Exploration of the key functional proteins from an efficient cellulolytic microbial consortium using dilution-to-extinction approach

In the present study, the cellulose binding proteins（CBPs） secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis（SDS-PAGE）. Using mass spect...

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Published in	Journal of environmental sciences (China) Vol. 43; no. 5; pp. 199 - 207
Main Authors	Zhang, Qinghua, Li, Hanguang, Zhu, Xiangdong, Lai, Fenju, Zhai, Zhijun, Wang, Yuanxiu
Format	Journal Article
Language	English
Published	Netherlands Elsevier B.V 01.05.2016
Subjects	active sites Bacterial Proteins - genetics binding proteins Cellulolytic cellulose Cellulose - metabolism Cellulose binding protein Clostridium digestion Dilution-to-extinction approach Electrophoresis, Polyacrylamide Gel enzyme activity glycosides Microbial Consortia Microbial consortium Paenibacillus polyacrylamide gel electrophoresis SDS-PAGE xylanases 催化结构域微生物稀释法纤维素分解纤维结合蛋白绝迹聚丙烯酰胺凝胶电泳 Dilution-to-extinction approach Cellulolytic Microbial consortium Cellulose binding protein
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ISSN	1001-0742 1878-7320
DOI	10.1016/j.jes.2015.09.003

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Abstract	In the present study, the cellulose binding proteins（CBPs） secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis（SDS-PAGE）. Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6（97 k Da） and 12（52 k Da） were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families（GH） 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose.
AbstractList	In the present study, the cellulose binding proteins（CBPs） secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis（SDS-PAGE）. Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6（97 k Da） and 12（52 k Da） were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families（GH） 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose. In the present study, the cellulose binding proteins (CBPs) secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE). Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6 (97kDa) and 12 (52kDa) were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families (GH) 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose. In the present study, the cellulose binding proteins (CBPs) secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE). Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6 (97kDa) and 12 (52kDa) were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families (GH) 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose. The efficient cellulolytic ability of a previously constructed microbial consortium was found to be correlated to the cellulose binding proteins (CBPs 6 and 12, which containing glycoside hydrolase families 9 and 48 catalytic modules respectively), and these two proteins can synergistically promote the efficient degradation of cellulose. [Display omitted] In the present study, the cellulose binding proteins (CBPs) secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6 (97 kDa) and 12 (52 kDa) were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families (GH) 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose. In the present study, the cellulose binding proteins (CBPs) secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6 (97kDa) and 12 (52kDa) were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families (GH) 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose.In the present study, the cellulose binding proteins (CBPs) secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6 (97kDa) and 12 (52kDa) were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families (GH) 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose.
Author	Qinghua Zhang Hanguang Li Xiangdong Zhu Fenju Lai Zhijun Zhai Yuanxiu Wang
AuthorAffiliation	Collefe of Bioscience and Enfineering, Jiangxi Enfineerin9 Laboratory for the Deuelopment and Utilization of Agricultural Microbial Resources,Jiangxi Agricultural University, Nanehan9 330045, China
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Notes	In the present study, the cellulose binding proteins（CBPs） secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis（SDS-PAGE）. Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6（97 k Da） and 12（52 k Da） were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families（GH） 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose. Microbial consortium Cellulolytic Cellulose binding protein Dilution-to-extinction approach 11-2629/X ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
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Snippet	In the present study, the cellulose binding proteins（CBPs） secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity... In the present study, the cellulose binding proteins (CBPs) secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity...
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SubjectTerms	active sites Bacterial Proteins - genetics binding proteins Cellulolytic cellulose Cellulose - metabolism Cellulose binding protein Clostridium digestion Dilution-to-extinction approach Electrophoresis, Polyacrylamide Gel enzyme activity glycosides Microbial Consortia Microbial consortium Paenibacillus polyacrylamide gel electrophoresis SDS-PAGE xylanases 催化结构域微生物稀释法纤维素分解纤维结合蛋白绝迹聚丙烯酰胺凝胶电泳
Title	Exploration of the key functional proteins from an efficient cellulolytic microbial consortium using dilution-to-extinction approach
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