Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora
Identifieur interne :
000242 ( PascalFrancis/Corpus );
précédent :
000241;
suivant :
000243
Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora
Auteurs : SALEH AHMED MOHAMED ;
Ehab A. Drees ;
Mohamed O. El-Badry ;
Afaf S. FahmySource :
-
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.
Notice en format standard (ISO 2709)
Pour connaître la documentation sur le format Inist Standard.
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| A08 | 01 | 1 | ENG | @1 Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora |
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| A11 | 01 | 1 | | @1 SALEH AHMED MOHAMED |
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| A11 | 02 | 1 | | @1 DREES (Ehab A.) |
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| A11 | 03 | 1 | | @1 EL-BADRY (Mohamed O.) |
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| A11 | 04 | 1 | | @1 FAHMY (Afaf S.) |
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| 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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| A20 | | | | @1 2054-2065 |
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| A21 | | | | @1 2010 |
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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. |
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| A45 | | | | @0 32 ref. |
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| A47 | 01 | 1 | | @0 10-0270833 |
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| A60 | | | | @1 P |
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| A61 | | | | @0 A |
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| 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. |
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| C02 | 01 | X | | @0 002A31 |
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| C02 | 02 | X | | @0 215 |
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| C03 | 01 | X | FRE | @0 α-Amylase @2 FE @5 01 |
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| C03 | 01 | X | ENG | @0 α-Amylase @2 FE @5 01 |
|---|
| C03 | 01 | X | SPA | @0 α-Amylase @2 FE @5 01 |
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| C03 | 02 | X | FRE | @0 Purification @5 02 |
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| 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 |
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| 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 |
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| C07 | 08 | X | FRE | @0 Spermatophyta @2 NS |
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| C07 | 08 | X | ENG | @0 Spermatophyta @2 NS |
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| C07 | 08 | X | SPA | @0 Spermatophyta @2 NS |
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| N44 | 01 | | | @1 OTO |
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| N82 | | | | @1 OTO |
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|
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Format Inist (serveur)
| NO : | PASCAL 10-0270833 INIST |
|---|
| ET : | Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora |
|---|
| AU : | SALEH AHMED MOHAMED; DREES (Ehab A.); EL-BADRY (Mohamed O.); FAHMY (Afaf S.) |
|---|
| AF : | Molecular Biology Department, National Research Center/Dokki. Cairo/Egypte (1 aut., 3 aut., 4 aut.); Biochemistry division, Chemistry Department, Faculty of Science, Fayoum University/Fayoum/Egypte (2 aut.) |
|---|
| DT : | Publication en série; Niveau analytique |
|---|
| SO : | Applied biochemistry and biotechnology; ISSN 0273-2289; Coden ABIBDL; Allemagne; Da. 2010; Vol. 160; No. 7; Pp. 2054-2065; Bibl. 32 ref. |
|---|
| LA : | Anglais |
|---|
| EA : | <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. |
|---|
| CC : | 002A31; 215 |
|---|
| FD : | α-Amylase; Purification; Citrus sinensis |
|---|
| FG : | Glycosidases; Glycosylases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta |
|---|
| ED : | α-Amylase; Purification; Citrus sinensis |
|---|
| EG : | Glycosidases; Glycosylases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta |
|---|
| SD : | α-Amylase; Purificación; Citrus sinensis |
|---|
| LO : | INIST-17423.354000181751000190 |
|---|
| ID : | 10-0270833 |
|---|
Links to Exploration step
Pascal:10-0270833
Le document en format XML
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</keywords><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><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0273-2289</s0>
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</fA05><fA08 i1="01" i2="1" l="ENG"><s1>Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora</s1>
</fA08><fA11 i1="01" i2="1"><s1>SALEH AHMED MOHAMED</s1>
</fA11><fA11 i1="02" i2="1"><s1>DREES (Ehab A.)</s1>
</fA11><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>
</fA14><fA20><s1>2054-2065</s1>
</fA20><fA21><s1>2010</s1>
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<s2>17423</s2>
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</fA66><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><fC02 i1="01" i2="X"><s0>002A31</s0>
</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>
<s2>NS</s2>
</fC07><fN21><s1>172</s1>
</fN21><fN44 i1="01"><s1>OTO</s1>
</fN44><fN82><s1>OTO</s1>
</fN82><server><NO>PASCAL 10-0270833 INIST</NO>
<ET>Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora</ET>
<AU>SALEH AHMED MOHAMED; DREES (Ehab A.); EL-BADRY (Mohamed O.); FAHMY (Afaf S.)</AU>
<AF>Molecular Biology Department, National Research Center/Dokki. Cairo/Egypte (1 aut., 3 aut., 4 aut.); Biochemistry division, Chemistry Department, Faculty of Science, Fayoum University/Fayoum/Egypte (2 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Applied biochemistry and biotechnology; ISSN 0273-2289; Coden ABIBDL; Allemagne; Da. 2010; Vol. 160; No. 7; Pp. 2054-2065; Bibl. 32 ref.</SO>
<LA>Anglais</LA>
<EA>-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.</EA><CC>002A31; 215</CC>
<FD>α-Amylase; Purification; Citrus sinensis</FD>
<FG>Glycosidases; Glycosylases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta</FG>
<ED>α-Amylase; Purification; Citrus sinensis</ED>
<EG>Glycosidases; Glycosylases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta</EG>
<SD>α-Amylase; Purificación; Citrus sinensis</SD>
<LO>INIST-17423.354000181751000190</LO>
<ID>10-0270833</ID>
</server>
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