OrangerV1, PascalFrancis, Corpus, bibRecord, 000868

Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue

Identifieur interne : 000868 ( PascalFrancis/Corpus ); précédent : 000867; suivant : 000869

Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue

Auteurs : Randall G. Cameron ; John A. Manthey ; Robert A. Baker ; Karel Grohmann

Source :

Journal of agricultural and food chemistry : (Print) [ 0021-8561 ] ; 2001.

RBID : Pascal:02-0002042

Descripteurs français

Pascal (Inist)
- Purification, Caractérisation, β-Glucosidase, Spécificité tissu, Fruit, Activité enzymatique, Spécificité substrat, Activité catalytique, pH optimum, Citrus sinensis, Masse moléculaire, Jus d'orange, Sous produit.

English descriptors

KwdEn :
- By product, Catalyst activity, Characterization, Citrus sinensis, Enzymatic activity, Fruit, Molecular mass, Optimum pH, Orange juice, Purification, Substrate specificity, Tissue specificity, β-Glucosidase.

Abstract

A preliminary survey demonstrated activity for α-D-glucosidase, α-D-mannosidase, α-L-arabinosidase, β-D-glucosidase, β-D-xylosidase, and β-D-galactosidase in orange fruit flavedo and albedo tissue, α-L-Rhamnosidase was not detected. Subsequently, a β-glucosidase was purified from mature fruit rag tissue (composed of intersegmental septa, squeezed juice sacs, and fruit core tissue) of Citrus sinensis var. Valencia. The β-glucosidase exhibited low levels of activity against p-nitrophenyl-β-D-fucopyranoside (13.5%) and p-nitrophenyl-a-D-glucopyranoside (7.0%), compared to its activity against p-nitrophenyl-β-D-glucopyranoside (pNPG, 100%). The enzyme was purified by a combination of ion exchange (anion and cation) and gel filtration (Superdex and Toyopearl HW-55S) chromatography. It has an apparent molecular mass of 64 kDa by denaturing electrophoresis or 55 kDa by gel filtration chromatography (BioGel P-100). Hydrolysis of pNPG demonstrated a pH optimum between 4.5 and 5.5. At pH 5.0 the temperature optimum was 40 °C. At pH 5.0 and 40 °C the K_m forpNPG was 0.1146 mM and it had a V_max of 5.2792 nkatal.mg^-1 protein (katal = 0.06 International Units = the amount of enzyme that produces, under standard conditions, one μmol of product per min). Of the substrates tested, the enzyme was most active against the disaccharide cellobiose (1⇒4), but was not active against p-nitrophenyl-β-D-cellobioside. High levels of activity also were observed with the disaccharides laminaribiose (1⇒3), gentiobiose (1⇒6), and sophorose (1⇒2). Activity greater than that observed with pNPG was obtained with the flavonoids hesperetin-7-glucoside and prunin (naringenin-7-glucoside), salicin, mandelonitrile-β-D-glucoside (a cyanogenic substrate), and sinigrin (a glucosinolate). The enzyme was not active against amygdalin, coniferin, or limonin glucoside.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 0021-8561`
