7, 2011): 1–11. http://dx.doi.org/10.4061/2011/805187.

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A large number of enzymes from bacteria, fungi, and plants have been reported to be involved in the biodegradation of toxic organic pollutants. Bioremediation is a cost effective and nature friendly biotechnology that is powered by microbial enzymes. The research activity in this area would contribute towards developing advanced bioprocess technology to reduce the toxicity of the pollutants and also to obtain novel useful substances. The information on the mechanisms of bioremediation-related enzymes such as oxido-reductases and hydrolases have been extensively studied. This review attempts to provide descriptive information on the enzymes from various microorganisms involved in the biodegradation of wide range of pollutants, applications, and suggestions required to overcome the limitations of their efficient use.

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25

Rao, Mala B., Aparna M. Tanksale, Mohini S. Ghatge, and Vasanti V. Deshpande. "Molecular and Biotechnological Aspects of Microbial Proteases." Microbiology and Molecular Biology Reviews 62, no. 3 (September 1, 1998): 597–635. http://dx.doi.org/10.1128/mmbr.62.3.597-635.1998.

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SUMMARY Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.

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Thapa, Santosh, Jitendra Mishra, Naveen Arora, Priya Mishra, Hui Li, Joshua O′Hair, Sarabjit Bhatti, and Suping Zhou. "Microbial cellulolytic enzymes: diversity and biotechnology with reference to lignocellulosic biomass degradation." Reviews in Environmental Science and Bio/Technology 19, no. 3 (May 29, 2020): 621–48. http://dx.doi.org/10.1007/s11157-020-09536-y.

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27

Verma, Amit, Hukum Singh, Shahbaz Anwar, Anirudha Chattopadhyay, Kapil K. Tiwari, Surinder Kaur, and Gurpreet Singh Dhilon. "Microbial keratinases: industrial enzymes with waste management potential." Critical Reviews in Biotechnology 37, no. 4 (June 13, 2016): 476–91. http://dx.doi.org/10.1080/07388551.2016.1185388.

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28

Kraft, Beate, Marc Strous, and Halina E. Tegetmeyer. "Microbial nitrate respiration – Genes, enzymes and environmental distribution." Journal of Biotechnology 155, no. 1 (August 2011): 104–17. http://dx.doi.org/10.1016/j.jbiotec.2010.12.025.

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29

Szymczak, Tomasz, Justyna Cybulska, Marcin Podleśny, and Magdalena Frąc. "Various Perspectives on Microbial Lipase Production Using Agri-Food Waste and Renewable Products." Agriculture 11, no. 6 (June 11, 2021): 540. http://dx.doi.org/10.3390/agriculture11060540.

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Lipases are enzymes that catalyze various types of reactions and have versatile applications. Additionally, lipases are the most widely used class of enzymes in biotechnology and organic chemistry. Lipases can be produced by a wide range of organisms including animals, plants and microorganisms. Microbial lipases are more stable, they have substrate specificity and a lower production cost as compared to other sources of these enzymes. Although commercially available lipases are widely used as biocatalysts, there are still many challenges concerning the production of microbial lipases with the use of renewable sources as the main component of microbial growth medium such as straw, bran, oil cakes and industrial effluents. Submerged fermentation (SmF) and solid-state fermentation (SSF) are the two important technologies for the production of lipases by microorganisms. Therefore, this review focuses on microbial lipases, especially their function, specificity, types and technology production, including the use of renewable agro-industrial residues and waste materials.

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30

Pollock, Thomas J., and Motohide Yamazaki. "Clarification of microbial polysaccharides with enzymes secreted fromLysobacter species." Journal of Industrial Microbiology 11, no. 3 (May 1993): 187–92. http://dx.doi.org/10.1007/bf01583721.

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31

Aparicio, Jesús F., and Juan F. Martín. "Microbial cholesterol oxidases: bioconversion enzymes or signal proteins?" Molecular BioSystems 4, no. 8 (2008): 804. http://dx.doi.org/10.1039/b717500k.

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32

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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33

Vaario, Lu-Min, Hannu Fritze, Peter Spetz, Jussi Heinonsalo, Peter Hanajík, and Taina Pennanen. "Tricholoma matsutake Dominates Diverse Microbial Communities in Different Forest Soils." Applied and Environmental Microbiology 77, no. 24 (October 7, 2011): 8523–31. http://dx.doi.org/10.1128/aem.05839-11.

