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Characterization and crystal structure of a novel zearalenone hydrolase from Cladophialophora bantiana
Author(s) -
Hui Renjie,
Hu Xiangying,
Liu Wenting,
Liu Weidong,
Zheng Yingying,
Chen Yun,
Guo Rey-Ting,
Jin Jian,
Chen Chun-Chi
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17011840
Subject(s) - characterization (materials science) , zearalenone , chemistry , biology , materials science , botany , nanotechnology , fusarium
Zearalenone (ZEN) is a mycotoxin which causes huge economic losses in the food and animal feed industries. The lactonase ZHD101 from Clonostachys rosea , which catalyzes the hydrolytic degradation of ZEN, is the only known ZEN‐detoxifying enzyme. Here, a protein homologous to ZHD101, denoted CbZHD, from Cladophialophora batiana was expressed and characterized. Sequence alignment indicates that CbZHD possesses the same catalytic triad and ZEN‐interacting residues as found in ZHD101. CbZHD exhibits optimal enzyme activity at 35°C and pH 8, and is sensitive to heat treatment. The crystal structure of apo CbZHD was determined to 1.75 Å resolution. The active‐site compositions of CbZHD and ZHD101 were analyzed.