| Literature DB >> 33715051 |
Jai Shankar Paul1, Nisha Gupta1, Esmil Beliya1,2, Shubhra Tiwari1, Shailesh Kumar Jadhav3.
Abstract
α-Amylases are the oldest and versatile starch hydrolysing enzymes which can replace chemical hydrolysis of starch in industries. It cleaves the α-(1,4)-D-glucosidic linkage of starch and other related polysaccharides to yield simple sugars like glucose, maltose and limit dextrin. α-Amylase covers about 30% shares of the total enzyme market. On account of their superior features, α-amylase is the most widely used among all the existing amylases for hydrolysis of polysaccharides. Endo-acting α-amylase of glycoside hydrolase family 13 is an extensively used biocatalyst and has various biotechnological applications like in starch processing, detergent, textile, paper and pharmaceutical industries. Apart from these, it has some novel applications including polymeric material for drug delivery, bioremediating agent, biodemulsifier and biofilm inhibitor. The present review will accomplish the research gap by providing the unexplored aspects of microbial α-amylase. It will allow the readers to know about the works that have already been done and the latest trends in this field. The manuscript has covered the latest immobilization techniques and the site-directed mutagenesis approaches which are readily being performed to confer the desirable property in wild-type α-amylases. Furthermore, it will state the inadequacies and the numerous obstacles coming in the way of its production during upstream and downstream steps and will also suggest some measures to obtain stable and industrial-grade α-amylase.Entities:
Keywords: Biocatalyst; Drug delivery; Glycoside hydrolases; Glycosidic linkage; α-Amylase
Year: 2021 PMID: 33715051 DOI: 10.1007/s12010-021-03546-4
Source DB: PubMed Journal: Appl Biochem Biotechnol ISSN: 0273-2289 Impact factor: 2.926