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ABSTRACTFungal and actinobacterial communities were analyzed together with soil chemistry and enzyme activities in order to profile the microbial diversity associated with the economically important mushroomTricholoma matsutake. Samples of mycelium-soil aggregation (shiro) were collected from three experimental sites where sporocarps naturally formed. PCR was used to confirm the presence and absence of matsutake in soil samples. PCR-denaturing gradient gel electrophoresis (DGGE) fingerprinting and direct sequencing were used to identify fungi and actinobacteria in the mineral and organic soil layers separately. Soil enzyme activities and hemicellulotic carbohydrates were analyzed in a productive experimental site. Soil chemistry was investigated in both organic and mineral soil layers at all three experimental sites. Matsutake dominated in the shiro but also coexisted with a high diversity of fungi and actinobacteria.Tomentollopsissp. in the organic layer above the shiro andPilodermasp. in the shiro correlated positively with the presence ofT. matsutakein all experimental sites. AThermomonosporaceaebacterium andNocardiasp. correlated positively with the presence ofT. matsutake, andStreptomycessp. was a common cohabitant in the shiro, although these operational taxonomic units (OTUs) did not occur at all sites. Significantly higher enzyme activity levels were detected in shiro soil. These enzymes are involved in the mobilization of carbon from organic matter decomposition. Matsutake was not associated with a particular soil chemistry compared to that of nearby sites where the fungus does not occur. The presence of a significant hemicellulose pool and the enzymes to degrade it indicates the potential for obtaining carbon from the soil rather than tree roots.

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Jaspars, Marcel. "The benefits of living together – studying marine symbioses to discover enzymes for biotechnology applications." Biochemist 44, no. 2 (February 24, 2022): 13–17. http://dx.doi.org/10.1042/bio_2022_102.

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Over the past 50 years, more than 15 pharmaceuticals derived from marine organisms have come to the market. Most of these come from filter-feeding invertebrates that contain a high proportion of microbial symbionts. Microbiology and molecular genetic studies have shown that many of these drug-like compounds are produced by the microbial symbiont. The enzymes that produce these compounds are promiscuous meaning they can process a diverse range of related substrates, making them extremely attractive to the biotechnology industry. Determining the structure of these enzymes makes them amenable to engineering, allowing them to process non-natural substrates. Using this approach, synthetic substrates can be treated with a cocktail of enzymes to prepare focused libraries of compounds to hit drug targets such as protein–protein interactions. These targets are involved in a range of diseases from cancer to immune disorders and are hard to modulate using small molecule drugs. Complex modified cyclic peptides produced using a chemoenzymatic process may be a promising approach to address these disease conditions.

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

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

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Frandsen, Kristian E. H., and Leila Lo Leggio. "Lytic polysaccharide monooxygenases: a crystallographer's view on a new class of biomass-degrading enzymes." IUCrJ 3, no. 6 (October 14, 2016): 448–67. http://dx.doi.org/10.1107/s2052252516014147.

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Lytic polysaccharide monooxygenases (LPMOs) are a new class of microbial copper enzymes involved in the degradation of recalcitrant polysaccharides. They have only been discovered and characterized in the last 5–10 years and have stimulated strong interest both in biotechnology and in bioinorganic chemistry. In biotechnology, the hope is that these enzymes will finally help to make enzymatic biomass conversion, especially of lignocellulosic plant waste, economically attractive. Here, the role of LPMOs is likely to be in attacking bonds that are not accessible to other enzymes. LPMOs have attracted enormous interest since their discovery. The emphasis in this review is on the past and present contribution of crystallographic studies as a guide to functional understanding, with a final look towards the future.

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37

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

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

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Syldatk, C., O. May, J. Altenbuchner, R. Mattes, and M. Siemann. "Microbial hydantoinases - industrial enzymes from the origin of life?" Applied Microbiology and Biotechnology 51, no. 3 (March 26, 1999): 293–309. http://dx.doi.org/10.1007/s002530051395.

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

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Sun, Haiyan, Pingjuan Zhao, Xiangyang Ge, Yongjun Xia, Zhikui Hao, Jianwen Liu, and Ming Peng. "Recent Advances in Microbial Raw Starch Degrading Enzymes." Applied Biochemistry and Biotechnology 160, no. 4 (March 10, 2009): 988–1003. http://dx.doi.org/10.1007/s12010-009-8579-y.

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Ovais, Muhammad, Ali Khalil, Muhammad Ayaz, Irshad Ahmad, Susheel Nethi, and Sudip Mukherjee. "Biosynthesis of Metal Nanoparticles via Microbial Enzymes: A Mechanistic Approach." International Journal of Molecular Sciences 19, no. 12 (December 18, 2018): 4100. http://dx.doi.org/10.3390/ijms19124100.

