Purification and physicochemical properties of a -amylase from irradiated wheat.
J Biosci
;
1981 Jun; 3(2): 105-116
Article
in English
| IMSEAR
| ID: sea-160101
ABSTRACT
α-Amylases from control and gamma-irradiated (at 0.2 and 2.0 kGy dose levels) wheat seedlings were purified to homogeneity and characterized. The molecular weight of the enzyme from a 2 kGy irradiated sample was slightly lower than that of the control; other general and catalytic properties also showed some differences. α-Amylase from the irradiated (2 kGy) sample had a narrow range of pH optimum and was inactivated faster at alkaline pH and by heat treatment than the enzyme from unirradiated wheat. A high apparent Michaelis constant (Km) and a low maximal velocity (Vmax) for the hydrolysis of soluble starch catalyzed by the enzyme from irradiated (2 kGy) wheat, suggested some modifications in the formation of the substrate α-amylase complex. Further, of the total number of amino acid residues lost on irradiation, dicarboxylic amino acids constituted the largest percentage; these structural alterations in the enzyme may be responsible for its partial inactivation. The total sugars liberated upon amylolysis of starch with the 2 kGy irradiated enzyme were lower than control, and there was accumulation of higher maltodextrins in the place of maltose.
Full text:
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Index:
IMSEAR (South-East Asia)
Language:
English
Journal:
J Biosci
Year:
1981
Type:
Article
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