Document Detail


Purification and properties of two type-B alpha-L-arabinofuranosidases produced by Penicillium chrysogenum.
MedLine Citation:
PMID:  12726996     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two distinct extracellular alpha-L-arabinofuranosidases (AFases; EC 3.2.1.55) were purified from the culture filtrate of Penicillium chrysogenum 31B. The molecular masses of the enzymes were estimated to be 79 kDa (AFQ1) and 52 kDa (AFS1) by SDS-PAGE. Both enzymes had their highest activities at 50 degrees C and were stable up to 50 degrees C. Enzyme activities of AFQ1 and AFS1 were highest at pH 4.0 to 6.5 and pH 3.3 to 5.0, respectively. Addition of 10 mg/ml arabinose to the reaction mixture decreased the AFS1 activity but hardly affected AFQ1. Both enzymes displayed broad substrate specificities; they released arabinose from branched arabinan, debranched arabinan, arabinoxylan, arabinogalactan, and arabino-oligosaccharides. AFS1 also showed low activity towards p-nitrophenyl-beta-D-xylopyranoside. An exo-arabinanase, which catalyzes the release of arabinobiose from linear arabinan at the nonreducing terminus, acted synergistically with both enzymes to produce L-arabinose from branched arabinan.
Authors:
T Sakamoto; H Kawasaki
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1621     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2003 May 
Date Detail:
Created Date:  2003-05-02     Completed Date:  2003-06-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  204-10     Citation Subset:  IM    
Affiliation:
Division of Applied Biochemistry, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, Osaka 599-8531, Japan. sakamoto@biochem.osakafu-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Fungal Proteins / isolation & purification*
Glycoside Hydrolases / chemistry,  isolation & purification*,  metabolism
Isoenzymes / isolation & purification
Molecular Sequence Data
Penicillium chrysogenum / enzymology*
Substrate Specificity
Chemical
Reg. No./Substance:
0/Fungal Proteins; 0/Isoenzymes; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.55/alpha-N-arabinofuranosidase

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