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During the last decade, metal nanoparticles (MtNPs) have gained immense popularity due to their characteristic physicochemical properties, as well as containing antimicrobial, anti-cancer, catalyzing, optical, electronic and magnetic properties. Primarily, these MtNPs have been synthesized through different physical and chemical methods. However, these conventional methods have various drawbacks, such as high energy consumption, high cost and the involvement of toxic chemical substances. Microbial flora has provided an alternative platform for the biological synthesis of MtNPs in an eco-friendly and cost effective way. In this article we have focused on various microorganisms used for the synthesis of different MtNPs. We also have elaborated on the intracellular and extracellular mechanisms of MtNP synthesis in microorganisms, and have highlighted their advantages along with their challenges. Moreover, due to several advantages over chemically synthesized nanoparticles, the microbial MtNPs, with their exclusive and dynamic characteristics, can be used in different sectors like the agriculture, medicine, cosmetics and biotechnology industries in the near future.

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Li, Jingxin, Qian Wang, Ronald S. Oremland, Thomas R. Kulp, Christopher Rensing, and Gejiao Wang. "Microbial Antimony Biogeochemistry: Enzymes, Regulation, and Related Metabolic Pathways." Applied and Environmental Microbiology 82, no. 18 (June 24, 2016): 5482–95. http://dx.doi.org/10.1128/aem.01375-16.

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ABSTRACTAntimony (Sb) is a toxic metalloid that occurs widely at trace concentrations in soil, aquatic systems, and the atmosphere. Nowadays, with the development of its new industrial applications and the corresponding expansion of antimony mining activities, the phenomenon of antimony pollution has become an increasingly serious concern. In recent years, research interest in Sb has been growing and reflects a fundamental scientific concern regarding Sb in the environment. In this review, we summarize the recent research on bacterial antimony transformations, especially those regarding antimony uptake, efflux, antimonite oxidation, and antimonate reduction. We conclude that our current understanding of antimony biochemistry and biogeochemistry is roughly equivalent to where that of arsenic was some 20 years ago. This portends the possibility of future discoveries with regard to the ability of microorganisms to conserve energy for their growth from antimony redox reactions and the isolation of new species of “antimonotrophs.”

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Liu, Long, Haiquan Yang, Hyun-dong Shin, Rachel R. Chen, Jianghua Li, Guocheng Du, and Jian Chen. "How to achieve high-level expression of microbial enzymes." Bioengineered 4, no. 4 (July 2013): 212–23. http://dx.doi.org/10.4161/bioe.24761.

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Karns, Jeffrey S. "Biotechnology for the Treatment of Pesticide Waste." HortScience 31, no. 4 (August 1996): 699c—699. http://dx.doi.org/10.21273/hortsci.31.4.699c.

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The use of microbes and/or microbial processes for the bioremediation of soils contaminated with pesticides is an idea that has enjoyed considerable interest over the past several years. Many microbes with specific pathways for the degradation of particular pesticides, or classes of pesticide, have been isolated and characterized. Unfortunately, most sites that are heavily contaminated with pesticides contain a mixture of the many different types of pesticides that have been used over the last 5 decades. This complex mixture of compounds may inhibit microbial degradation or may require multiple treatments to assure that all the chemicals are degraded. Treatment of wastes before they contaminate the environment is one way to avoid the problems associated with mixed wastes. We have isolated a number of microorganisms that detoxify insecticides, such as carbaryl of parathion via the action of hydrolase enzymes. These enzymes can be used to treat waste pesticide solutions before disposal. A system was developed for the disposal of one high-volume organophosphate insecticide waste by treatment with parathion hydrolase, followed by ozonation to yield harmless products that were readily degraded by other soil microorganisms. A second method for disposal of this waste involves altering the environmental conditions in the waste to stimulate the growth of microorganisms naturally present in the material utilizing the pesticide as a carbon source. This accomplishes degradation of the material over a 2-week period. Many, if not all, pesticides are degradable to some degree by microorganisms, and this fact can be exploited to provide cost-effective methods for the safe disposal of pesticide wastes.

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Traving, Sachia J., Uffe H. Thygesen, Lasse Riemann, and Colin A. Stedmon. "A Model of Extracellular Enzymes in Free-Living Microbes: Which Strategy Pays Off?" Applied and Environmental Microbiology 81, no. 21 (August 7, 2015): 7385–93. http://dx.doi.org/10.1128/aem.02070-15.

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ABSTRACTAn initial modeling approach was applied to analyze how a single, nonmotile, free-living, heterotrophic bacterial cell may optimize the deployment of its extracellular enzymes. Free-living cells live in a dilute and complex substrate field, and to gain enough substrate, their extracellular enzymes must be utilized efficiently. The model revealed that surface-attached and free enzymes generate unique enzyme and substrate fields, and each deployment strategy has distinctive advantages. For a solitary cell, surface-attached enzymes are suggested to be the most cost-efficient strategy. This strategy entails potential substrates being reduced to very low concentrations. Free enzymes, on the other hand, generate a radically different substrate field, which suggests significant benefits for the strategy if free cells engage in social foraging or experience high substrate concentrations. Swimming has a slight positive effect for the attached-enzyme strategy, while the effect is negative for the free-enzyme strategy. The results of this study suggest that specific dissolved organic compounds in the ocean likely persist below a threshold concentration impervious to biological utilization. This could help explain the persistence and apparent refractory state of oceanic dissolved organic matter (DOM). Microbial extracellular enzyme strategies, therefore, have important implications for larger-scale processes, such as shaping the role of DOM in ocean carbon sequestration.