A02	`01`			`@0 JAFCAU`
A03		`1`		`@0 J. agric. food chem. : (Print)`
A05				`@2 49`
A06				`@2 9`
A08	`01`	`1`	`ENG`	`@1 Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue`
A11	`01`	`1`		`@1 CAMERON (Randall G.)`
A11	`02`	`1`		`@1 MANTHEY (John A.)`
A11	`03`	`1`		`@1 BAKER (Robert A.)`
A11	`04`	`1`		`@1 GROHMANN (Karel)`
A14	`01`			`@1 Citrus and Subtropical Products Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue S NW @2 Winter Haven, Florida 33881 @3 USA @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut.`
A20				`@1 4457-4462`
A21				`@1 2001`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 7332 @5 354000099550560530`
A44				`@0 0000 @1 © 2002 INIST-CNRS. All rights reserved.`
A45				`@0 21 ref.`
A47	`01`	`1`		`@0 02-0002042`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Journal of agricultural and food chemistry : (Print)`
A66	`01`			`@0 USA`
C01	`01`		`ENG`	@0 A preliminary survey demonstrated activity for α-D-glucosidase, α-D-mannosidase, α-L-arabinosidase, β-D-glucosidase, β-D-xylosidase, and β-D-galactosidase in orange fruit flavedo and albedo tissue, α-L-Rhamnosidase was not detected. Subsequently, a β-glucosidase was purified from mature fruit rag tissue (composed of intersegmental septa, squeezed juice sacs, and fruit core tissue) of Citrus sinensis var. Valencia. The β-glucosidase exhibited low levels of activity against p-nitrophenyl-β-D-fucopyranoside (13.5%) and p-nitrophenyl-a-D-glucopyranoside (7.0%), compared to its activity against p-nitrophenyl-β-D-glucopyranoside (pNPG, 100%). The enzyme was purified by a combination of ion exchange (anion and cation) and gel filtration (Superdex and Toyopearl HW-55S) chromatography. It has an apparent molecular mass of 64 kDa by denaturing electrophoresis or 55 kDa by gel filtration chromatography (BioGel P-100). Hydrolysis of pNPG demonstrated a pH optimum between 4.5 and 5.5. At pH 5.0 the temperature optimum was 40 °C. At pH 5.0 and 40 °C the K_m forpNPG was 0.1146 mM and it had a V_max of 5.2792 nkatal.mg^-1 protein (katal = 0.06 International Units = the amount of enzyme that produces, under standard conditions, one μmol of product per min). Of the substrates tested, the enzyme was most active against the disaccharide cellobiose (1⇒4), but was not active against p-nitrophenyl-β-D-cellobioside. High levels of activity also were observed with the disaccharides laminaribiose (1⇒3), gentiobiose (1⇒6), and sophorose (1⇒2). Activity greater than that observed with pNPG was obtained with the flavonoids hesperetin-7-glucoside and prunin (naringenin-7-glucoside), salicin, mandelonitrile-β-D-glucoside (a cyanogenic substrate), and sinigrin (a glucosinolate). The enzyme was not active against amygdalin, coniferin, or limonin glucoside.
