| Enzymatic production of 5'-inosinic acid by a newly synthesised acid phosphatase/phosphotransferase. | |
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MedLine Citation:
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PMID: 23107712 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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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. |
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Authors:
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Zhi-Qiang Liu; Ling Zhang; Li-Hui Sun; Xiao-Jun Li; Nan-Wei Wan; Yu-Guo Zheng |
Publication Detail:
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Type: Journal Article Date: 2012-03-08 |
Journal Detail:
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Title: Food chemistry Volume: 134 ISSN: 0308-8146 ISO Abbreviation: Food Chem Publication Date: 2012 Sep |
Date Detail:
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Created Date: 2012-10-30 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7702639 Medline TA: Food Chem Country: England |
Other Details:
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Languages: eng Pagination: 948-56 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Elsevier Ltd. All rights reserved. |
Affiliation:
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Institute of Bioengineering, Zhejiang University of Technology, Hangzhou 310014, People's Republic of China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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