Comparative study of performances of lipase immobilized asymmetric polysulfone and polyether sulfone membranes in olive oil hydrolysis.
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.
Gupta
S
S
Reverse Osmosis Discipline, Central Salt and Marine Chemicals Research Institute, G.B. Marg, Bhavnagar 364002, Gujarat, India.
Yogesh
Javiya
S
S
Bhambi
M
M
Pundir
C S
CS
Singh
K
K
Bhattacharya
A
A
D002175:Candida / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D015394:Molecular Structure; D000069463:Olive Oil; D010938:Plant Oils / Q000737:chemistry* / Q000378:metabolism*; D011108:Polymers / Q000737:chemistry* / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013450:Sulfones / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D014961:X-Ray Diffraction
D004800:Enzymes, Immobilized; D000069463:Olive Oil; D010938:Plant Oils; D011108:Polymers; D013450:Sulfones; C017662:polysulfone P 1700; C022840:polyether sulfone; D008049:Lipase