P.H. Theaswini1, B.A. Parthasarathi2 and H.B. Mahesha3*

1Department of Biotechnology, Maharani’s Science College for Women, Mysore - 570005 India 2Department of Sericulture, Manasagangotri, University of Mysore, Mysore - 570006 India 3Department of Sericulture, Yuvaraja’s College, University of Mysore, Mysore-570005 India #Authors contributed equally to the research work *Corresponding Author E-mail:hbmahesh@ycm.uni-mysore.ac.in

ABSTRACT

Cocoonase (protease) 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 using Sephadex G-100. Of the fractions, the purified fraction-II was used to produce G-banding on eukaryotic chromosomes. Trypsin was also used for G-banding similarlyas standard protease. The results clearly indicated the protease activity of mulberry silkworm Bombyx mori L., which can be used in silk industry at various processes.

Key words : Bombyx mori, chromosomes, cocoonase, trypsin, G-banding.

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