Purification and properties of trehalase from the thermophilic fungus Humicola lanuginosa

Prasad, ARS and Maheshwari, Ramesh (1978) Purification and properties of trehalase from the thermophilic fungus Humicola lanuginosa. In: Biochimica et Biophysica Acta (BBA), 525 (1). 162-170 .

PDF from.pdf - Published Version Restricted to Registered users only Download (547kB) | Request a copy

Abstract

Trehalase (?,?-Trehalosee gludohydrolase, EC 3.2.1.28) was partially solubilized from the thermophilic fungus Humicola lanuginosa RM-B, and purified 184-fold. The purified enzyme was optimally active at 50°C in acetate buffer at pH 5.5. It was highly specific for ?,?-trehalose and had an apparent Km = 0.4 mM at 50°C. None of the other disaccharides tested either inhibited or activated the enzyme. The molecular weight of the enzyme was around 170000. Trehalase from mycelium grown at 40 and 50°C had similar properties. The purified enzyme, in contrast to that in the crude-cell free extract, was less stable. At low concentration, purified trehalase was afforded protection against heat-inactivation by �protective factor(s)� present in mycelial extracts. The �protective factor(s)� was sensitive to proteolytic digestion. It was not diffusable and was stable to boiling for at least 30 min. Bovine serum albumin and casein also protected the enzyme from heat-inactivation.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA)
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	22 Sep 2010 10:36
Last Modified:	22 Sep 2010 10:36
URI:	http://eprints.iisc.ac.in/id/eprint/32321

Actions (login required)

View Item