dc.contributor.author | Arya Nandan | |
dc.contributor.author | Nampoothiri, K M | |
dc.date.accessioned | 2018-07-31T09:28:41Z | |
dc.date.available | 2018-07-31T09:28:41Z | |
dc.date.issued | 2017-12 | |
dc.identifier.citation | Bioresource Technology, 245(Part B):1757-1765 | en_US |
dc.identifier.uri | http://10.10.100.66:8080/xmlui/handle/123456789/3253 | |
dc.description.abstract | Aminopeptidases are exopeptidases that catalyze the hydrolysis of amino acid residues from the N terminus of peptides and proteins. They are widely and diversely used for protein hydrolysis in industrial and research applications. They form a large enzyme family in microorganisms and most of the sequenced microbial genomes contain several aminopeptidase coding genes. Various approaches are being used to enhance the yield and desired properties of these enzymes to make it more suited for industrial applications. Novel aminopeptidases are being developed by site directed mutagenesis and recombinant DNA technology with improved substrate specificity and stability. This review focuses on its classification and recent advancements in the molecular studies pertaining to this enzyme. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | Aminopeptidases | en_US |
dc.subject | Metalloproteases | en_US |
dc.subject | Gene cloning | en_US |
dc.subject | Protein engineering | en_US |
dc.subject | Thermostability | en_US |
dc.title | Molecular Advances in Microbial Aminopeptidases | en_US |
dc.type | Article | en_US |