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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 .

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Official URL: http://dx.doi.org/10.1016/0005-2744(78)90210-3

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
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.ernet.in/id/eprint/32321

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