Abstract
The cocoon of the silkworm, Bombyx mori contained trehalase activity. Trehalase activity in the cocoon floss was higher than in the cocoon layer. Trehalase from crude extracts prepared from cocoon floss had a pH optimum of 5.5, a K m of 1.41 mM and an activation energy of 10.9 kcal/mole. The enzyme was inhibited by divalent cations such as Mn 2+, Cu 2+ and Zn 2+. Trehalase and saccharase (β-fructosidase) in the cocoon floss were near-completely separated by ion-exchange chromatography. Trehalase was not present in the liquid silk of the silk glands.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
