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柚苷酶的研究进展:结构与生物技术方面。

Updates on naringinase: structural and biotechnological aspects.

机构信息

Centre for Biotechnology, Chemistry and System Biology (Biodeakin), Institute of Technology Research and Innovation (ITRI), Deakin University, Warrnambool, Victoria, Australia.

出版信息

Appl Microbiol Biotechnol. 2012 Jan;93(1):49-60. doi: 10.1007/s00253-011-3679-3. Epub 2011 Nov 13.

DOI:10.1007/s00253-011-3679-3
PMID:22080346
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.

摘要

近年来,由于其水解活性,包括产生鼠李糖、普鲁宁和柑橘果汁脱苦,柚皮苷酶引起了极大的关注。虽然这种酶广泛分布于真菌中,但细菌来源的酶的生产却鲜为人知。真菌柚皮苷酶非常重要,因为它们在工业上大量使用,并在过去十年中得到了广泛的研究。本文讨论了细菌柚皮苷酶的生产及其潜在的生物技术应用。细菌鼠李糖苷酶是外切酶,可从含有α-L-鼠李糖的多糖和糖苷中水解末端非还原α-L-鼠李糖基。在结构上,它们被分类为糖苷水解酶家族 78,并以其活性部位存在 Asp567 和 Glu841 为特征。发酵条件的优化和酶工程将允许开发改进的鼠李糖苷酶,以推进建议的工业应用。

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