Hongbo Liang

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The NADPH-dependent (S)-carbonyl reductaseII from Candida parapsilosis catalyzes acetophenone to chiral phenylethanol in a very low yield of 3.2%. Site-directed mutagenesis was used to design two mutants Ala220Asp and Glu228Ser, inside or adjacent to the substrate-binding pocket. Both mutations caused a significant enantioselectivity shift toward(More)
Starch debranching is fundamental for understanding the structure-function relationships of starch. In this paper, atomic force microscopy (AFM) was used to investigate potato starch by isoamylase [EC] debranching at nanometer scale. The hydrolysates were separated by gel-permeation chromatography and the fractions were imaged. In addition to(More)
OBJECTIVE To realize efficient biotransformation of (S)-1-phenyl-1,2-ethanediol by recombinant (S)-carbonyl reductase II, we expressed (S)- carbonyl reductase II from Candida parapsilosis CCTCC M203011 and embedded it in the spores of Saccharomyces cerevisiae AN120. METHODS (S)-carbonyl reductase II gene was cloned from C. parapsilosis genome and(More)
BACKGROUND Candida parapsilosis (R)-carbonyl reductase (RCR) and (S)-carbonyl reductase (SCR) are involved in the stereoconversion of racemic (R,S)-1-phenyl-1,2-ethanediol (PED) to its (S)-isomer. RCR catalyzes (R)-PED to 2-hydroxyacetophenone (2-HAP), and SCR catalyzes 2-HAP to (S)-PED. However, the stereoconversion efficiency of racemic mixture to (S)-PED(More)
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