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

Shanshan Pei; Xiaobo Ruan; Jia Liu; Wei Song; Xiulai Chen; Qiuling Luo; Liming Liu; Jing Wu

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

Biotechnology and Bioengineering | Updated：2026-01-06

- Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis
- Chinese Journal of Chemical Engineering Vol. 28, Issue 8, Pages: 2190-2199(2020)
- Affiliations：
  
  1. School of Pharmaceutical Science, Jiangnan University,Wuxi,China,214122
  2. Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University,Wuxi,China,214122
  3. State Key Laboratory of Food Science and Technology, Jiangnan University,Wuxi,China,214122
  4. National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University,Wuxi,China,214122
- Author bio：
- Funds：
- DOI：
  CLC：
- Published：2020
- Accepted：
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[J]. 中国化学工程学报, 2020, 28(8): 2190-2199.
DOI：

[J]. 中国化学工程学报, 2020, 28(8): 2190-2199. DOI：

摘要

Abstract

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 production. In 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 inhibition. The four mutant PM-LAAD

(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

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 bio

conversion method

and also provide the understanding of the mechanism of the relieved product inhibition of PM-LAAD.

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⁰

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

DOI：

摘要

Abstract

关键词

Keywords

references