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Enzymatic production of 5'-inosinic acid by a newly synthesised acid phosphatase/phosphotransferase.
MedLine Citation:
PMID:  23107712     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
5'-Nucleotides including 5'-inosinic acid have characteristic taste and important application in various foods as flavour potentiators. The selective nucleoside acid phosphatase/phosphotransferase (AP/PTase) can catalyse the synthesis of 5'-nucleotides by transfer of phosphate groups. In this study, a 747-bp gene encoding AP/PTase from Escherichia blattae was synthesised. After expression, the recombinant AP/PTase was purified using nickel-NTA. The optimal temperature and pH of this enzyme were 30°C and 5.0, respectively. The activity was partially inhibited by metal ions such as Hg(2+), Ag(+) and Cu(2+), but not by chelating reagents such as EDTA. The values of K(m) and V(max) for inosine were 40mM and 3.5U/mg, respectively. Using this purified enzyme, 16.83mM of 5'-IMP was synthesised from 37mM of inosine and the molar yield reached 45.5%. Homology modelling and docking simulation were discussed.
Authors:
Zhi-Qiang Liu; Ling Zhang; Li-Hui Sun; Xiao-Jun Li; Nan-Wei Wan; Yu-Guo Zheng
Publication Detail:
Type:  Journal Article     Date:  2012-03-08
Journal Detail:
Title:  Food chemistry     Volume:  134     ISSN:  0308-8146     ISO Abbreviation:  Food Chem     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-10-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7702639     Medline TA:  Food Chem     Country:  England    
Other Details:
Languages:  eng     Pagination:  948-56     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
Affiliation:
Institute of Bioengineering, Zhejiang University of Technology, Hangzhou 310014, People's Republic of China.
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