OrangerV1, PascalFrancis, Curation, bibRecord, 000758

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

Identifieur interne : 000758 ( PascalFrancis/Curation ); précédent : 000757; suivant : 000759

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.

A01	`01`	`1`		`@0 0273-2289`
A02	`01`			`@0 ABIBDL`
A03		`1`		`@0 Appl. biochem. biotechnol.`
A05				`@2 160`
A06				`@2 7`
A08	`01`	`1`	`ENG`	`@1 Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora`
A11	`01`	`1`		`@1 SALEH AHMED MOHAMED`
A11	`02`	`1`		`@1 DREES (Ehab A.)`
A11	`03`	`1`		`@1 EL-BADRY (Mohamed O.)`
A11	`04`	`1`		`@1 FAHMY (Afaf S.)`
A14	`01`			`@1 Molecular Biology Department, National Research Center @2 Dokki. Cairo @3 EGY @Z 1 aut. @Z 3 aut. @Z 4 aut.`
A14	`02`			`@1 Biochemistry division, Chemistry Department, Faculty of Science, Fayoum University @2 Fayoum @3 EGY @Z 2 aut.`
A20				`@1 2054-2065`
A21				`@1 2010`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 17423 @5 354000181751000190`
A44				`@0 0000 @1 © 2010 INIST-CNRS. All rights reserved.`
A45				`@0 32 ref.`
A47	`01`	`1`		`@0 10-0270833`
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A61				`@0 A`
A64	`01`	`1`		`@0 Applied biochemistry and biotechnology`
A66	`01`			`@0 DEU`
C01	`01`		`ENG`	@0 <is proportional to>-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.
C02	`01`	`X`		`@0 002A31`
C02	`02`	`X`		`@0 215`
C03	`01`	`X`	`FRE`	`@0 α-Amylase @2 FE @5 01`
C03	`01`	`X`	`ENG`	`@0 α-Amylase @2 FE @5 01`
C03	`01`	`X`	`SPA`	`@0 α-Amylase @2 FE @5 01`
C03	`02`	`X`	`FRE`	`@0 Purification @5 02`
C03	`02`	`X`	`ENG`	`@0 Purification @5 02`
C03	`02`	`X`	`SPA`	`@0 Purificación @5 02`
C03	`03`	`X`	`FRE`	`@0 Citrus sinensis @2 NS @5 13`
C03	`03`	`X`	`ENG`	`@0 Citrus sinensis @2 NS @5 13`
C03	`03`	`X`	`SPA`	`@0 Citrus sinensis @2 NS @5 13`
C07	`01`	`X`	`FRE`	`@0 Glycosidases @2 FE`
C07	`01`	`X`	`ENG`	`@0 Glycosidases @2 FE`
C07	`01`	`X`	`SPA`	`@0 Glycosidases @2 FE`
C07	`02`	`X`	`FRE`	`@0 Glycosylases @2 FE`
C07	`02`	`X`	`ENG`	`@0 Glycosylases @2 FE`
C07	`02`	`X`	`SPA`	`@0 Glycosylases @2 FE`
C07	`03`	`X`	`FRE`	`@0 Hydrolases @2 FE`
C07	`03`	`X`	`ENG`	`@0 Hydrolases @2 FE`
C07	`03`	`X`	`SPA`	`@0 Hydrolases @2 FE`
C07	`04`	`X`	`FRE`	`@0 Enzyme @2 FE`
C07	`04`	`X`	`ENG`	`@0 Enzyme @2 FE`
C07	`04`	`X`	`SPA`	`@0 Enzima @2 FE`
C07	`05`	`X`	`FRE`	`@0 Rutaceae @2 NS`
C07	`05`	`X`	`ENG`	`@0 Rutaceae @2 NS`
C07	`05`	`X`	`SPA`	`@0 Rutaceae @2 NS`
C07	`06`	`X`	`FRE`	`@0 Dicotyledones @2 NS`
C07	`06`	`X`	`ENG`	`@0 Dicotyledones @2 NS`
C07	`06`	`X`	`SPA`	`@0 Dicotyledones @2 NS`
C07	`07`	`X`	`FRE`	`@0 Angiospermae @2 NS`
C07	`07`	`X`	`ENG`	`@0 Angiospermae @2 NS`
C07	`07`	`X`	`SPA`	`@0 Angiospermae @2 NS`
C07	`08`	`X`	`FRE`	`@0 Spermatophyta @2 NS`
C07	`08`	`X`	`ENG`	`@0 Spermatophyta @2 NS`
C07	`08`	`X`	`SPA`	`@0 Spermatophyta @2 NS`
N21				`@1 172`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

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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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<fA08 i1="01" i2="1" l="ENG"><s1>Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora</s1>
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<fA11 i1="01" i2="1"><s1>SALEH AHMED MOHAMED</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>DREES (Ehab A.)</s1>
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<fA11 i1="03" i2="1"><s1>EL-BADRY (Mohamed O.)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>FAHMY (Afaf S.)</s1>
</fA11>
<fA14 i1="01"><s1>Molecular Biology Department, National Research Center</s1>
<s2>Dokki. Cairo</s2>
<s3>EGY</s3>
<sZ>1 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Biochemistry division, Chemistry Department, Faculty of Science, Fayoum University</s1>
<s2>Fayoum</s2>
<s3>EGY</s3>
<sZ>2 aut.</sZ>
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<fA20><s1>2054-2065</s1>
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<fC01 i1="01" l="ENG"><s0>-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.</s0>
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</fC02>
<fC02 i1="02" i2="X"><s0>215</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>α-Amylase</s0>
<s2>FE</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>α-Amylase</s0>
<s2>FE</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>α-Amylase</s0>
<s2>FE</s2>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Purification</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Purification</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Purificación</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Citrus sinensis</s0>
<s2>NS</s2>
<s5>13</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Citrus sinensis</s0>
<s2>NS</s2>
<s5>13</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Citrus sinensis</s0>
<s2>NS</s2>
<s5>13</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Glycosidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Glycosidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Glycosidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Glycosylases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Glycosylases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Glycosylases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Rutaceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Rutaceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Rutaceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Dicotyledones</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Dicotyledones</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Dicotyledones</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Angiospermae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Angiospermae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Angiospermae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="08" i2="X" l="FRE"><s0>Spermatophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="08" i2="X" l="ENG"><s0>Spermatophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="08" i2="X" l="SPA"><s0>Spermatophyta</s0>
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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

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