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球毛壳菌重组辅助活性9与纤维素酶在纤维素水解中协同作用的优化

Optimization of synergism of a recombinant auxiliary activity 9 from Chaetomium globosum with cellulase in cellulose hydrolysis.

作者信息

Kim In Jung, Nam Ki Hyun, Yun Eun Ju, Kim Sooah, Youn Hak Jin, Lee Hee Jin, Choi In-Geol, Kim Kyoung Heon

机构信息

Department of Biotechnology, Korea University Graduate School, Seoul, 136-713, Republic of Korea.

Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, 790-784, Republic of Korea.

出版信息

Appl Microbiol Biotechnol. 2015 Oct;99(20):8537-47. doi: 10.1007/s00253-015-6592-3. Epub 2015 May 5.

DOI:10.1007/s00253-015-6592-3
PMID:25936375
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4768223/
Abstract

Auxiliary activity family 9 (AA9, formerly known as glycoside hydrolase family 61 or polysaccharide monooxygenase) is a group of fungal proteins that were recently found to have a significant synergism with cellulase in cellulose hydrolysis via the oxidative cleavage of glycosidic bonds of cellulose chains. In this study, we report the active expression of a recombinant fungal AA9 from Chaetomium globosum (CgAA9) in a bacterial host, Escherichia coli, and the optimization of its synergistic activity in cellulose hydrolysis by using cellulase. The recombinant CgAA9 (0.9 mg/g cellulose) exhibited 1.7-fold synergism in the hydrolysis of Avicel when incubated with 0.9 filter paper units of Celluclast 1.5 L/g cellulose. The first study of the active expression of AA9 using a bacterial host and its synergistic optimization could be useful for the industrial application of AA9 for the saccharification of lignocellulose.

摘要

辅助活性家族9(AA9,以前称为糖苷水解酶家族61或多糖单加氧酶)是一组真菌蛋白,最近发现它们通过氧化裂解纤维素链的糖苷键,在纤维素水解过程中与纤维素酶具有显著的协同作用。在本研究中,我们报道了来自球毛壳菌的重组真菌AA9(CgAA9)在细菌宿主大肠杆菌中的活性表达,以及通过使用纤维素酶对其在纤维素水解中的协同活性进行优化。当与0.9滤纸单位的纤维素酶Celluclast 1.5 L/g纤维素一起孵育时,重组CgAA9(0.9 mg/g纤维素)在微晶纤维素水解中表现出1.7倍的协同作用。首次利用细菌宿主对AA9进行活性表达及其协同优化的研究,可能有助于AA9在木质纤维素糖化工业应用中的应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/d94e21d0b21b/253_2015_6592_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/e5679fbf1b43/253_2015_6592_Fig1_HTML.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/d95d4d293b08/253_2015_6592_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/f5666ae81270/253_2015_6592_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/458753b2f20b/253_2015_6592_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/d94e21d0b21b/253_2015_6592_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/e5679fbf1b43/253_2015_6592_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/bcdfe75a2bd9/253_2015_6592_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/acdbd8283fe2/253_2015_6592_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/d95d4d293b08/253_2015_6592_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/f5666ae81270/253_2015_6592_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/458753b2f20b/253_2015_6592_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a17/4768223/d94e21d0b21b/253_2015_6592_Fig7_HTML.jpg

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