Literature DB >> 25272752

[Novel immobilization of arginase I via cellulose-binding domain and its application in producing of L-ornitine].

M Li, J Iang, H Qu, Q Zhang, F Bai, G Bai.   

Abstract

The recombinant Escherichia coli strain pET35b-ARG, which overexpresses arginase I fused to a cellulose-binding domain (CBD), was developed. After preparing cellulose microspheres, arginase I was immobilized via the CBD of the fusion protein. Under optimal reaction conditions (40 degrees C, pH 9.5, 1 mM of Mn2+, 30 microl/ml of immobilized enzyme, 30 g/l of L-Arg, and for I h), the conversion rate of L-Arg was 98.7%. After 7 reuses of 30 microl of immobilized enzyme in 1 ml of catalytic solution, 153 mg of L-Orn with 97.3% purity was obtained. This indicated that the immobilization method was effective, feasible and could be used for the industrial production of L-Orn in the future.

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Year:  2014        PMID: 25272752

Source DB:  PubMed          Journal:  Prikl Biokhim Mikrobiol        ISSN: 0555-1099


  1 in total

1.  High-level expression of human arginase I in Pichia pastoris and its immobilization on chitosan to produce L-ornithine.

Authors:  Xue Zhang; Jin Liu; Xianhong Yu; Fei Wang; Li Yi; Zhezhe Li; Yunyun Liu; Lixin Ma
Journal:  BMC Biotechnol       Date:  2015-07-31       Impact factor: 2.563

  1 in total

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