alexa PURIFICATION AND PHYSICOCHEMICAL CHARACTERIZATION OF THE α- GLUCOSIDASE OF THE DIGESTIVE JUICE OF THE SNAIL LIMICOLRIA FLAMMEA (Müller 1774).


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Research Article

PURIFICATION AND PHYSICOCHEMICAL CHARACTERIZATION OF THE α- GLUCOSIDASE OF THE DIGESTIVE JUICE OF THE SNAIL LIMICOLRIA FLAMMEA (Müller 1774).

Saki Suomion Justin1*, Sea Tehi Bernard1, Koffi Kouame Mathias3, Soro Yade Rene1, KRA Kouassi Aboutou s1 and Diopoh Kore J1
  1. Laboratory of Biotechnology, University Félix Houphouet Boigny Cocody- Abidjan 22 BP 582 Abidjan 22
  2. Laboratory of Biochemistry Pharmacodinamy, University Félix Houphouet Boigny Cocody-Abidjan 22 BP 582 Abidjan 22
  3. Laboratory of Biochemistry and the Food Sciences University Félix Houphouet Boigny Cocody- Abidjan 22 BP 582 Abidjan 22
Corresponding Author: Saki Suomion Justin, Laboratory of Biotechnology, University Félix Houphouet Boigny Cocody- Abidjan 22 BP 582 Abidjan 22,E-mail: [email protected], phone: (225) 01 84 17 82//(225) 49 39 96 72
Received: 01 November 2013 Accepted: 19 November 2013
 

Abstract

In this study we are interested by the α-glucosidase, a protein biocatalyst from the digestive juice of a snail Limicolaria flammea which we purified by the chromatographic methods. Then the physico-chemical characteristics of this enzyme were determined. With a specific activity of the crude extract of 4.31 U/mg, purification have been done on Sephacryl S-200 HR gel then, specific activity has passed to 34.17 U/mg with purification factor of 7,93.With Anx-sepharose 4 fast flow gel, specific activity increased to 92.58U/mg with purification factor of 21.48 and 147 U/mg on phenyl-Sepharose CL 6B with purification factor of 34.11. The apparent molecular weights of the α-glucosidase purified on gel filtration (64,000 Da) and by electrophoresis on polyacrylamide gel (68,200 Da) were nearly identical. With a stability zone of pH between 4 and 7.5, the α- glucosidase had its maximum activity at pH 6.5. Optimum temperature of hydrolysis was obtained at 45°C and was stable at 37 to 40°C. The study of substrate specificity showed that para-nitrophenyl-α-D glucopyranoside and sucrose are hydrolyzed by the enzyme. It was inhibited by Cu2+, Ni2+, Hg2+ and activated by Mn2+. Ideal conditions for activity of this enzyme were known therefore it could be used to achieve synthesis.

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