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Enzymic synthesis of salidroside: Purification and characterization of salidrosidase from Aspergillas niger

Paper ID Volume ID Publish Year Pages File Format Full-Text
36250 45125 2005 5 PDF Available
Title
Enzymic synthesis of salidroside: Purification and characterization of salidrosidase from Aspergillas niger
Abstract

An enzyme synthesising salidroside with p-tyrosol and β-d-glucose was isolated from Aspergillas niger, purified and characterized in this paper. After (NH4)2SO4 precipitation and ion exchange chromatography, the enzyme was purified to one band in SDS-polyacrylamide gel electrophoresis, and its molecular weight was about 84.6 kDa. The optimum temperature of the enzyme was 45 °C, and the optimum pH was 5.0. The enzyme was stable at less than 55 °C and pH 4.5–6.0. The enzyme catalyzed p-tyrosol and β-d-glucose to form salidroside in the concentrations of 1.5% p-tyrosol and 6% β-d-glucose. The yield of salidroside was about 10%.

Keywords
Purification; Characterization; Salidrosidase; Salidroside; Enzymatic synthesis
First Page Preview
Enzymic synthesis of salidroside: Purification and characterization of salidrosidase from Aspergillas niger
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 9, September 2005, Pages 3143–3147
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering