Effect of sulfonated lignin on enzymatic activity of the ligninolytic enzymes Cα-dehydrogenase LigD and β-etherase LigF
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- 作者：Chao Wanga ; chaow1990@yahoo.com" class="auth_mail" title="E-mail the corresponding author ; wangchao612@sina.com" class="auth_mail" title="E-mail the corresponding author ; Xianhong Ouyanga ; Sisi Sua ; Xiao Liangb ; Chao Zhanga ; Wenya Wanga ; wangwy@mail.buct.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Qipeng Yuana ; Qiang Lib
- 关键词：SL ; sulfonated lignin ; GGE ; guaiacylglycerol-β-guaiacyl ether ; NAD+ ; nicotinamide adenine dinucleotide ; NADH ; nicotinamide adenine dinucleotide hydrogen ; MPHPV ; α-(2-methoxyphenoxy)-β-hydroxypropiovanillone ; GSH ; glutathione ; GSSG ; oxidized glutathione ; GS-HPV ; α-glutathionyl-β-hydroxypropiovanillone ; LigD ; Cα-dehydrogenase ; LigF ; β-etherase ; SPR ; surface plasmon resonance ; ITC ; isothermal titration calorimetry ; GPC ; gel permeation chromatography ; Mw ; weight-average molecular weight
- 刊名：Enzyme and Microbial Technology
- 出版年：2016
- 出版时间：November 2016
- 年：2016
- 卷：93-94
- 期：Complete
- 页码：59-69
- 全文大小：3187 K
文摘
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Sulfonated lignin could inhibit the catalytic efficiency of β-etherase LigF significantly, not for Cα-dehydrogenase LigD.
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Sulfonated lignin samples with larger molecular weight had prior impact on the catalytic efficiency of β-etherase LigF.
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Hydrophobic interactions and ionic bond interactions were responsible for the increased adsorption of the enzymes to sulfonated lignin.
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Nonspecific adsorption between protein and sulfonated lignin with different molecular weights did exist.