Separation and characterization of a salt-dependent pectin methylesterase from Citrus sinensis Var. valencia fruit tissue
Identifieur interne : 000755 ( PascalFrancis/Corpus ); précédent : 000754; suivant : 000756Separation and characterization of a salt-dependent pectin methylesterase from Citrus sinensis Var. valencia fruit tissue
Auteurs : Randall G. Cameron ; Brett J. Savary ; Arland T. Hotchkiss ; Marshall L. Fishman ; H. O. A. K. Chau ; Robert A. Baker ; Karel GrohmannSource :
- Journal of agricultural and food chemistry : (Print) [ 0021-8561 ] ; 2003.
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Abstract
A pectin methylesterase (PME) from sweet orange fruit rag tissue, which does not destabilize citrus juice cloud, has been characterized. It is a salt-dependent PME (type II) and exhibits optimal activity between 0.1 and 0.2 M NaCI at pH 7.5. The pH optimum shifted to a more alkaline range as the salt molarity decreased (pH 8.5-9.5 at 50 mM NaCI). It has an apparent molecular mass of 32.4 kDa as determined by gel filtration chromatography, an apparent molecular mass of 33.5 kDa as determined by denaturing electrophoresis, and a pl of 10.1 and exhibits a single activity band after isoelectric focusing (IEF). It has a Km of 0.0487 mg/mL and a Vmax of 4.2378 nkat/mg of protein on 59% DE citrus pectin. Deblocking the N-terminus revealed a partial peptide composed of SVTPNV. Deesterification of non-calcium-sensitive pectin by 6.5% increased the calcium-sensitive pectin ratio (CSPR) from 0. 045 ± 0.011 to 0. 829 ± 0.033 but had little, if any, effect on pectin molecular weight. These properties indicate this enzyme will be useful for studying the PME mode of action as it relates to juice cloud destabilization.
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Format Inist (serveur)
| NO : | PASCAL 03-0344968 INIST |
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| ET : | Separation and characterization of a salt-dependent pectin methylesterase from Citrus sinensis Var. valencia fruit tissue |
| AU : | CAMERON (Randall G.); SAVARY (Brett J.); HOTCHKISS (Arland T.); FISHMAN (Marshall L.); CHAU (H. O. A. K.); BAKER (Robert A.); GROHMANN (Karel) |
| AF : | Citrus and Subtropical Products Laboratory, South Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue South N.W./Winter Haven, Florida 33881/Etats-Unis (1 aut.); Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane/Wyndmoor, Pennsylvania 19038/Etats-Unis (2 aut., 3 aut., 4 aut., 5 aut.) |
| DT : | Publication en série; Niveau analytique |
| SO : | Journal of agricultural and food chemistry : (Print); ISSN 0021-8561; Coden JAFCAU; Etats-Unis; Da. 2003; Vol. 51; No. 7; Pp. 2070-2075; Bibl. 39 ref. |
| LA : | Anglais |
| EA : | A pectin methylesterase (PME) from sweet orange fruit rag tissue, which does not destabilize citrus juice cloud, has been characterized. It is a salt-dependent PME (type II) and exhibits optimal activity between 0.1 and 0.2 M NaCI at pH 7.5. The pH optimum shifted to a more alkaline range as the salt molarity decreased (pH 8.5-9.5 at 50 mM NaCI). It has an apparent molecular mass of 32.4 kDa as determined by gel filtration chromatography, an apparent molecular mass of 33.5 kDa as determined by denaturing electrophoresis, and a pl of 10.1 and exhibits a single activity band after isoelectric focusing (IEF). It has a Km of 0.0487 mg/mL and a Vmax of 4.2378 nkat/mg of protein on 59% DE citrus pectin. Deblocking the N-terminus revealed a partial peptide composed of SVTPNV. Deesterification of non-calcium-sensitive pectin by 6.5% increased the calcium-sensitive pectin ratio (CSPR) from 0. 045 ± 0.011 to 0. 829 ± 0.033 but had little, if any, effect on pectin molecular weight. These properties indicate this enzyme will be useful for studying the PME mode of action as it relates to juice cloud destabilization. |
| CC : | 002A35B09 |
| FD : | Caractérisation; Séparation; Pectinesterase; Sensibilité résistance; Activité enzymatique; Citrus sinensis; Sel; Galacturonique acide; Pectine |
| FG : | Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Agrume; Fruit; Polyoside; Biopolymère |
| ED : | Characterization; Separation; Pectinesterase; Sensitivity resistance; Enzymatic activity; Citrus sinensis; Salt; Galacturonic acid; Pectin |
| EG : | Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Citrus fruit; Fruit; Polysaccharide; Biopolymer |
| SD : | Caracterización; Separación; Pectinesterase; Sensibilidad resistencia; Actividad enzimática; Citrus sinensis; Sal; Galacturónico ácido; Pectina |
