2022
DOI: 10.1016/j.bej.2022.108418
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The replacement of main cap domain to improve the activity of a ZEN lactone hydrolase with broad substrate spectrum

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Cited by 9 publications
(12 citation statements)
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“…The V max (maximum velocity) and k cat (catalytic constant) were determined as 125.9 μM/min and 46.8 min –1 , respectively, resulting in a calculated k cat / K m (catalytic efficiency) of 0.203 μM –1 s –1 . This catalytic efficiency of ZENM was notably higher than that of ZHD11B . ZENM demonstrated excellent substrate affinity, displaying remarkably high efficiency in degrading ZEN (100% degradation of ZEN in 3 min).…”
Section: Resultsmentioning
confidence: 91%
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“…The V max (maximum velocity) and k cat (catalytic constant) were determined as 125.9 μM/min and 46.8 min –1 , respectively, resulting in a calculated k cat / K m (catalytic efficiency) of 0.203 μM –1 s –1 . This catalytic efficiency of ZENM was notably higher than that of ZHD11B . ZENM demonstrated excellent substrate affinity, displaying remarkably high efficiency in degrading ZEN (100% degradation of ZEN in 3 min).…”
Section: Resultsmentioning
confidence: 91%
“…The specific activities of ZHD11B toward ZEN, α-ZOL, β-ZOL, and α-ZAL were reported as 16.4, 11.9, 2.9, and 17.2 U/mg, respectively . On the other hand, ZHD101 showed a degradation efficiency of only 45% toward α-ZOL compared to its efficiency for ZEN degradation .…”
Section: Resultsmentioning
confidence: 96%
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“…Zearalenone degradation by ZHD is a hydrolysis reaction, and the reaction substrate is ZEN and water [ 25 ]. However, since the concentration of water changes little during the reaction process, it can be treated as a constant, so the reaction can be regarded as a single substrate enzyme catalyzed reaction.…”
Section: Resultsmentioning
confidence: 99%