Clean Production of l-Alanyl-l-glutamine by an Efficient Yeast Biocatalyst Expressing α-Amino Acid Ester Acyltransferase without N-Glycosylation

Biocatalysis
DOI: 10.1021/acs.jafc.3c00669 Publication Date: 2023-04-07T20:02:00Z
ABSTRACT
l-Alanyl-l-glutamine (Ala-Gln) is a widely used value-added dipeptide whose production relies heavily upon an efficient biocatalyst. The currently available yeast biocatalysts that express α-amino acid ester acyltransferase (SsAet) possess relatively low activity, which may be attributed to glycosylation. Here, promote SsAet activity in yeast, we identified the N-glycosylation site as Asn residue at position 442 and subsequently eliminated negative effect of on by removing artificial native signal peptides obtain K3A1, novel biocatalyst with significantly improved activity. Additionally, optimal reaction conditions strain K3A1 were determined (25 °C, pH 8.5, AlaOMe/Gln = 1:2), resulting maximum molar yield productivity approximately 80% 1.74 g·(L·min)-1, respectively. Therefore, developed promising system cleanly produce Ala-Gln safe, efficient, sustainable manner, contribute future industrial Ala-Gln.
SUPPLEMENTAL MATERIAL
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