The cocoon trehalase of the silkworm, Bombyx mori

Autor:	Shoji Asano, Shuya Shimada, Atsushi Kamada
Rok vydání:	1980
Předmět:	chemistry.chemical_classification biology Ph optimum Trehalase activity biology.organism_classification Biochemistry Divalent SILK Enzyme chemistry Bombyx mori Insect Science Trehalase Molecular Biology
Zdroj:	Insect Biochemistry. 10:49-52
ISSN:	0020-1790
DOI:	10.1016/0020-1790(80)90037-2
Popis:	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 Mn2+, Cu2+ and Zn2+. 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::6c8292831854174a2f5f98f405b4b8e0 https://doi.org/10.1016/0020-1790(80)90037-2 Zobrazit plný text záznamu