Hydrolysis of citrus peel naringin by recombinant α-L-rhamnosidase from Clostridium stercorarium

被引:38
作者
Kaur, Aneet [2 ]
Singh, Satbir [2 ]
Singh, Ram S. [2 ]
Schwarz, W. H. [3 ]
Puri, Munish [1 ,2 ]
机构
[1] Deakin Univ, Ctr Biotechnol & Multidisciplinary Sci Biodeakin, Inst Technol Res & Innovat ITRI, Geelong, Vic 3217, Australia
[2] Punjabi Univ, Fermentat & Prot Biotechnol Lab, Dept Biotechnol, Patiala, Punjab, India
[3] Tech Univ Munich, Dept Microbiol, D-85350 Freising Weihenstephan, Germany
关键词
recombinant rhamnosidase; Clostridium stercorarium; citrus peel waste; naringin; rhamnose; ORANGE PEEL; PURIFICATION; WASTE; HYDROLASE;
D O I
10.1002/jctb.2433
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The citrus fruit processing industry generates substantial quantities of waste rich in glycosylated phenolic substances such as naringin, which are a valuable natural source of polyphenols as well as L-rhamnopyranose. Naringin is the major polyphenol in bitter orange peel and its hydrolysis by alpha-L-rhamnosidase (EC 3.2.1.40) catalyzes the cleavage of the terminal rhamnosyl groups to form prunin and rhamnose. In this work, a recombinant alpha-L-rhamnosidase from C. stercorarium was shown to be suitable for narigin hydrolysis. The recombinant rhamnosidase was found to be relatively stable at 60 degrees C, and a residual activity close to 50% after 180 min of incubation was demonstrated. The purified enzyme established hydrolysis of naringin extracted from citrus peel waste (CPW). The result indicated that recombinant alpha-L-rhamnosidase has industrial applicability and is an interesting candidate for producing rhamnose from citrus peel. (C) 2010 Society of Chemical Industry
引用
收藏
页码:1419 / 1422
页数:4
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