Linked Life Data

7887599

Source:http://linkedlifedata.com/resource/pubmed/id/7887599

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-4-10
pubmed:abstractText
Bacillus stearothermophilus T-6 produced an alpha-L-arabinofuranosidase when grown in the presence of L-arabinose, sugar beet arabinan, or oat spelt xylan. At the end of a fermentation, about 40% of the activity was extracellular, and enzyme activity in the cell-free supernatant could reach 25 U/ml. The enzymatic activity in the supernatant was concentrated against polyethylene glycol 20000, and the enzyme was purified eightfold by anion-exchange and hydrophobic interaction chromatographies. The molecular weight of T-6 alpha-L-arabinofuranosidase was 256,000, and it consisted of four identical subunits as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration. The native enzyme had a pI of 6.5 and was most active at 70 degrees C and at pH 5.5 to 6.0. Its thermostability at pH 7.0 was characterized by half-lives of 53, 15, and 1 h at 60, 65, and 70 degrees C, respectively. Kinetic experiments at 60 degrees C with p-nitrophenyl alpha-L-arabinofuranoside as a substrate gave a Vmax, a Km, and an activation energy of 749 U/mg, 0.42 mM, and 16.6 kcal/mol, (ca. 69.5 kJ/mol), respectively. The enzyme had no apparent requirement for cofactors, and its activity was strongly inhibited by 1 mM Hg2+. T-6 alpha-L-arabinofuranosidase released L-arabinose from arabinan and had low activity on oat spelt xylan. The enzyme acted cooperatively with T-6 xylanase in hydrolyzing oat spelt xylan, and L-arabinose, xylose, and xylobiose were detected as the end reaction products.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-1622210, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-16348679, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-16660741, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-6528977, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-6650260, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-6742828, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-8031084, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-8092996, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-8327884, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-8328796, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887599-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0099-2240
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
170-4
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Purification and characterization of alpha-L-arabinofuranosidase from Bacillus stearothermophilus T-6.
pubmed:affiliation
Department of Food Engineering and Biotechnology, Technion-Israel Institute of Technology, Haifa.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't