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Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis

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Chinese Journal of Chemical Engineering 2020年第8期28卷 2190-2199页

作者： Shanshan Pei Xiaobo Ruan Jia Liu Wei Song Xiulai Chen Qiuling Luo Liming Liu Jing Wu School of Pharmaceutical Science Jiangnan UniversityWuxi 214122China Key Laboratory of Industrial Biotechnology Ministry of EducationJiangnan UniversityWuxi 214122China State Key Laboratory of Food Science and Technology Jiangnan UniversityWuxi 214122China National Engineering Laboratory for Cereal Fermentation Technology Jiangnan UniversityWuxi 214122China

L-Amino acid deaminase(LAAD) is a key enzyme in the deamination of L-valine(L-val) to produce α-ketoisovalerate(KIV). However, the product inhibition of LAAD is a major hindrance to industrial KIV *** the present study, a combination strategy of modification of flexible loop regions around the product binding site and the avoidance of dramatic change of main-chain dynamics was reported to reduce the product *** four mutant PM-LAAD^(M4)(PM-LAAD^(S98A/T105A/S106A/L341A)) achieved a 6.2-fold higher catalytic efficiency and an almost 6.7-fold reduction in product inhibition than the wild-type enzyme. Docking experiments suggested that weakened interactions between the product and enzyme, and the flexibility of the "lid" structure relieved LAAD product inhibition. Finally, the whole-cell biocatalyst PM-LAAD^(M4) has been applied to KIV production,the titer and conversion rate of KIV from L-val were 98.5 g·L^-1 and 99.2% at a 3-L scale, respectively. These results demonstrate that the newly engineered catalyst can significantly reduce the product inhibition, that making KIV a prospective product by bioconversion method, and also provide the understanding of the mechanism of the relieved product inhibition of PM-LAAD.

关键词： Product inhibition L-Amino acid deaminases α-ketoisovalerate Bio-catalysis Protein engineering

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