BIOCHEMICAL STUDIES OF COCOONASE FROM FOUR BREEDS OF MULBERRY SILKWORM BOMBYX MORI L.

Abstract

Cocoonase collected from two multivoltine breeds of mulberry silkworm namely Nistari, C. nichi, and two bivoltine breeds namely KA and NB4D2. The crude enzyme was isolated and purified by column chromatography. The bivoltines yielded 750 mgs, where as multivoltines yielded 670 mgs for every gram of crude sample loaded on to DEAE-Cellulose column. The analysis of electrophoretic mobility of bound protein from DEAE-Cellulose column and that of Fraction-II of sephadex gel filtration displayed similarity in molecular weight. The results of amino acid analysis exhibited the results that the amount of aromatic amino acids is very less and tryptophane is found to be completely absent. The results of paper chromatography of carbohydrates showed presence of glucose like substance in the cocoonase sample of all the breeds.