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Synthesis and sensory characteristics of kokumi #-[Glu]n-Phe in the presence of glutamine and phenylalanine: Glutaminase from Bacillus amyloliquefaciens or Aspergillus oryzae as the catalyst Juan Yang, Dongxiao Sun-Waterhouse, Chun Cui, Keming Dong, and Wei Wang J. Agric. Food Chem., Just Accepted Manuscript • DOI: 10.1021/acs.jafc.7b03419 • Publication Date (Web): 13 Sep 2017 Downloaded from http://pubs.acs.org on September 13, 2017
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Journal of Agricultural and Food Chemistry is published by the American Chemical Society. 1155 Sixteenth Street N.W., Washington, DC 20036 Published by American Chemical Society. Copyright © American Chemical Society. However, no copyright claim is made to original U.S. Government works, or works produced by employees of any Commonwealth realm Crown government in the course of their duties.
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Journal of Agricultural and Food Chemistry
Synthesis and sensory characteristics of kokumi γ-[Glu]n-Phe in the presence of
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glutamine and phenylalanine: Glutaminase from Bacillus amyloliquefaciens or Aspergillus
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oryzae as the catalyst
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Juan Yanga, Dongxiao Sun-Waterhousea, Chun Cuia*, Keming Dongb, Wei Wanga
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School of food science and engineering, South China University of Technology, Guangzhou 510640, China
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Guangdong Weiwei Biotechnology Co., LTD., Guangzhou 510640, China
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Corresponding author: Chun Cui, PhD. Tel: +86 20 87114954; Fax: +86 20 87114954; E-mail:
[email protected] First author: Juan Yang, PhD. Tel: +86 20 87114954; Fax: +86 20 87114954; E-mail:
[email protected] 1
ACS Paragon Plus Environment
Journal of Agricultural and Food Chemistry
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ABSTRACT:
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The transpeptidase activity of glutaminase from Bacillus amyloliquefaciens (GBA) and
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Aspergillus oryzae (GAO) to yield γ-[Glu]n-Phe peptides were verified for the first time. In the
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presence of Gln and Phe, γ-Glu-Phe and γ-Glu-γ-Glu-Phe were synthesized by GAO, and
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γ-Glu-Phe,
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γ-Glu-γ-Glu-γ-Glu-γ-Glu-γ-Glu-Phe were synthesized by GBA. The Km values for the
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transpeptidation catalysed by GBA and GAO were 47.88 and 153.92 mM (Phe as the acceptor),
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84.89 and 236.47 mM (γ-Glu-Phe as the acceptor), indicating that GBA had a greater affinity than
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GAO for Phe and γ-Glu-Phe in the transpeptidation reaction. The Km values for the
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transpeptidation catalysed by GBA against acceptors, Phe and γ-[Glu](1≦n
