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
English descriptors
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.
pA |
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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. |
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A23 | 01 | | | @0 ENG |
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A43 | 01 | | | @1 INIST @2 17423 @5 354000181751000190 |
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A44 | | | | @0 0000 @1 © 2010 INIST-CNRS. All rights reserved. |
---|
A45 | | | | @0 32 ref. |
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A47 | 01 | 1 | | @0 10-0270833 |
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A64 | 01 | 1 | | @0 Applied biochemistry and biotechnology |
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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 |
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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 |
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N82 | | | | @1 OTO |
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|
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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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<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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<fC03 i1="01" i2="X" l="FRE"><s0>α-Amylase</s0>
<s2>FE</s2>
<s5>01</s5>
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<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>
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<s5>01</s5>
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<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>
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<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>
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<fC07 i1="02" i2="X" l="SPA"><s0>Glycosylases</s0>
<s2>FE</s2>
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<fC07 i1="03" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
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<fC07 i1="03" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
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<s2>FE</s2>
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<fC07 i1="04" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
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<fC07 i1="04" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
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<fC07 i1="05" i2="X" l="FRE"><s0>Rutaceae</s0>
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<fC07 i1="05" i2="X" l="ENG"><s0>Rutaceae</s0>
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<fC07 i1="06" i2="X" l="ENG"><s0>Dicotyledones</s0>
<s2>NS</s2>
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<fC07 i1="06" i2="X" l="SPA"><s0>Dicotyledones</s0>
<s2>NS</s2>
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<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>
<s2>NS</s2>
</fC07>
<fN21><s1>172</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
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|texte= Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora
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