| LO : | INIST-7332.354000109555090500 |
| ID : | 03-0344968 |
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Pascal:03-0344968Le document en format XML
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Cameron</name><affiliation><inist:fA14 i1="01"><s1>Citrus and Subtropical Products Laboratory, South Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue South N.W.</s1><s2>Winter Haven, Florida 33881</s2><s3>USA</s3><sZ>1 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Savary, Brett J" sort="Savary, Brett J" uniqKey="Savary B" first="Brett J." last="Savary">Brett J. Savary</name><affiliation><inist:fA14 i1="02"><s1>Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane</s1><s2>Wyndmoor, Pennsylvania 19038</s2><s3>USA</s3><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Hotchkiss, Arland T" sort="Hotchkiss, Arland T" uniqKey="Hotchkiss A" first="Arland T." last="Hotchkiss">Arland T. Hotchkiss</name><affiliation><inist:fA14 i1="02"><s1>Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane</s1><s2>Wyndmoor, Pennsylvania 19038</s2><s3>USA</s3><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Fishman, Marshall L" sort="Fishman, Marshall L" uniqKey="Fishman M" first="Marshall L." last="Fishman">Marshall L. Fishman</name><affiliation><inist:fA14 i1="02"><s1>Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane</s1><s2>Wyndmoor, Pennsylvania 19038</s2><s3>USA</s3><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Chau, H O A K" sort="Chau, H O A K" uniqKey="Chau H" first="H. O. A. K." last="Chau">H. O. A. K. Chau</name><affiliation><inist:fA14 i1="02"><s1>Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane</s1><s2>Wyndmoor, Pennsylvania 19038</s2><s3>USA</s3><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Baker, Robert A" sort="Baker, Robert A" uniqKey="Baker R" first="Robert A." last="Baker">Robert A. Baker</name></author><author><name sortKey="Grohmann, Karel" sort="Grohmann, Karel" uniqKey="Grohmann K" first="Karel" last="Grohmann">Karel Grohmann</name></author></analytic><series><title level="j" type="main">Journal of agricultural and food chemistry : (Print)</title><title level="j" type="abbreviated">J. agric. food chem. : (Print)</title><idno type="ISSN">0021-8561</idno><imprint><date when="2003">2003</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of agricultural and food chemistry : (Print)</title><title level="j" type="abbreviated">J. agric. food chem. : (Print)</title><idno type="ISSN">0021-8561</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Characterization</term><term>Citrus sinensis</term><term>Enzymatic activity</term><term>Galacturonic acid</term><term>Pectin</term><term>Pectinesterase</term><term>Salt</term><term>Sensitivity resistance</term><term>Separation</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Caractérisation</term><term>Séparation</term><term>Pectinesterase</term><term>Sensibilité résistance</term><term>Activité enzymatique</term><term>Citrus sinensis</term><term>Sel</term><term>Galacturonique acide</term><term>Pectine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A pectin methylesterase (PME) from sweet orange fruit rag tissue, which does not destabilize citrus juice cloud, has been characterized. It is a salt-dependent PME (type II) and exhibits optimal activity between 0.1 and 0.2 M NaCI at pH 7.5. The pH optimum shifted to a more alkaline range as the salt molarity decreased (pH 8.5-9.5 at 50 mM NaCI). It has an apparent molecular mass of 32.4 kDa as determined by gel filtration chromatography, an apparent molecular mass of 33.5 kDa as determined by denaturing electrophoresis, and a pl of 10.1 and exhibits a single activity band after isoelectric focusing (IEF). It has a K<sub>m</sub> of 0.0487 mg/mL and a V<sub>max</sub> of 4.2378 nkat/mg of protein on 59% DE citrus pectin. Deblocking the N-terminus revealed a partial peptide composed of SVTPNV. Deesterification of non-calcium-sensitive pectin by 6.5% increased the calcium-sensitive pectin ratio (CSPR) from 0. 045 ± 0.011 to 0. 829 ± 0.033 but had little, if any, effect on pectin molecular weight. These properties indicate this enzyme will be useful for studying the PME mode of action as it relates to juice cloud destabilization.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0021-8561</s0></fA01><fA02 i1="01"><s0>JAFCAU</s0></fA02><fA03 i2="1"><s0>J. agric. food chem. : (Print)</s0></fA03><fA05><s2>51</s2></fA05><fA06><s2>7</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Separation and characterization of a salt-dependent pectin methylesterase from Citrus sinensis Var. valencia fruit tissue</s1></fA08><fA11 i1="01" i2="1"><s1>CAMERON (Randall G.)