C02	`01`	`X`		`@0 002A32E05G`
C02	`02`	`X`		`@0 002A35B09`
C03	`01`	`X`	`FRE`	`@0 Purification @5 01`
C03	`01`	`X`	`ENG`	`@0 Purification @5 01`
C03	`01`	`X`	`SPA`	`@0 Purificación @5 01`
C03	`02`	`X`	`FRE`	`@0 Caractérisation @5 02`
C03	`02`	`X`	`ENG`	`@0 Characterization @5 02`
C03	`02`	`X`	`SPA`	`@0 Caracterización @5 02`
C03	`03`	`X`	`FRE`	`@0 β-Glucosidase @2 FE @5 03 @6 «β»-Glucosidase`
C03	`03`	`X`	`ENG`	`@0 β-Glucosidase @2 FE @5 03 @6 «β»-Glucosidase`
C03	`03`	`X`	`SPA`	`@0 β-Glucosidase @2 FE @5 03 @6 «β»-Glucosidase`
C03	`04`	`X`	`FRE`	`@0 Spécificité tissu @5 04`
C03	`04`	`X`	`ENG`	`@0 Tissue specificity @5 04`
C03	`04`	`X`	`SPA`	`@0 Especificidad tejido @5 04`
C03	`05`	`X`	`FRE`	`@0 Fruit @5 05`
C03	`05`	`X`	`ENG`	`@0 Fruit @5 05`
C03	`05`	`X`	`SPA`	`@0 Fruto @5 05`
C03	`06`	`X`	`FRE`	`@0 Activité enzymatique @5 06`
C03	`06`	`X`	`ENG`	`@0 Enzymatic activity @5 06`
C03	`06`	`X`	`SPA`	`@0 Actividad enzimática @5 06`
C03	`07`	`X`	`FRE`	`@0 Spécificité substrat @5 07`
C03	`07`	`X`	`ENG`	`@0 Substrate specificity @5 07`
C03	`07`	`X`	`SPA`	`@0 Especificidad sustrato @5 07`
C03	`08`	`X`	`FRE`	`@0 Activité catalytique @5 08`
C03	`08`	`X`	`ENG`	`@0 Catalyst activity @5 08`
C03	`08`	`X`	`SPA`	`@0 Actividad catalítica @5 08`
C03	`09`	`X`	`FRE`	`@0 pH optimum @5 09`
C03	`09`	`X`	`ENG`	`@0 Optimum pH @5 09`
C03	`09`	`X`	`SPA`	`@0 pH óptimo @5 09`
C03	`10`	`X`	`FRE`	`@0 Citrus sinensis @2 NS @5 10`
C03	`10`	`X`	`ENG`	`@0 Citrus sinensis @2 NS @5 10`
C03	`10`	`X`	`SPA`	`@0 Citrus sinensis @2 NS @5 10`
C03	`11`	`X`	`FRE`	`@0 Masse moléculaire @5 33`
C03	`11`	`X`	`ENG`	`@0 Molecular mass @5 33`
C03	`11`	`X`	`SPA`	`@0 Masa molecular @5 33`
C03	`12`	`X`	`FRE`	`@0 Jus d'orange @5 34`
C03	`12`	`X`	`ENG`	`@0 Orange juice @5 34`
C03	`12`	`X`	`SPA`	`@0 Zugo naranja @5 34`
C03	`13`	`X`	`FRE`	`@0 Sous produit @5 35`
C03	`13`	`X`	`ENG`	`@0 By product @5 35`
C03	`13`	`X`	`SPA`	`@0 Subproducto @5 35`
C07	`01`	`X`	`FRE`	`@0 O-Glycosidases @2 FE @6 «O»-Glycosidases`
C07	`01`	`X`	`ENG`	`@0 O-Glycosidases @2 FE @6 «O»-Glycosidases`
C07	`01`	`X`	`SPA`	`@0 O-Glycosidases @2 FE @6 «O»-Glycosidases`
C07	`02`	`X`	`FRE`	`@0 Glycosidases @2 FE`
C07	`02`	`X`	`ENG`	`@0 Glycosidases @2 FE`
C07	`02`	`X`	`SPA`	`@0 Glycosidases @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`
C07	`04`	`X`	`ENG`	`@0 Enzyme`
C07	`04`	`X`	`SPA`	`@0 Enzima`
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`
C07	`09`	`X`	`FRE`	`@0 Agrume @5 39`
C07	`09`	`X`	`ENG`	`@0 Citrus fruit @5 39`
C07	`09`	`X`	`SPA`	`@0 Agrios @5 39`
C07	`10`	`X`	`FRE`	`@0 Arbre fruitier @5 40`
C07	`10`	`X`	`ENG`	`@0 Fruit tree @5 40`
C07	`10`	`X`	`SPA`	`@0 Arbol frutal @5 40`
N21				`@1 001`

