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IJBB Vol.42 [2005] >
IJBB Vol.42(3) [June 2005] >


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 CodeA 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
Source:IJBB Vol.42(3) [June 2005]

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