Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-9-10
pubmed:abstractText
Aerobic cultures of an actinomycete were found to produce penicillin V acylase (PVA) (PA, EC-3.5.1.11) extracellularly. The presence of L-2-3 diamino-propionic acid in cell wall and formation of sclerotia on culture media led to its identification as Chainia, a sclerotial Streptomyces. Partially purified acylase was adsorbed on kieselguhr and entrapped in polyacrylamide gel. The immobilized preparation proved effective with respect to retention of enzyme and enzyme activity even after 15 successful cycles. The pH optimum for crude enzyme was in the range of pH 7.5-8.0, and for the (NH4)2 SO4 fraction it was pH 8.5. The immobilized enzyme showed maximal activity at pH 9.5. The optimum temperature for acylase activity was at 55 degrees C. The crude enzyme, ammonium sulfate fraction, and immobilized enzyme showed Km value for penicillin V of 6.13 mM, 14.3 mM, and 17.1 mM, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0343-8651
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
186-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Chainia penicillin V acylase: strain characteristics, enzyme immobilization, and kinetic studies.
pubmed:affiliation
Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi-110067, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't