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  • Sortase A-mediated crosslinked short-chain dehydrogenases/reductases as novel biocatalysts with improved thermostability and catalytic efficiency.

Sortase A-mediated crosslinked short-chain dehydrogenases/reductases as novel biocatalysts with improved thermostability and catalytic efficiency.

Scientific reports (2017-06-10)
Kunpeng Li, Rongzhen Zhang, Yan Xu, Zhimeng Wu, Jing Li, Xiaotian Zhou, Jiawei Jiang, Haiyan Liu, Rong Xiao
ABSTRACT

(S)-carbonyl reductase II (SCRII) from Candida parapsilosis is a short-chain alcohol dehydrogenase/reductase. It catalyses the conversion of 2-hydroxyacetophenone to (S)-1-phenyl-1,2-ethanediol with low efficiency. Sortase was reported as a molecular "stapler" for site-specific protein conjugation to strengthen or add protein functionality. Here, we describe Staphylococcus aureus sortase A-mediated crosslinking of SCRII to produce stable catalysts for efficient biotransformation. Via a native N-terminal glycine and an added GGGGSLPETGG peptide at C-terminus of SCRII, SCRII subunits were conjugated by sortase A to form crosslinked SCRII, mainly dimers and trimers. The crosslinked SCRII showed over 6-fold and 4-fold increases, respectively, in activity and k

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
1-Phenyl-1,2-ethanediol, 97%
Sigma-Aldrich
4′-Methoxyacetophenone, 99%
Sigma-Aldrich
3′-Chloroacetophenone, 98%
Sigma-Aldrich
4′-Bromoacetophenone, 98%
Sigma-Aldrich
2-Hydroxyacetophenone, 98%
Sigma-Aldrich
2′-Chloroacetophenone, 97%
Sigma-Aldrich
Valerophenone, 99%
Sigma-Aldrich
3′-Methylacetophenone, 98%