Linked Life Data

16900329

Source:http://linkedlifedata.com/resource/pubmed/id/16900329

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2006-9-26
pubmed:databankReference
pubmed:abstractText
Strains of thermophilic bacilli were screened for cellulolytic activity by gel diffusion assay on selective medium at 55 degrees C. Strain B-41361, identified as a strain of Bacillus licheniformis, displayed activity against carboxymethylcellulose. Zymogram analysis demonstrated several catalytically active polypeptides with the most prominent species having a mass of 37 kDa. The enzyme was purified 60-fold with a 17% yield and specific activity of 183 U/mg. The amino terminal sequence was homologous to members of glycoside hydrolase family 5. Optimal temperature was 65 degrees C (measured over 30 min), but the enzyme was most stable at 60 degrees C, retaining greater than 90% activity after one hour. The enzyme had a broad pH range, with maximal activity at pH 6.0, 75% maximal activity at pH 4.5, and 40% at pH 10. The enzyme hydrolyzed p-nitrophenylcellobioside, barley beta-glucan, and lichenan, but no activity was detected against avicel or acid-swollen cellulose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0141-5492
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1761-5
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Purification and characterization of a family 5 endoglucanase from a moderately thermophilic strain of Bacillus licheniformis.
pubmed:affiliation
U.S. Department of Agriculture, Agricultural Research Service, National Center for Agricultural Utilization Research, 1815 N. University St., Peoria, IL 61604, USA. bischoffk@ncaur.usda.gov
pubmed:publicationType
Journal Article