Purification and some important characters of extracellular inulinase of Alternaria alternata (Fr.) Keissler.
Indian J Exp Biol
;
2002 Dec; 40(12): 1393-8
Article
in English
| IMSEAR
| ID: sea-58229
ABSTRACT
Protein precipitate of cell-free dialysate of extracellular inulinase (2,1-beta-fructan fructanohydrolase, EC 3.2.1.7) of A. alternata was maximally obtained by methanol. Such protein was fractionated by using 2-step column chromatography on Sephadex G150 and DEAE-cellulose. The partially purified enzyme had activity of 81 x 10(3) U/mg protein, with a yield of 69% of the original activity and the fold of purification was 62. Optimum temperature and pH for the activity of the purified enzyme were found to be 55 degrees C and 4.5, respectively. The enzyme was found to be stable up to 55 degrees C and in pH range of 4 to 5. Ba2+ and Ca2+ were found to stimulate the enzyme activity while Cu2+, Fe3+, Hg2+, and iodoacetate were recorded as strong inhibitors. T(1/2) of the enzyme was estimated to be two weeks and its apparent Km was calculated to be 0.066 M. The enzyme recorded hydrolyzing activity against sucrose and raffinose recording I/S ratio of 0.50. Molecular mass of the enzyme preparation was estimated by gel filtration and found to be 115 +/- 5 kDa.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Temperature
/
Enzyme Stability
/
Enzyme Inhibitors
/
Alternaria
/
Hydrogen-Ion Concentration
/
Insulysin
Language:
English
Journal:
Indian J Exp Biol
Year:
2002
Type:
Article
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