Format Inist (serveur)

NO :	PASCAL 02-0002042 INIST
ET :	Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue
AU :	CAMERON (Randall G.); MANTHEY (John A.); BAKER (Robert A.); GROHMANN (Karel)
AF :	Citrus and Subtropical Products Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue S NW/Winter Haven, Florida 33881/Etats-Unis (1 aut., 2 aut., 3 aut., 4 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of agricultural and food chemistry : (Print); ISSN 0021-8561; Coden JAFCAU; Etats-Unis; Da. 2001; Vol. 49; No. 9; Pp. 4457-4462; Bibl. 21 ref.
LA :	Anglais
EA :	A preliminary survey demonstrated activity for α-D-glucosidase, α-D-mannosidase, α-L-arabinosidase, β-D-glucosidase, β-D-xylosidase, and β-D-galactosidase in orange fruit flavedo and albedo tissue, α-L-Rhamnosidase was not detected. Subsequently, a β-glucosidase was purified from mature fruit rag tissue (composed of intersegmental septa, squeezed juice sacs, and fruit core tissue) of Citrus sinensis var. Valencia. The β-glucosidase exhibited low levels of activity against p-nitrophenyl-β-D-fucopyranoside (13.5%) and p-nitrophenyl-a-D-glucopyranoside (7.0%), compared to its activity against p-nitrophenyl-β-D-glucopyranoside (pNPG, 100%). The enzyme was purified by a combination of ion exchange (anion and cation) and gel filtration (Superdex and Toyopearl HW-55S) chromatography. It has an apparent molecular mass of 64 kDa by denaturing electrophoresis or 55 kDa by gel filtration chromatography (BioGel P-100). Hydrolysis of pNPG demonstrated a pH optimum between 4.5 and 5.5. At pH 5.0 the temperature optimum was 40 °C. At pH 5.0 and 40 °C the K_m forpNPG was 0.1146 mM and it had a V_max of 5.2792 nkatal.mg^-1 protein (katal = 0.06 International Units = the amount of enzyme that produces, under standard conditions, one μmol of product per min). Of the substrates tested, the enzyme was most active against the disaccharide cellobiose (1⇒4), but was not active against p-nitrophenyl-β-D-cellobioside. High levels of activity also were observed with the disaccharides laminaribiose (1⇒3), gentiobiose (1⇒6), and sophorose (1⇒2). Activity greater than that observed with pNPG was obtained with the flavonoids hesperetin-7-glucoside and prunin (naringenin-7-glucoside), salicin, mandelonitrile-β-D-glucoside (a cyanogenic substrate), and sinigrin (a glucosinolate). The enzyme was not active against amygdalin, coniferin, or limonin glucoside.
CC :	002A32E05G; 002A35B09
FD :	Purification; Caractérisation; β-Glucosidase; Spécificité tissu; Fruit; Activité enzymatique; Spécificité substrat; Activité catalytique; pH optimum; Citrus sinensis; Masse moléculaire; Jus d'orange; Sous produit
FG :	O-Glycosidases; Glycosidases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Agrume; Arbre fruitier
ED :	Purification; Characterization; β-Glucosidase; Tissue specificity; Fruit; Enzymatic activity; Substrate specificity; Catalyst activity; Optimum pH; Citrus sinensis; Molecular mass; Orange juice; By product
EG :	O-Glycosidases; Glycosidases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Citrus fruit; Fruit tree
SD :	Purificación; Caracterización; β-Glucosidase; Especificidad tejido; Fruto; Actividad enzimática; Especificidad sustrato; Actividad catalítica; pH óptimo; Citrus sinensis; Masa molecular; Zugo naranja; Subproducto
LO :	INIST-7332.354000099550560530
ID :	02-0002042

