GIEC OpenIR
The inhibitory effect of xylan on enzymatic hydrolysis of cellulose is dependent on cellulose ultrastructure
Chen, Xindong1,2; Xiong, Lian1,3,4,5; Li, Hailong1,3,4,5; Zhang, Liquan1,2; Yuan, Ge1,2; Chen, Xuefang1,3,4,5; Wang, Can1,3,4,5; Chen, Xinde1,3,4,5
2020-05-01
发表期刊CELLULOSE
ISSN0969-0239
卷号27期号:8页码:4417-4428
通讯作者Li, Hailong(lihl@ms.giec.ac.cn) ; Chen, Xinde(cxd_cxd@hotmail.com)
摘要The inhibitory effect of xylan on enzymatic hydrolysis of cellulose with different ultrastructure is not clear. In this work, cellulose II, cellulose III, and amorphous cellulose were prepared from cellulose I by NaOH, ethylenediamine, and ball-milling treatment, respectively. Their crystalline structure and enzymatic hydrolyzability were systematically characterized and compared with cellulose I. Furthermore, the inhibitory effect of xylan on cellulose with different ultrastructure was investigated in detail. Results suggested that the enzymatic hydrolyzability of different cellulose increased in sequence from cellulose I (25.4%), cellulose III (41.7%), cellulose II (56.2%) to amorphous cellulose (77.4%) at enzyme loadings of 5.56 mg protein/g substrate. The enzymatic hydrolyzability of allomorphic cellulose was strongly inhibited by xylan, while a little inhibition was observed for amorphous cellulose. It was found that cellobiose released from different cellulose was decreased after the addition of xylan. At the initial hydrolysis stage, the inhibition degree was obviously increased for all of different cellulose, and then, the inhibition degree of cellulose I and cellulose II gradually decreased as enzymatic hydrolysis proceeded, while the inhibition degree of cellulose III and amorphous cellulose had changed a little. In addition, at a longer time of hydrolysis, the inhibition degree was decreased with the increase of cellulase dosage except for cellulose III, which remained approximately unchanged. Overall, this study demonstrated that the inhibitory effect of xylan on cellulose hydrolysis was substantially affected by the ultrastructure of cellulose, and thus it provides new insights for relieving the inhibitory effect of xylan by altering the ultrastructure of cellulose.
关键词Cellulose Xylan inhibition Enzymatic hydrolysis Cellulase
DOI10.1007/s10570-020-03087-9
关键词[WOS]AMMONIA PRETREATMENT ; ENZYMES ; LIGNOCELLULOSE ; LIGNIN ; RECALCITRANCE ; EFFICIENCY ; CONVERSION ; ALLOMORPH
收录类别SCI
语种英语
WOS研究方向Materials Science ; Polymer Science
WOS类目Materials Science, Paper & Wood ; Materials Science, Textiles ; Polymer Science
WOS记录号WOS:000528396300018
出版者SPRINGER
引用统计
被引频次:17[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.giec.ac.cn/handle/344007/26801
专题中国科学院广州能源研究所
通讯作者Li, Hailong; Chen, Xinde
作者单位1.Chinese Acad Sci, Guangzhou Inst Energy Convers, 2 Energy Rd, Guangzhou 510640, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.CAS Key Lab Renewable Energy, Guangzhou 510640, Peoples R China
4.Guangdong Prov Key Lab New & Renewable Energy Res, Guangzhou 510640, Peoples R China
5.Chinese Acad Sci, R&D Ctr Xuyi Attapulgite Appl Technol, Guangzhou Inst Energy Convers, Xuyi 211700, Peoples R China
第一作者单位中国科学院广州能源研究所
推荐引用方式
GB/T 7714
Chen, Xindong,Xiong, Lian,Li, Hailong,et al. The inhibitory effect of xylan on enzymatic hydrolysis of cellulose is dependent on cellulose ultrastructure[J]. CELLULOSE,2020,27(8):4417-4428.
APA Chen, Xindong.,Xiong, Lian.,Li, Hailong.,Zhang, Liquan.,Yuan, Ge.,...&Chen, Xinde.(2020).The inhibitory effect of xylan on enzymatic hydrolysis of cellulose is dependent on cellulose ultrastructure.CELLULOSE,27(8),4417-4428.
MLA Chen, Xindong,et al."The inhibitory effect of xylan on enzymatic hydrolysis of cellulose is dependent on cellulose ultrastructure".CELLULOSE 27.8(2020):4417-4428.
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Chen, Xindong]的文章
[Xiong, Lian]的文章
[Li, Hailong]的文章
百度学术
百度学术中相似的文章
[Chen, Xindong]的文章
[Xiong, Lian]的文章
[Li, Hailong]的文章
必应学术
必应学术中相似的文章
[Chen, Xindong]的文章
[Xiong, Lian]的文章
[Li, Hailong]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。