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Sharma, Neha, Shuchi Kaushik, and Rajesh Singh Tomar. "Isolation and Characterization of Extracellular Enzyme (Glutaminase and Urease) producing Bacteria isolated from Soil Samples of Different Regions of Gwalior, Madhya Pradesh, India." Research Journal of Biotechnology 16, no. 7 (June 25, 2021): 122–29. http://dx.doi.org/10.25303/167rjbt12221.

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Microbial glutaminase and urease have demonstrated their benefits in various fields like medicinal, pharmaceutical and biotechnological industries. Keeping this viewpoint, the aim of the present study was the isolation and characterization of extracellular enzyme-producing bacteria from soil samples collected from different regions of Gwalior (M.P.). The isolated bacterial cultures were processed by serial dilution method and maintained on nutrient agar medium following standard microbiological laboratory practices for maintenance and preservation of bacteria. We screened out three enzyme producing strains of Salmonella sp., Proteus vulgaris and Bacillus subtilis. The screening was based on biochemical testing and enzyme assays. To accomplish this work, we used differential as well as selective media. All the selected isolates were able to produce enzymes like L-Glutaminase and Urease with different specific enzymatic activity. These bacterial isolates were not reported to show any type of allergenicity when their sequences were checked by bioinformatics tool Algpred. So, these bacterial isolates can be considered as an alternative source for the production of enzymes and can be used for largescale production of enzymes at the industrial level.

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Sewalt, Vincent, Diane Shanahan, Lori Gregg, James La Marta, and Roberto Carrillo. "The Generally Recognized as Safe (GRAS) Process for Industrial Microbial Enzymes." Industrial Biotechnology 12, no. 5 (October 2016): 295–302. http://dx.doi.org/10.1089/ind.2016.0011.

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Kim, Kyoung-Rok, and Deok-Kun Oh. "Production of hydroxy fatty acids by microbial fatty acid-hydroxylation enzymes." Biotechnology Advances 31, no. 8 (December 2013): 1473–85. http://dx.doi.org/10.1016/j.biotechadv.2013.07.004.

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Kwon, Yong-Chan, Kyung-Ho Lee, Ho-Cheol Kim, Kyuboem Han, Joo-Hyun Seo, Byung-Gee Kim, and Dong-Myung Kim. "Cloning-Independent Expression and Analysis of ω-Transaminases by Use of a Cell-Free Protein Synthesis System." Applied and Environmental Microbiology 76, no. 18 (July 23, 2010): 6295–98. http://dx.doi.org/10.1128/aem.00029-10.

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ABSTRACT Herewith we report the expression and screening of microbial enzymes without involving cloning procedures. Computationally predicted putative ω-transaminase (ω-TA) genes were PCR amplified from the bacterial colonies and expressed in a cell-free protein synthesis system for subsequent analysis of their enzymatic activity and substrate specificity. Through the cell-free expression analysis of the putative ω-TA genes, a number of enzyme-substrate pairs were identified in a matter of hours. We expect that the proposed strategy will provide a universal platform for bridging the information gap between nucleotide sequence and protein function to accelerate the discovery of novel enzymes.

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Awolusi, Oluyemi Olatunji, Adedeji Nelson Ademakinwa, Abidemi Ojo, Mariana Erasmus, Faizal Bux, and Mayowa Oladele Agunbiade. "Marine Actinobacteria Bioflocculant: A Storehouse of Unique Biotechnological Resources for Wastewater Treatment and Other Applications." Applied Sciences 10, no. 21 (October 30, 2020): 7671. http://dx.doi.org/10.3390/app10217671.

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The bioactive compounds produced by actinobacteria have played a major role in antimicrobials, bioremediation, biofuels, enzymes, and anti-cancer activities. Biodegradable microbial flocculants have been produced by bacteria, algae, and fungi. Microbial bioflocculants have also attracted biotechnology importance over chemical flocculants as a result of degradability and environmentally friendly attributes they possess. Though, freshwater actinobacteria flocculants have been explored in bioflocculation. Yet, there is a paucity of information on the application of actinobacteria flocculants isolated from the marine environment. Similarly, marine habitats that supported the biodiversity of actinobacteria strains in the field of biotechnology have been underexplored in bioflocculation. Hence, this review reiterates the need to optimize culture conditions and other parameters that affect bioflocculant production by using a response surface model or artificial neural network.

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