Links to Exploration step

Pascal:02-0002042

Le document en format XML

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<term>Enzymatic activity</term>
<term>Fruit</term>
<term>Molecular mass</term>
<term>Optimum pH</term>
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<term>Purification</term>
<term>Substrate specificity</term>
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<term>Activité enzymatique</term>
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<term>Activité catalytique</term>
<term>pH optimum</term>
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<front><div type="abstract" xml:lang="en">A preliminary survey demonstrated activity for α-D-glucosidase, α-D-mannosidase, α-L-arabinosidase, β-D-glucosidase, β-D-xylosidase, and β-D-galactosidase in orange fruit flavedo and albedo tissue, α-L-Rhamnosidase was not detected. Subsequently, a β-glucosidase was purified from mature fruit rag tissue (composed of intersegmental septa, squeezed juice sacs, and fruit core tissue) of Citrus sinensis var. Valencia. The β-glucosidase exhibited low levels of activity against p-nitrophenyl-β-D-fucopyranoside (13.5%) and p-nitrophenyl-a-D-glucopyranoside (7.0%), compared to its activity against p-nitrophenyl-β-D-glucopyranoside (pNPG, 100%). The enzyme was purified by a combination of ion exchange (anion and cation) and gel filtration (Superdex and Toyopearl HW-55S) chromatography. It has an apparent molecular mass of 64 kDa by denaturing electrophoresis or 55 kDa by gel filtration chromatography (BioGel P-100). Hydrolysis of pNPG demonstrated a pH optimum between 4.5 and 5.5. At pH 5.0 the temperature optimum was 40 °C. At pH 5.0 and 40 °C the K<sub>m</sub>
 forpNPG was 0.1146 mM and it had a V<sub>max</sub>
 of 5.2792 nkatal.mg<sup>-1</sup>
 protein (katal = 0.06 International Units = the amount of enzyme that produces, under standard conditions, one μmol of product per min). Of the substrates tested, the enzyme was most active against the disaccharide cellobiose (1⇒4), but was not active against p-nitrophenyl-β-D-cellobioside. High levels of activity also were observed with the disaccharides laminaribiose (1⇒3), gentiobiose (1⇒6), and sophorose (1⇒2). Activity greater than that observed with pNPG was obtained with the flavonoids hesperetin-7-glucoside and prunin (naringenin-7-glucoside), salicin, mandelonitrile-β-D-glucoside (a cyanogenic substrate), and sinigrin (a glucosinolate). The enzyme was not active against amygdalin, coniferin, or limonin glucoside.</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>49</s2>
</fA05>
<fA06><s2>9</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Purification and characterization of a beta-glucosidase 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>MANTHEY (John A.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>BAKER (Robert A.)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>GROHMANN (Karel)</s1>
</fA11>
<fA14 i1="01"><s1>Citrus and Subtropical Products Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue S NW</s1>
<s2>Winter Haven, Florida 33881</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
</fA14>
<fA20><s1>4457-4462</s1>
</fA20>
<fA21><s1>2001</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>7332</s2>
<s5>354000099550560530</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2002 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>21 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>02-0002042</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 preliminary survey demonstrated activity for α-D-glucosidase, α-D-mannosidase, α-L-arabinosidase, β-D-glucosidase, β-D-xylosidase, and β-D-galactosidase in orange fruit flavedo and albedo tissue, α-L-Rhamnosidase was not detected. Subsequently, a β-glucosidase was purified from mature fruit rag tissue (composed of intersegmental septa, squeezed juice sacs, and fruit core tissue) of Citrus sinensis var. Valencia. The β-glucosidase exhibited low levels of activity against p-nitrophenyl-β-D-fucopyranoside (13.5%) and p-nitrophenyl-a-D-glucopyranoside (7.0%), compared to its activity against p-nitrophenyl-β-D-glucopyranoside (pNPG, 100%). The enzyme was purified by a combination of ion exchange (anion and cation) and gel filtration (Superdex and Toyopearl HW-55S) chromatography. It has an apparent molecular mass of 64 kDa by denaturing electrophoresis or 55 kDa by gel filtration chromatography (BioGel P-100). Hydrolysis of pNPG demonstrated a pH optimum between 4.5 and 5.5. At pH 5.0 the temperature optimum was 40 °C. At pH 5.0 and 40 °C the K<sub>m</sub>
