Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation.

Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation.
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DOI:
10.1021/ja9046697
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发表时间:
2009-11-04
影响因子:
15
通讯作者:
Montclare, Jin Kim
Montclare, Jin Kim
中科院分区:
化学1区
文献类型:
--
作者:
Liu, Zhiqiang;Gosser, Yuying;Baker, Peter James;Ravee, Yaniv;Lu, Ziying;Alemu, Girum;Li, Huiguang;Butterfoss, Glenn L.;Kong, Xiang-Peng;Gross, Richard;Montclare, Jin Kim

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Cutinases are responsible for hydrolysis of the protective cutin lipid polyester matrix in plants and thus have been exploited for hydrolysis of small molecule esters and polyesters. Here we explore the reactivity, stability, and structure of Aspergillus oryzae cutinase and compare it to the well-studied enzyme from Fusarium solani. Two critical differences are highlighted in the crystallographic analysis of the A. oryzae structure: (i) an additional disulfide bond and (ii) a topologically favored catalytic triad with a continuous and deep groove. These structural features of A. oryzae cutinase are proposed to result in improved hydrolytic activity and altered substrate specificity profile, enhanced thermostability and remarkable reactivity towards the degradation of the synthetic polyester, polycaprolactone. The results presented here provide insight into engineering new cutinase-inspired biocatalysts with tailor-made properties.
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影响因子: 3
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