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Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Identifieur interne : 001C95 ( Main/Exploration ); précédent : 001C94; suivant : 001C96

Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Auteurs : SALEH AHMED MOHAMED [Égypte] ; Ehab A. Drees [Égypte] ; Mohamed O. El-Badry [Égypte] ; Afaf S. Fahmy [Égypte]

Source :

Applied biochemistry and biotechnology [ 0273-2289 ] ; 2010.

RBID : Pascal:10-0270833

Descripteurs français

Pascal (Inist)
- α-Amylase, Purification, Citrus sinensis.

English descriptors

KwdEn :
- Citrus sinensis, Purification, α-Amylase.

Abstract

-Amylase activity was screened in the peel, as waste fruit, of 13 species and cultivars of Egyptian citrus. The species Citrus sirzensis cv. Abosora had the highest activity. α-Amylase Al from Abosora peel was purified to homogeneity using anion and cation-exchange, and gel filtration chromatographies. Molecular weight of α-amylase Al was found to be 42 kDa. The hydrolysis properties of α-amylase Al toward different substrates indicated that corn starch is the best substrate. The α-amylase had the highest activity toward glycogen compared with amylopectin and dextrin. Potato starch had low affinity toward α-amylase Al but it did not hydrolyze β-cyclodextrin and dextran. Apparent Km for α-amylase Al was 5 mg (0.5%) starch/ml. α-Amylase Al showed optimum activity at pH 5.6 and 40 °C. The enzyme was thermally stable up to 40 °C and inactivated at 70 °C. The effect of mono and divalent metal ions were tested for the α-amylase Al. Ba²⁺ was found to have activating effect, where as Li⁺ had negligible effect on activity. The other metals caused inhibition effect. Activity of the α-amylase Al was increased one and half in the presence of 4 mM Ca²⁺ and was found to be partially inactivated at 10 mM Ca²⁺. The reduction of starch viscosity indicated that the enzyme is endoamylase. The results suggested that, in addition to citrus peel is a rich source of pectins and flavanoids, α-amylase Al from orange peel could be involved in the development and ripening of citrus fruit and may be used for juice processing.

Affiliations:

Égypte

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Le document en format XML

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<front><div type="abstract" xml:lang="en">-Amylase activity was screened in the peel, as waste fruit, of 13 species and cultivars of Egyptian citrus. The species Citrus sirzensis cv. Abosora had the highest activity. α-Amylase Al from Abosora peel was purified to homogeneity using anion and cation-exchange, and gel filtration chromatographies. Molecular weight of α-amylase Al was found to be 42 kDa. The hydrolysis properties of α-amylase Al toward different substrates indicated that corn starch is the best substrate. The α-amylase had the highest activity toward glycogen compared with amylopectin and dextrin. Potato starch had low affinity toward α-amylase Al but it did not hydrolyze β-cyclodextrin and dextran. Apparent Km for α-amylase Al was 5 mg (0.5%) starch/ml. α-Amylase Al showed optimum activity at pH 5.6 and 40 °C. The enzyme was thermally stable up to 40 °C and inactivated at 70 °C. The effect of mono and divalent metal ions were tested for the α-amylase Al. Ba<sup>2+</sup>
 was found to have activating effect, where as Li<sup>+</sup>
 had negligible effect on activity. The other metals caused inhibition effect. Activity of the α-amylase Al was increased one and half in the presence of 4 mM Ca<sup>2+</sup>
 and was found to be partially inactivated at 10 mM Ca<sup>2+</sup>
. The reduction of starch viscosity indicated that the enzyme is endoamylase. The results suggested that, in addition to citrus peel is a rich source of pectins and flavanoids, α-amylase Al from orange peel could be involved in the development and ripening of citrus fruit and may be used for juice processing.</div>
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Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri