Enzymatic Production ofL-Alanyl-L-glutamine by RecombinantE. coliExpressing α-Amino Acid Ester Acyltransferase fromSphingobacterium siyangensis | Zendy

Yoshinori Hirao | Zendy; Yasuhiro Mihara | Zendy; Ikuo Kira | Zendy; Isao Abe | Zendy; Kenzo Yokozeki | Zendy

Open Access

Enzymatic Production ofL-Alanyl-L-glutamine by RecombinantE. coliExpressing α-Amino Acid Ester Acyltransferase fromSphingobacterium siyangensis

Author(s) -

Yoshinori Hirao,

Yasuhiro Mihara,

Ikuo Kira,

Isao Abe,

Kenzo Yokozeki

Publication year - 2013

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.120859

Subject(s) - glutamine , enzyme , escherichia coli , chemistry , yield (engineering) , biochemistry , acyltransferase , recombinant dna , molar ratio , amino acid , gene , materials science , metallurgy , catalysis

An enzymatic production method for synthesizing L-alanyl-L-glutamine (Ala-Gln) from L-alanine methyl ester hydrochloride (AlaOMe) and L-glutamine (Gln) was developed in this study. The cultivation conditions for an Escherichia coli strain overexpressing α-amino acid ester acyltransferase from Sphingobacterium siyangensis AJ 2458 (SAET) and reaction conditions for Ala-Gln production were optimized. A high cell density culture broth prepared by fed-batch cultivation showed 440 units/mL of Ala-Gln-producing activity. In addition, an Ala-Gln-producing reaction using intact E. coli cells overexpressing SAET under optimum conditions was conducted. A total Ala-Gln yield of 69.7 g/L was produced in 40 min. The molar yield was 67% against both AlaOMe and Gln.

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