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Updates on naringinase: structural and biotechnological aspects
Authors:Munish?Puri  author-information"  >  author-information__contact u-icon-before"  >  mailto:munish.puri@deakin.edu.au"   title="  munish.puri@deakin.edu.au"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Centre for Biotechnology, Chemistry and System Biology (Biodeakin), Institute of Technology Research and Innovation (ITRI), Deakin University, Warrnambool, Victoria, 3217, Australia;(2) Fermentation and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Punjab, India
Abstract:Naringinases has attracted a great deal of attention in recent years due to its hydrolytic activities which include the production of rhamnose, and prunin and debittering of citrus fruit juices. While this enzyme is widely distributed in fungi, its production from bacterial sources is less commonly known. Fungal naringinase are very important as they are used industrially in large amounts and have been extensively studied during the past decade. In this article, production of bacterial naringinase and potential biotechnological applications are discussed. Bacterial rhamnosidases are exotype enzymes that hydrolyse terminal non-reducing α-l-rhamnosyl groups from α-l-rhamnose containing polysaccharides and glycosides. Structurally, they are classified into family 78 of glycoside hydrolases and characterized by the presence of Asp567 and Glu841 in their active site. Optimization of fermentation conditions and enzyme engineering will allow the development of improved rhamnosidases for advancing suggested industrial applications.
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