 forpNPG was 0.1146 mM and it had a V<sub>max</sub>
 of 5.2792 nkatal.mg<sup>-1</sup>
 protein (katal = 0.06 International Units = the amount of enzyme that produces, under standard conditions, one μmol of product per min). Of the substrates tested, the enzyme was most active against the disaccharide cellobiose (1⇒4), but was not active against p-nitrophenyl-β-D-cellobioside. High levels of activity also were observed with the disaccharides laminaribiose (1⇒3), gentiobiose (1⇒6), and sophorose (1⇒2). Activity greater than that observed with pNPG was obtained with the flavonoids hesperetin-7-glucoside and prunin (naringenin-7-glucoside), salicin, mandelonitrile-β-D-glucoside (a cyanogenic substrate), and sinigrin (a glucosinolate). The enzyme was not active against amygdalin, coniferin, or limonin glucoside.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A32E05G</s0>
</fC02>
<fC02 i1="02" i2="X"><s0>002A35B09</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Purification</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Purification</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Purificación</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Caractérisation</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Characterization</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Caracterización</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>β-Glucosidase</s0>
<s2>FE</s2>
<s5>03</s5>
<s6>«β»-Glucosidase</s6>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>β-Glucosidase</s0>
<s2>FE</s2>
<s5>03</s5>
<s6>«β»-Glucosidase</s6>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>β-Glucosidase</s0>
<s2>FE</s2>
<s5>03</s5>
<s6>«β»-Glucosidase</s6>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Spécificité tissu</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Tissue specificity</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Especificidad tejido</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Fruit</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Fruit</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Fruto</s0>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Activité enzymatique</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Enzymatic activity</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Actividad enzimática</s0>
<s5>06</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Spécificité substrat</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Substrate specificity</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Especificidad sustrato</s0>
<s5>07</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Activité catalytique</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Catalyst activity</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Actividad catalítica</s0>
<s5>08</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>pH optimum</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Optimum pH</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>pH óptimo</s0>
<s5>09</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Citrus sinensis</s0>
<s2>NS</s2>
<s5>10</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Citrus sinensis</s0>
<s2>NS</s2>
<s5>10</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Citrus sinensis</s0>
<s2>NS</s2>
<s5>10</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Masse moléculaire</s0>
<s5>33</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Molecular mass</s0>
<s5>33</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Masa molecular</s0>
<s5>33</s5>
</fC03>
<fC03 i1="12" i2="X" l="FRE"><s0>Jus d'orange</s0>
<s5>34</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Orange juice</s0>
<s5>34</s5>
</fC03>
<fC03 i1="12" i2="X" l="SPA"><s0>Zugo naranja</s0>
<s5>34</s5>
</fC03>
<fC03 i1="13" i2="X" l="FRE"><s0>Sous produit</s0>
<s5>35</s5>
</fC03>
<fC03 i1="13" i2="X" l="ENG"><s0>By product</s0>
<s5>35</s5>
</fC03>
<fC03 i1="13" i2="X" l="SPA"><s0>Subproducto</s0>
<s5>35</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>O-Glycosidases</s0>
<s2>FE</s2>
<s6>«O»-Glycosidases</s6>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>O-Glycosidases</s0>
<s2>FE</s2>
