Purification, characterization and function analysis of an extracellular β-glucosidase from elongating stipe cell walls in Coprinopsis cinerea. Issue 9 (29th March 2016)
- Record Type:
- Journal Article
- Title:
- Purification, characterization and function analysis of an extracellular β-glucosidase from elongating stipe cell walls in Coprinopsis cinerea. Issue 9 (29th March 2016)
- Main Title:
- Purification, characterization and function analysis of an extracellular β-glucosidase from elongating stipe cell walls in Coprinopsis cinerea
- Authors:
- Zhang, Wenming
Kang, Liqin
Yang, Mingmei
Zhou, Yajun
Wang, Jun
Liu, Zhonghua
Yuan, Sheng - Editors:
- Poeggeler, Stefanie
- Abstract:
- Abstract : A β-glycoside hydrolase was isolated from cell walls material in Coprinopsis cinerea elongating stipes. By analysis of SDS-PAGE, MALDI-TOF/TOF MS and substrate specificity, this enzyme was characterized as an extracellular β-glucosidase which is a trimer consisting of three homosubunits. β-Glucosidase did not degrade β-glucans with modified ends, whereas it hydrolyzed various β-glucans with free ends and related oligosaccharides with β-1, 3-, β-1, 4- or β-1, 6-linkages. Although this β-glucosidase possesses glycosyltransferase activity on laminarioligosaccharides, it did not transfer glucose residues from laminaritriose to β-glucan in stipe cell walls to produce larger β-glucan molecules; instead, it caused a decrease in the molecular size of stipe wall β-glucan by removing glucose. Relatively, the molecular size of wall β-glucans in the elongating apical stipe was less than that found in the non-elongating basal stipes, and this β-glucosidase was more highly expressed in the elongating apical stipe than in non-elongating basal regions. Therefore, we propose that β-glucosidase functions by trimming or cutting the β-glucan side chains on the β-1, 3-glucan backbone to prevent them from forming longer branches, keeping the wall plastic to promote diffuse wall growth. Abstract : The β-glucosidase from cell walls of Coprinopsis cinerea caused a decrease in the molecular size of stipe wall β-glucan, and may function by trimming or cutting the β-glucan side chains.Abstract : A β-glycoside hydrolase was isolated from cell walls material in Coprinopsis cinerea elongating stipes. By analysis of SDS-PAGE, MALDI-TOF/TOF MS and substrate specificity, this enzyme was characterized as an extracellular β-glucosidase which is a trimer consisting of three homosubunits. β-Glucosidase did not degrade β-glucans with modified ends, whereas it hydrolyzed various β-glucans with free ends and related oligosaccharides with β-1, 3-, β-1, 4- or β-1, 6-linkages. Although this β-glucosidase possesses glycosyltransferase activity on laminarioligosaccharides, it did not transfer glucose residues from laminaritriose to β-glucan in stipe cell walls to produce larger β-glucan molecules; instead, it caused a decrease in the molecular size of stipe wall β-glucan by removing glucose. Relatively, the molecular size of wall β-glucans in the elongating apical stipe was less than that found in the non-elongating basal stipes, and this β-glucosidase was more highly expressed in the elongating apical stipe than in non-elongating basal regions. Therefore, we propose that β-glucosidase functions by trimming or cutting the β-glucan side chains on the β-1, 3-glucan backbone to prevent them from forming longer branches, keeping the wall plastic to promote diffuse wall growth. Abstract : The β-glucosidase from cell walls of Coprinopsis cinerea caused a decrease in the molecular size of stipe wall β-glucan, and may function by trimming or cutting the β-glucan side chains. Abstract : … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 363:Issue 9(2016:May)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 363:Issue 9(2016:May)
- Issue Display:
- Volume 363, Issue 9 (2016)
- Year:
- 2016
- Volume:
- 363
- Issue:
- 9
- Issue Sort Value:
- 2016-0363-0009-0000
- Page Start:
- Page End:
- Publication Date:
- 2016-03-29
- Subjects:
- extracellular β-glucosidase -- hydrolyase activity -- glycosyltransferase activity -- stipe elongation -- Coprinopsis cinerea
Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1093/femsle/fnw078 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12377.xml