Document Detail


Purification and characterization of a rhamnogalacturonase with protopectinase activity from Trametes sanguinea.
MedLine Citation:
PMID:  8001546     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In a culture filtrate of Trametes sanguinea IFO 6490, we found a protopectin-solubilizing enzyme, protopectinase-T, that did not degrade polygalacturonic acid. The enzyme was purified to homogeneity with hydrophobic, cation-exchange, anion-exchange, and size-exclusion chromatographies. It had an apparent molecular mass of 55 kDa by SDS/PAGE and 39 kDa by size-exclusion chromatography on Superose 12. The isoelectric point was at pH 8.1. Protopectinase-T was stable from pH 3.0 to 6.0 and at temperatures up to 50 degrees C. The optimum pH for enzyme activity was 4.0 at 37 degrees C, and the optimum temperature was 50 degrees C at pH 5.0. Protopectinase-T catalyzed the release of highly polymerized pectin from lemon peel protopectin.
Authors:
M Sakamoto; Y Shirane; I Naribayashi; K Kimura; N Morishita; T Sakamoto; T Sakai
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  226     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1994 Dec 
Date Detail:
Created Date:  1995-01-26     Completed Date:  1995-01-26     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  285-91     Citation Subset:  IM    
Affiliation:
Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture, Japan.
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MeSH Terms
Descriptor/Qualifier:
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Glycoside Hydrolases / chemistry,  isolation & purification*,  metabolism*
Hydrogen-Ion Concentration
Isoelectric Point
Molecular Weight
Pectins / isolation & purification
Polyporaceae / enzymology*
Temperature
Chemical
Reg. No./Substance:
0/Pectins; 9000-69-5/pectin; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.-/protopectinase; EC 3.2.1.-/rhamnogalacturonase A

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