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Title: Structural and Functional Studies of Aspergillus oryzae Cutinase: Enhanced Thermostability and Hydrolytic Activity of Synthetic Ester and Polyester Degradation

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.

Authors:
; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
DOE - OFFICE OF SCIENCE
OSTI Identifier:
1019828
Report Number(s):
BNL-95674-2011-JA
Journal ID: ISSN 0002-7863; JACSAT; TRN: US201115%%464
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 131; Journal Issue: 43; Journal ID: ISSN 0002-7863
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ASPERGILLUS; DISULFIDES; ENZYMES; ESTERS; FUNCTIONALS; FUSARIUM; HYDROLYSIS; LIPIDS; POLYESTERS; SPECIFICITY; STABILITY; SUBSTRATES; national synchrotron light source

Citation Formats

Liu, Z, Gosser, Y, Baker, P, Ravee, Y, Li, H, Butterfoss, G, Kong, X, Gross, R, Montclare, J, and et al. Structural and Functional Studies of Aspergillus oryzae Cutinase: Enhanced Thermostability and Hydrolytic Activity of Synthetic Ester and Polyester Degradation. United States: N. p., 2009. Web. doi:10.1021/ja9046697.
Liu, Z, Gosser, Y, Baker, P, Ravee, Y, Li, H, Butterfoss, G, Kong, X, Gross, R, Montclare, J, & et al. Structural and Functional Studies of Aspergillus oryzae Cutinase: Enhanced Thermostability and Hydrolytic Activity of Synthetic Ester and Polyester Degradation. United States. doi:10.1021/ja9046697.
Liu, Z, Gosser, Y, Baker, P, Ravee, Y, Li, H, Butterfoss, G, Kong, X, Gross, R, Montclare, J, and et al. Thu . "Structural and Functional Studies of Aspergillus oryzae Cutinase: Enhanced Thermostability and Hydrolytic Activity of Synthetic Ester and Polyester Degradation". United States. doi:10.1021/ja9046697.
@article{osti_1019828,
title = {Structural and Functional Studies of Aspergillus oryzae Cutinase: Enhanced Thermostability and Hydrolytic Activity of Synthetic Ester and Polyester Degradation},
author = {Liu, Z and Gosser, Y and Baker, P and Ravee, Y and Li, H and Butterfoss, G and Kong, X and Gross, R and Montclare, J and et al.},
abstractNote = {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.},
doi = {10.1021/ja9046697},
journal = {Journal of the American Chemical Society},
issn = {0002-7863},
number = 43,
volume = 131,
place = {United States},
year = {2009},
month = {1}
}