Department of Biological sciences Adamawa State University, Mubi, Nigeria; Department of Industrial Biotechnology, Faculty of Bioscience and Bioengineering University Teknologi Malaysia, Malaysia
Mienda, B.S., Department of Biological sciences Adamawa State University, Mubi, Nigeria, Department of Industrial Biotechnology, Faculty of Bioscience and Bioengineering University Teknologi Malaysia, Malaysia; Yahya, A., Department of Industrial Biotechnology, Faculty of Bioscience and Bioengineering University Teknologi Malaysia, Malaysia
Proteolytic enzymes are becoming more ubiquitous as bacteria and fungi. Some proteases from microbial sources are industrially important enzymes but often have to be improved for their catalytic efficiency and stabilities in solvents and temperature at industrial scales in order to suit their applications. Research on protein engineering of microbial proteases to improve their stability and catalytic performances have been extensively conducted by various researchers across the globe using different molecular approaches vis a vis site-directed mutagenesis (SDM) and directed evolutions (DE). SDM has been extremely useful in substitution of important amino acids of microbial proteases; though its major obstacle is that it is imperative to know the three dimensional (3D) structure of the protease in question. Directed evolutions (DE) subsequently emerged as an alternative to SDM, since the knowledge of the enzymes 3D structure is less significant, though its major drawback has been the creation of large mutant libraries and high through put screening of mutant with desired properties. To overcome the drawback of DE, a flow cytometry based screening system have been recently developed which may likely pave way for efficient and fastest way of screening of mutants with improved desired properties. Sometimes these two approaches can be applied concurrently to obtain enzymes with novel properties. This review aimed at gathering the disperse literature on the approaches where bacteria and fungi have been chosen as sources of microbial proteases. A recent flow cytometry based screening system for DE of proteases has also been reported.
alanine; alpha levo fucosidase; amidase; aqualysin I; aspartate aminotransferase; aspartic acid; aspartic proteinase; aspergillopepsin; bacterial enzyme; beta galactosidase; beta lactamase; cysteine; dihydropyrimidinase; esterase; fructose bisphosphate aldolase; fungal enzyme; glycine; leucine; methionine; pepsin A; peroxidase; protein LasA; proteinase; serine; serine proteinase; subtilisin; triacylglycerol lipase; unclassified drug; amino acid substitution; article; Aspergillus oryzae; aspergillus saitoi; Bacillus subtilis; catalysis; directed molecular evolution; Eggerthella lenta; enzyme engineering; enzyme stability; enzyme structure; flow cytometry; fungus; Geobacillus stearothermophilus; Lactobacillus delbrueckii; Lysobacter; mutant; nonhuman; Pseudomonas aeruginosa; rhizopus niveus; Saccharomyces cerevisiae; site directed mutagenesis; thermostability; Thermus aquaticus