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Biocatalysts: The Different Classes and Applications for Synthesis of APIs
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
These hydrolyzing enzymes catalyze the cleavage of a covalent bond using water. Hydrolases comprise lipases, esterases, proteases, nitrilases, epoxidases, and hydantoinases. They are attractive candidates for application in organic synthesis because they need no costly cofactors that must be recycled as prerequisite for an economic production. Many of these enzymes contain a nucleophilic serine as part of the catalytic triad that contains in addition an aspartate or glutamate as acidic and a histidine as basic residue; hydrolysis proceeds via the formation of an acyl-enzyme intermediate through a nucleophilic attack of the hydroxyl group of Ser on the carbonyl carbon (formation of an ester bond) which is followed by a nucleophilic attack of the water oxygen on the carbonyl carbon of the acyl-enzyme intermediate leading to its hydrolysis and regeneration of the enzyme.
Hemicellulases: Diversity and Applications
Published in Charles E. Wyman, Handbook on Bioethanol, 2018
John S. Brigham, William S. Adney, Michael E. Himmel
In keeping with other hydrolytic enzyme systems important for modern biomass conversion biotechnology, numerous xylanolytic genes have been cloned [69,70, 71]and site-directed mutagenesis has begun with the goal of obtaining mutant enzymes with higher catalytic efficiencies or stabilities [72]. Furthermore, development of recombinant techniques has also provided a tool for sorting out the complex degradation pathways by permitting sufficient quantities of key enzymes to be produced in heterologous hosts to test interaction (synergistic) phenomena at reasonable hydrolysis levels. Also, by cloning hydrolase genes in organisms that produce large quantities of heterologous protein, new industrial sources of targeted enzymes can be obtained. Recent breakthroughs in cellulase research provide encouragement that new, artificial enzyme systems can be produced by recombinant fungi or bacteria that provide enhanced kinetic and physical properties [21]. We can very safely predict that there will be research into cost-effectively converting biomass to useful chemical feedstocks until the problem is solved, and hemicellulose is a key component of the puzzle.
Lipase-Mediated Biocatalysis as a Greener and Sustainable Choice for Pharmaceutical Processes
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2020
Monika Sharma, Tanya Bajaj, Rohit Sharma
Hydrolases are a group of enzymes catalyzing basic reactions such as bond cleavage (hydrolysis), condensation, and alcoholysis. Hydrolases include glycosidases, proteases, nitrilases, esterases, and lipases. These enzymes constitute about 95% of the total production of industrial enzymes. Hydrolases are chemically unique enzymes that can withstand harsh environmental conditions. Lipases and esterases are capable of functioning in the presence of water-miscible as well as immiscible solvents (Bornscheuer and Kazlauskas, 2006). This provides a basis for their utilization in biocatalysis at a larger scale.
Xenobiotic metabolism and transport in Caenorhabditis elegans
Published in Journal of Toxicology and Environmental Health, Part B, 2021
Jessica H. Hartman, Samuel J. Widmayer, Christina M. Bergemann, Dillon E. King, Katherine S. Morton, Riccardo F. Romersi, Laura E. Jameson, Maxwell C. K. Leung, Erik C. Andersen, Stefan Taubert, Joel N. Meyer
Hydrolysis reactions use water to break a chemical bond. Enzymes that perform hydrolysis reactions are referred to as hydrolases. Xenobiotic-metabolizing hydrolases include esterases, amidases, and epoxide hydrolases. Of those, only epoxide hydrolases were studied in detail in C. elegans. Although humans express four epoxide hydrolase isoforms including both membrane-bound (microsomal) and soluble (cytosolic) forms, C. elegans possesses only two isoforms, ceeh-1 and ceeh-2 (Harris et al. 2008). These are most orthologous with the EH3 and EH4 human isoforms, which are the most recently discovered and least well characterized among human isoforms but are postulated to predominantly metabolize lipids. The C. elegans enzymes were confirmed to exhibit endobiotic and xenobiotic metabolizing activities, with ceeh-1 displaying higher activity toward substrates compared to ceeh-2 (Harris et al. 2008). Further studies are needed to establish the substrate specificity of both isoforms, particularly for xenobiotic substrates.
Improving operational stability of thermostable Pythium myriotylum secretory serine protease by preparation of cross-linked enzyme aggregates (CLEAs)
Published in Preparative Biochemistry & Biotechnology, 2020
Aswati R. Nair, Geethu Chellapan
Global market for industrial enzymes was estimated at 5.6$billion in 2018 and this demand is expected to increase at 6.8% compound annual growth rate (CAGR) by 2024.[1] Approximately, 75% of the enzymes used in industries are hydrolases like proteases, cellulases, amylases, and lipases.[1] Proteases remain the dominant enzyme type among hydrolases[2,3] due to their extensive use in the detergent and dairy industries.[4] Among proteases, alkaline serine proteases (SPs) are the most important group of commercially exploited enzymes and account for approximately 35% of the total microbial enzyme sales.[5,6] Most of the commercial alkaline proteases viz. Subtilisin Carlsberg, Subtilisin BPN’, Alcalase, Esperase and Savinase sourced from Bacillus find major applications in detergent industry.[4,7] However these proteases exhibit some drawbacks that include instability in presence of surfactants and oxidizing agents commonly found in detergent formulations besides high production costs.[8]
Evaluation of droplet-based microfluidic platforms as a convenient tool for lipases and esterases assays
Published in Preparative Biochemistry and Biotechnology, 2019
Pawel Jankowski, Adam Samborski, Ryszard Ostaszewski, Piotr Garstecki
Enzymes catalyze a variety of organic and biochemical reactions. Consequently, the determination of the enzyme activity is extremely important in medical diagnostics, in biotechnology, and in research. The most important property of all enzymes is their catalytic power – measured by the kinetic parameters of an enzymatic reaction. Measurement of rapid enzyme kinetics is essential to an understanding of many biological and chemical processes.[1] Special attention has been paid to hydrolytic enzymes due to their ability to accept a wide range of substrates and to their stability in aqueous environments. Interestingly, hydrolases may also be active in organic solvents. This makes hydrolases attractive both in academic research and in industrial applications. Often, the kinetic properties of hydrolases do not meet the requirements of a particular application. Directed evolution techniques are widely used for the generation of enzymes expressing desired kinetic properties in respect to particular substrates.[2] Fast and efficient test methods for the determination of hydrolase hydrolytic activity are very valuable for high-throughput screening in biotechnology.