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 .
from.pdf - Published Version
Restricted to Registered users only
Download (535Kb) | Request a copy
Trehalase (?,?-Trehalosee gludohydrolase, EC 18.104.22.168) was partially solubilized from the thermophilic fungus Humicola lanuginosa RM-B, and purified 184-fold. The purified enzyme was optimally active at 50Â°C in acetate buffer at pH 5.5. It was highly specific for ?,?-trehalose and had an apparent Km = 0.4 mM at 50Â°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 50Â°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 ï¿½protective factor(s)ï¿½ present in mycelial extracts. The ï¿½protective factor(s)ï¿½ 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|
Actions (login required)