<s6>«O»-Glycosidases</s6>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>O-Glycosidases</s0>
<s2>FE</s2>
<s6>«O»-Glycosidases</s6>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Glycosidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Glycosidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Glycosidases</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>39</s5>
</fC07>
<fC07 i1="09" i2="X" l="ENG"><s0>Citrus fruit</s0>
<s5>39</s5>
</fC07>
<fC07 i1="09" i2="X" l="SPA"><s0>Agrios</s0>
<s5>39</s5>
</fC07>
<fC07 i1="10" i2="X" l="FRE"><s0>Arbre fruitier</s0>
<s5>40</s5>
</fC07>
<fC07 i1="10" i2="X" l="ENG"><s0>Fruit tree</s0>
<s5>40</s5>
</fC07>
<fC07 i1="10" i2="X" l="SPA"><s0>Arbol frutal</s0>
<s5>40</s5>
</fC07>
<fN21><s1>001</s1>
</fN21>
</pA>
</standard>
<server><NO>PASCAL 02-0002042 INIST</NO>
<ET>Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue</ET>
<AU>CAMERON (Randall G.); MANTHEY (John A.); BAKER (Robert A.); GROHMANN (Karel)</AU>
<AF>Citrus and Subtropical Products Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 600 Avenue S NW/Winter Haven, Florida 33881/Etats-Unis (1 aut., 2 aut., 3 aut., 4 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. 2001; Vol. 49; No. 9; Pp. 4457-4462; Bibl. 21 ref.</SO>
<LA>Anglais</LA>
<EA>A preliminary survey demonstrated activity for α-D-glucosidase, α-D-mannosidase, α-L-arabinosidase, β-D-glucosidase, β-D-xylosidase, and β-D-galactosidase in orange fruit flavedo and albedo tissue, α-L-Rhamnosidase was not detected. Subsequently, a β-glucosidase was purified from mature fruit rag tissue (composed of intersegmental septa, squeezed juice sacs, and fruit core tissue) of Citrus sinensis var. Valencia. The β-glucosidase exhibited low levels of activity against p-nitrophenyl-β-D-fucopyranoside (13.5%) and p-nitrophenyl-a-D-glucopyranoside (7.0%), compared to its activity against p-nitrophenyl-β-D-glucopyranoside (pNPG, 100%). The enzyme was purified by a combination of ion exchange (anion and cation) and gel filtration (Superdex and Toyopearl HW-55S) chromatography. It has an apparent molecular mass of 64 kDa by denaturing electrophoresis or 55 kDa by gel filtration chromatography (BioGel P-100). Hydrolysis of pNPG demonstrated a pH optimum between 4.5 and 5.5. At pH 5.0 the temperature optimum was 40 °C. At pH 5.0 and 40 °C the K<sub>m</sub>
 forpNPG was 0.1146 mM and it had a V<sub>max</sub>
 of 5.2792 nkatal.mg<sup>-1</sup>
 protein (katal = 0.06 International Units = the amount of enzyme that produces, under standard conditions, one μmol of product per min). Of the substrates tested, the enzyme was most active against the disaccharide cellobiose (1⇒4), but was not active against p-nitrophenyl-β-D-cellobioside. High levels of activity also were observed with the disaccharides laminaribiose (1⇒3), gentiobiose (1⇒6), and sophorose (1⇒2). Activity greater than that observed with pNPG was obtained with the flavonoids hesperetin-7-glucoside and prunin (naringenin-7-glucoside), salicin, mandelonitrile-β-D-glucoside (a cyanogenic substrate), and sinigrin (a glucosinolate). The enzyme was not active against amygdalin, coniferin, or limonin glucoside.</EA>
<CC>002A32E05G; 002A35B09</CC>
<FD>Purification; Caractérisation; β-Glucosidase; Spécificité tissu; Fruit; Activité enzymatique; Spécificité substrat; Activité catalytique; pH optimum; Citrus sinensis; Masse moléculaire; Jus d'orange; Sous produit</FD>
<FG>O-Glycosidases; Glycosidases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Agrume; Arbre fruitier</FG>
<ED>Purification; Characterization; β-Glucosidase; Tissue specificity; Fruit; Enzymatic activity; Substrate specificity; Catalyst activity; Optimum pH; Citrus sinensis; Molecular mass; Orange juice; By product</ED>
<EG>O-Glycosidases; Glycosidases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta; Citrus fruit; Fruit tree</EG>
<SD>Purificación; Caracterización; β-Glucosidase; Especificidad tejido; Fruto; Actividad enzimática; Especificidad sustrato; Actividad catalítica; pH óptimo; Citrus sinensis; Masa molecular; Zugo naranja; Subproducto</SD>
<LO>INIST-7332.354000099550560530</LO>
<ID>02-0002042</ID>
</server>
</inist>
</record>

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Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue

Purification and characterization of a beta-glucosidase from Citrus sinensis var. valencia fruit tissue

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