BioChem - DOS

Combination of site-directed mutagenesis and yeast surface display enhances Rhizomucor miehei lipase esterification activity in organic solvent

Biotechnology letters. : a monthly journal for the rapid communication of results and developments in all aspects of biotechnology

Han, Shuang-yan; Zhang, Jun-hui; Han, Zhen-lin; Zheng, Sui-ping; Lin, Ying

<P>To increase the activity of Rhizomucor miehei lipase (RML) in organic solvent, multiple sequence alignments and rational site-directed mutagenesis were used to create RML variants. The obtained proteins were surface-displayed on Pichia pastoris by fusion to Flo1p as an anchor protein. The synthetic activity of four variants showed from 1.1- to 5-fold the activity of native lipase in an esterification reaction in heptane with alcohol and caproic acid as substrates. The increase in esterification activity may be attributed to the four mutations changing the flexibility of RML or facilitating the reaction. In conclusion, this method demonstrated that multiple sequence alignments and rational site-directed mutagenesis combined with yeast display technology is a faster and more effective means of obtaining high-efficiency esterification lipase variants compared with previous similar methods.</P>

2011

Springer-Verlag

0141-5492

1573-6776

33

12

pp.2431-2438

10.1007/s10529-011-0705-6

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