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

Liu Zhiqiang, Yuying Gosser, Peter James Baker, Yaniv Ravee, Lu Ziying, Girum Alemu, Li Huiguang, Glenn L. Butterfoss, Xiang Peng Kong, Richard Gross, Jin Kim Montclare

Research output: Contribution to journalArticle

Abstract

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 an improved hydrolytic activity and altered substrate specificity profile, enhanced thermostability, and remarkable reactivity toward the degradation of the synthetic polyester polycaprolactone. The results presented here provide insight into engineering new cutinase-inspired biocatalysts with tailor-made properties.

Original languageEnglish (US)
Pages (from-to)15711-15716
Number of pages6
JournalJournal of the American Chemical Society
Volume131
Issue number43
DOIs
StatePublished - Nov 4 2009

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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