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Title: | Purification and partial characterization of α-D-mannosidase from Erythrina indica seeds |
Authors: | Kestwal, Rakesh M Bhide, Shobhana V |
Keywords: | Erythrina indica;⍺-D-mannosidase;Purification;con-A CL seralose;Zinc |
Issue Date: | Jun-2005 |
Publisher: | CSIR |
IPC Code: | A 23 J 1/14, C 07 K |
Abstract: | ⍺-D-Mannosidase (EC: 3.2.1.24), a glycoprotein with 8.6% carbohydrate was purified (26 fold purification) to homogeneity from Erythrina indica seeds, by gel filtration on Bio-Gel P-100 and affinity chromatography on Con-A CL Seralose. The enzyme had the molecular mass of 124 kDa and 127 kDa by gel filtration and SDS-PAGE, respectively. The optimum pH and temperature for enzyme activity were found to be 4.6 and 50ºC, respectively. The Km value for the enzyme was 2.1 mM for p-nitrophenyl-α-D-mannopyranoside. The enzyme activity was found to depend on the presence of Zn²⁺. Chemical modification studies revealed the involvement of tryptophan, serine and cysteine for enzyme activity. |
Page(s): | 156-160 |
ISSN: | 0301-1208 |
Appears in Collections: | IJBB Vol.42(3) [June 2005] |
Files in This Item:
File | Description | Size | Format | |
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IJBB 42(3) 156-160.pdf | 356.18 kB | Adobe PDF | View/Open |
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