</s1></fA11><fA11 i1="02" i2="1"><s1>SAVARY (Brett J.)</s1></fA11><fA11 i1="03" i2="1"><s1>HOTCHKISS (Arland T.)</s1></fA11><fA11 i1="04" i2="1"><s1>FISHMAN (Marshall L.)</s1></fA11><fA11 i1="05" i2="1"><s1>CHAU (H. O. A. K.)</s1></fA11><fA11 i1="06" i2="1"><s1>BAKER (Robert A.)</s1></fA11><fA11 i1="07" i2="1"><s1>GROHMANN (Karel)</s1></fA11><fA14 i1="01"><s1>Citrus and Subtropical Products Laboratory, South Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue South N.W.</s1><s2>Winter Haven, Florida 33881</s2><s3>USA</s3><sZ>1 aut.</sZ></fA14><fA14 i1="02"><s1>Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane</s1><s2>Wyndmoor, Pennsylvania 19038</s2><s3>USA</s3><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></fA14><fA20><s1>2070-2075</s1></fA20><fA21><s1>2003</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>7332</s2><s5>354000109555090500</s5></fA43><fA44><s0>0000</s0><s1>© 2003 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>39 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>03-0344968</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of agricultural and food chemistry : (Print)</s0></fA64><fA66 i1="01"><s0>USA</s0></fA66><fC01 i1="01" l="ENG"><s0>A pectin methylesterase (PME) from sweet orange fruit rag tissue, which does not destabilize citrus juice cloud, has been characterized. It is a salt-dependent PME (type II) and exhibits optimal activity between 0.1 and 0.2 M NaCI at pH 7.5. The pH optimum shifted to a more alkaline range as the salt molarity decreased (pH 8.5-9.5 at 50 mM NaCI). It has an apparent molecular mass of 32.4 kDa as determined by gel filtration chromatography, an apparent molecular mass of 33.5 kDa as determined by denaturing electrophoresis, and a pl of 10.1 and exhibits a single activity band after isoelectric focusing (IEF). It has a K<sub>m</sub> of 0.0487 mg/mL and a V<sub>max</sub> of 4.2378 nkat/mg of protein on 59% DE citrus pectin. Deblocking the N-terminus revealed a partial peptide composed of SVTPNV. Deesterification of non-calcium-sensitive pectin by 6.5% increased the calcium-sensitive pectin ratio (CSPR) from 0. 045 ± 0.011 to 0. 829 ± 0.033 but had little, if any, effect on pectin molecular weight. These properties indicate this enzyme will be useful for studying the PME mode of action as it relates to juice cloud destabilization.</s0></fC01><fC02 i1="01" i2="X"><s0>002A35B09</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Caractérisation</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Characterization</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Caracterización</s0><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Séparation</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Separation</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Separación</s0><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Pectinesterase</s0><s2>FE</s2><s5>10</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Pectinesterase</s0><s2>FE</s2><s5>10</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Pectinesterase</s0><s2>FE</s2><s5>10</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Sensibilité résistance</s0><s5>19</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Sensitivity resistance</s0><s5>19</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Sensibilidad resistencia</s0><s5>19</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Activité enzymatique</s0><s5>20</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Enzymatic activity</s0><s5>20</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Actividad enzimática</s0><s5>20</s5></fC03><fC03 i1="06" i2="X" l="FRE"><s0>Citrus sinensis</s0><s2>NS</s2><s5>24</s5></fC03><fC03 i1="06" i2="X" l="ENG"><s0>Citrus sinensis</s0><s2>NS</s2><s5>24</s5></fC03><fC03 i1="06" i2="X" l="SPA"><s0>Citrus sinensis</s0><s2>NS</s2><s5>24</s5></fC03><fC03 i1="07" i2="X" l="FRE"><s0>Sel</s0><s5>26</s5></fC03><fC03 i1="07" i2="X" l="ENG"><s0>Salt</s0><s5>26</s5></fC03><fC03 i1="07" i2="X" l="SPA"><s0>Sal</s0><s5>26</s5></fC03><fC03 i1="08" i2="X" l="FRE"><s0>Galacturonique acide</s0><s2>NK</s2><s5>28</s5></fC03><fC03 i1="08" i2="X" l="ENG"><s0>Galacturonic acid</s0><s2>NK</s2><s5>28</s5></fC03><fC03 i1="08" i2="X" l="SPA"><s0>Galacturónico ácido</s0><s2>NK</s2><s5>28</s5></fC03><fC03 i1="09" i2="X" l="FRE"><s0>Pectine</s0><s5>29</s5></fC03><fC03 i1="09" i2="X" l="ENG"><s0>Pectin</s0><s5>29</s5></fC03><fC03 