Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-1
pubmed:abstractText
In the present study, lipase was immobilized via glutaraldehyde crosslinking on the polysulfone and polyether sulfone asymmetric membranes. The results indicated that the overall immobilization of lipase is related to the hydrophobicity of the membrane material and thus higher immobilization is achieved for polysulfone membrane. The evidence of immobilization is done by XRD, SEM, contact angle and porometric studies. Hydrolytic activity of lipase in immobilized form is determined by hydrolyzing olive oil and compared with hydrolytic activity of free lipase. The effect of different reaction parameters viz., temperature, pH, substrate concentration, and incubation time on the lipase activity is investigated. The observed maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) of polysulfone and polyether sulfone is determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-51
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Comparative study of performances of lipase immobilized asymmetric polysulfone and polyether sulfone membranes in olive oil hydrolysis.
pubmed:affiliation
Reverse Osmosis Discipline, Central Salt and Marine Chemicals Research Institute, G.B. Marg, Bhavnagar 364002, Gujarat, India.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't