Linked Life Data

14538102

Source:http://linkedlifedata.com/resource/pubmed/id/14538102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-10-10
pubmed:abstractText
Interest in the alpha-L-arabinofuranosidases has increased in recent years because of their application in the conversion of various hemicellulosic substrates to fermentable sugars for subsequent production of fuel alcohol. Xylanases, in conjunction with alpha-L-arabinofuranosidases and other accessory enzymes, act synergistically to degrade xylan to component sugars. The induction of alpha-L-arabinofuranosidase production, physico-chemical characteristics, substrate specificity, and molecular biology of the enzyme are described. The current state of research and development of the arabinofuranosidases and their role in biotechnology are presented.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Aug
pubmed:issn
0734-9750
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
403-23
pubmed:dateRevised
2006-7-7
pubmed:year
2000
pubmed:articleTitle
Alpha-L-arabinofuranosidases: biochemistry, molecular biology and application in biotechnology.
pubmed:affiliation
Fermentation Biochemistry Research Unit, National Center for Agricultural Utilization Research, U.S. Department of Agriculture, Agricultural Research Service, Peoria, IL 61604, USA. sahabc@mail.ncaur.usda.gov
pubmed:publicationType
Journal Article