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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
Prediction of protein structures has been made possible by the use of a number of bioinformatics tools. The amino acid sequence of a protein can define its function, and thus the protein sequence-function relationship is an interesting approach exploited by the protein engineering methods. Protein engineering can be defined as the process of altering the amino acid sequence to obtain desirable activity, specificity, and stability of a protein. It involves the use of a combination of techniques like rational/semi-rational design which help in generating the outline of a protein with desired properties, which is then achieved practically through the means of directed evolution (Bernal et al., 2018). Thermomyces lanuginosus lipase was modified for improved organic solvent stability through protein engineering technique by Tian et al. (2017).
Engineered enzymes and enzyme systems
Published in Ruben Michael Ceballos, Bioethanol and Natural Resources, 2017
A more recent and promising alternative to the development of ideal industrial enzymes is protein engineering. Using methods in molecular biology, protein biochemistry, and computational biology, scientists have sought to understand the molecular underpinnings of specific enzyme functionalities to generate novel enzymes featuring the most desirable traits from one or more natural or previously modified model enzymes. Two general approaches in protein engineering have been employed over recent decades with varying levels of success: rational design and directed evolution. (A third approach for protein improvement based on statistical analysis is also used; however, it is not as prevalent and will not be emphasized here). In rational design, knowledge of enzyme structure (primary, secondary, tertiary, and quaternary) is required, and the catalytic mechanism must be known (Johnsson et al., 1993; Pleiss, 2012). Alternatively, in directed evolution, conditions are altered, and artificial selection is employed to direct changes in emerging populations of enzyme-expressing microorganisms. This approach relies on screening samples from cultures after random mutagenesis, molecular recombination, or focused mutagenesis (Packer and Liu, 2015) (Figure 4.1; left and middle panels).
Production, Purification, and Application of the Microbial Enzymes
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Anupam Pandey, Ankita H. Tripathi, Priyanka H. Tripathi
Protein engineering is a technique for altering the sequence of a protein in order to obtain a specific result, such as enhanced stability to temperature, chemical solvents, and high and low pH. Protein engineering includes site-directed mutagenesis, which involves the substitution of particular amino acids, which requires a significant quantity of knowledge about the biocatalyst being modified, with modulation in its three-dimensional structure and mechanism involved in the chemical process. Engineered enzymes with improved performance have already been used in industrial operations, such as proteinases, cellulases, amylases, lipases, and glucoamylases (Patel et al., 2017).
Combination of engineering the substrate and Ca2+ binding domains of heparinase I to improve the catalytic activity
Published in Preparative Biochemistry & Biotechnology, 2023
Hua-Ping Zhou, Ding-Ran Wang, Chen-Lu Xu, Ye-Wang Zhang
The low activity of heparinase I was one of the main causes that currently hamper its industrial application. Therefore, structural engineering of heparinase I is an effective approach to improve the catalytic activity of heparinase I. The enzyme production reached 20,650 U·L−1 by fuzing maltose binding protein (MBP) with heparinase I to form a fusion protein.[24] After mutation of C297 on MBP-Hep I, its enzyme activity (149 U/mg) was increased by 30.6% by inhibiting the formation of intramolecular disulfide bonds.[25] The clone E. coli-heparinase-I133T/P316T was obtained by directed evolution of heparinase I, and its enzymatic activity was increased by 57.8%.[26] The amino acid residues near the active pocket of heparinase I were modified by protein engineering. The multiple-point mutant S169D/A259D showed a 122.05% increase in enzyme activity.[12] However, the present heparinase I is not enough for its industrial application. Therefore, we need to find new candidate mutants to further improve the catalytic performance of heparinase I.
Extremozymes used in textile industry
Published in The Journal of The Textile Institute, 2022
Priyanka Kakkar, Neeraj Wadhwa
Extremozymes are the new approach to the industrial area as they can tolerate harsh environment used in the industrial processes. Extremophiles opens a field for the researchers to explore the novel biocatalyst. Various extremozymes found their application in textile processing or finishing process depending on the catalytic parameters. Thermozymes are used where the reaction temperature is high whereas psychrophiles works at low temperature. Usage of extreme biocatalyst in textile improves the efficiency of process, quality of the fabric, less energy consumption, and releases less chemical to the textile effluents. Detergent industry turning towards the cold adaptive alkaline enzymes for detergent formulation and some are already present in the market. The major challenge with extremophiles is their production process and mimicking the extreme external lab conditions. But the metagenomic approach of direct isolation of genomic DNA and increasing the production yield by protein engineering or heterologous expression of protein is the best possible solution.
In-silico investigation of the efficiency of microbial dioxygenases in degradation of sulfonylurea group herbicides
Published in Bioremediation Journal, 2022
Sutapa Bauri, Madhab Kumar Sen, Renuka Das, Sunil Kanti Mondal
Among the most dynamically developing scientific fields, protein engineering has changed thrillingly due to developing technologies like high throughput and deep sequencing, directed evolution methods, and fluorescence-based sorting technologies. In silico studies, aiding in protein design and engineering are being developed with new experimental techniques. Results from our molecular docking studies with microbial dioxygenase from three different microorganisms (Pseudomonas putida, Brevibacterium fuscum and Arthrobacter globiformis) with chlorsulfuron and metsulfuron-methyl, showed that homoprotocatechuate 2,3-dioxygenase from B. fuscum and A. globiformis were more effective than catechol 2, 3-dioxygenase from P. putida. So, B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuron-methyl. Our results will help in the scientific development and usage of herbicides and their microbial degradation mechanisms. The bioinformatics approaches can be most successfully used for engineering protein stability due to their ability to produce good resolution data and identify stabilizing mutations. The results of this study will be socially beneficial in order to maintain the soil health in which appropriate growth of crop plants are dependent. Therefore, microbial biodegradation of herbicides can be considered as a suitable option for future studies. In future, use of bioherbicides is expected to relieve our dependency on chlorsulfuron and metsulfuron-methyl to minimize ever-increasing environmental pollution.