i1="09" i2="X" l="SPA"><s0>Pectina</s0><s5>29</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Carboxylic ester hydrolases</s0><s2>FE</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Carboxylic ester hydrolases</s0><s2>FE</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Carboxylic ester hydrolases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Esterases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Esterases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Esterases</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></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Enzyme</s0></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Enzima</s0></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><fC07 i1="09" i2="X" l="FRE"><s0>Agrume</s0><s5>32</s5></fC07><fC07 i1="09" i2="X" l="ENG"><s0>Citrus fruit</s0><s5>32</s5></fC07><fC07 i1="09" i2="X" l="SPA"><s0>Agrios</s0><s5>32</s5></fC07><fC07 i1="10" i2="X" l="FRE"><s0>Fruit</s0><s5>33</s5></fC07><fC07 i1="10" i2="X" l="ENG"><s0>Fruit</s0><s5>33</s5></fC07><fC07 i1="10" i2="X" l="SPA"><s0>Fruto</s0><s5>33</s5></fC07><fC07 i1="11" i2="X" l="FRE"><s0>Polyoside</s0><s2>NK</s2><s5>34</s5></fC07><fC07 i1="11" i2="X" l="ENG"><s0>Polysaccharide</s0><s2>NK</s2><s5>34</s5></fC07><fC07 i1="11" i2="X" l="SPA"><s0>Poliósido</s0><s2>NK</s2><s5>34</s5></fC07><fC07 i1="12" i2="X" l="FRE"><s0>Biopolymère</s0><s5>54</s5></fC07><fC07 i1="12" i2="X" l="ENG"><s0>Biopolymer</s0><s5>54</s5></fC07><fC07 i1="12" i2="X" l="SPA"><s0>Biopolímero</s0><s5>54</s5></fC07><fN21><s1>246</s1></fN21><fN82><s1>PSI</s1></fN82></pA></standard><server><NO>PASCAL 03-0344968 INIST</NO><ET>Separation and characterization of a salt-dependent pectin methylesterase from Citrus sinensis Var. valencia fruit tissue</ET><AU>CAMERON (Randall G.); SAVARY (Brett J.); HOTCHKISS (Arland T.); FISHMAN (Marshall L.); CHAU (H. O. A. K.); BAKER (Robert A.); GROHMANN (Karel)</AU><AF>Citrus and Subtropical Products Laboratory, South Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue South N.W./Winter Haven, Florida 33881/Etats-Unis (1 aut.); Eastern Regional Research Center, North Atlantic Area, Agricultural Research Service, U.S. Department of Agriculture, 600 Mermaid Lane/Wyndmoor, Pennsylvania 19038/Etats-Unis (2 aut., 3 aut., 4 aut., 5 aut.)</AF><DT>Publication en série; Niveau analytique</DT><SO>Journal of agricultural and food chemistry : (Print); ISSN 0021-8561; Coden JAFCAU; Etats-Unis; Da. 2003; Vol. 51; No. 7; Pp. 2070-2075; Bibl. 39 ref.</SO><LA>Anglais</LA><EA>A pectin methylesterase (PME) from sweet orange fruit rag tissue, which does not destabilize citrus juice cloud, has been characterized. It is a salt-dependent PME (type II) and exhibits optimal activity between 0.1 and 0.2 M NaCI at pH 7.5. The pH optimum shifted to a more alkaline range as the salt molarity decreased (pH 8.5-9.5 at 50 mM NaCI). It has an apparent molecular mass of 32.4 kDa as determined by gel filtration chromatography, an apparent molecular mass of 33.5 kDa as determined by denaturing electrophoresis, and a pl of 10.1 and exhibits a single activity band after isoelectric focusing (IEF). It has a K<sub>m</sub> of 0.0487 mg/mL and a V<sub>max</sub> of 4.2378 nkat/mg of protein on 59% DE citrus pectin. Deblocking the N-terminus revealed a partial peptide composed of SVTPNV. Deesterification of non-calcium-sensitive pectin by 6.5% increased the calcium-sensitive pectin ratio (CSPR) from 0. 045 ± 0.011 to 0. 829 ± 0.033 but had little, if any, effect on pectin molecular weight. These properties indicate this enzyme will be useful for studying the PME mode of action as it relates to juice cloud destabilization.</EA><CC>002A35B09</CC><FD>Caractérisation; Séparation; Pectinesterase; Sensibilité résistance; Activité enzymatique; Citrus sinensis; Sel; Galacturonique acide; Pectine</FD><FG>Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Agrume; Fruit; Polyoside; Biopolymère</FG><ED>Characterization; Separation; Pectinesterase; Sensitivity resistance; Enzymatic activity; Citrus sinensis; Salt; Galacturonic acid; Pectin</ED><EG>Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Citrus fruit; Fruit; Polysaccharide; Biopolymer</EG><SD>Caracterización; Separación; Pectinesterase; Sensibilidad resistencia; Actividad enzimática; Citrus sinensis; Sal; Galacturónico ácido; Pectina</SD><LO>INIST-7332.354000109555090500</LO><ID>03-0344968</ID></server></inist></record>Pour manipuler ce document sous Unix (Dilib)
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