Bioaffinity immobilization of tannase from Aspergillus niger on concanavalin A-Sepharose CL-4B.
Tannase from Aspergillus niger van Teighem was immobilized on concanavalin A-Sepharose via bioaffinity interaction. The immobilized enzyme showed a pH optimum similar to that of the free enzyme. K(m) values for free and immobilized enzyme were 0.3 and 0.6 mM respectively. V(max) changed from 0.013 to 0.02 micromol x min(-1) upon immobilization. The immobilized preparation was quite stable to reuse, there was no loss of enzyme activity after three cycles and it retained 81% activity even after the sixth cycle. Ester hydrolysis using the immobilized enzyme led to a 40% conversion into gallic acid as compared with 30% obtained with the free enzyme.
Sharma
Shweta
S
Chemistry Department, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi, India.
Bhat
Tej Krishan
TK
Gupta
Munishwar Nath
MN
D001234:Aspergillus niger / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*; D003208:Concanavalin A / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D012685:Sepharose / Q000031:analogs & derivatives* / Q000737:chemistry
D004800:Enzymes, Immobilized; C028326:concanavalin A-sepharose; D003208:Concanavalin A; C035771:Sepharose CL 4B; D012685:Sepharose; D002265:Carboxylic Ester Hydrolases; C022711:tannase