|
KMID : 0364819910290020104
|
|
Korean Journal of Microbiology
1991 Volume.29 No. 2 p.104 ~ p.110
|
|
|
Purification and Properties of Glucoamylase from Schwanniomyces castellii
|
|
|
|
|
Abstract
|
|
|
1
The glucoamylase of Schwanniomyces castellii was purified to homogeneity from the culture filtrate. The purified enzyme was a glycoprotein with a molecular mass of about 145 KDa, which was monomeric protein with an isoelectric point of 43. The pH and temperature optima were 5.5 and 40C, respectively. The enzyme was fairly stable up to 50C and at acid pH range (pH 4.5-6.0). The apparent Km of the enzyme toward soluble starch, isomaltose and pullulan were 3.84, 0.51 and 13.7 mg/ml, respectively. The analysis of amino acid composition on this enzyme was found to be acidic protein like other fungal glucoamylase. The amino acid sequence of N-terminal peptide consisted of Ala-Pro-Ala-Asp-Gly-Ile-Gly-Asp-X-Ala-X-Ala.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
Listed journal information
|
|
|