Structural Characterization of the Thermally Tolerant Pectin Methylesterase Purified from Citrus sinensis Fruit and Its Gene Sequence
Identifieur interne : 000028 ( PascalFrancis/Corpus ); précédent : 000027; suivant : 000029Structural Characterization of the Thermally Tolerant Pectin Methylesterase Purified from Citrus sinensis Fruit and Its Gene Sequence
Auteurs : Brett J. Savary ; Prasanna Vasu ; Randall G. Cameron ; T. Gregory Mccollum ; Alberto NunezSource :
- Journal of agricultural and food chemistry : (Print) [ 0021-8561 ] ; 2013.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
Despite the longstanding importance of the thermally tolerant pectin methylesterase (TT-PME) activity in citrus juice processing and product quality, the unequivocal identification of the protein and its corresponding gene has remained elusive. TT-PME was purified from sweet orange [Citrus sinensis (L.) Osbeck] finisher pulp (8.0 mg/1.3 kg tissue) with an improved purification scheme that provided 20-fold increased enzyme yield over previous results. Structural characterization of electrophoretically pure TT-PME by MALDI-TOF MS determined molecular masses of approximately 47900 and 53000 Da for two principal glycoisoforms. De novo sequences generated from tryptic peptides by MALDI-TOF/TOF MS matched multiple anonymous Citrus EST cDNA accessions. The complete tt-pme cDNA (1710 base pair) was cloned from a fruit mRNA library using RT- and RLM-RACE PCR. Citrus TT-PME is a novel isoform that showed higher sequence identity with the multiply glycosylated kiwifruit PME than to previously described Citrus thermally labile PME isoforms.
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Format Inist (serveur)
NO : | PASCAL 14-0041424 INIST |
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ET : | Structural Characterization of the Thermally Tolerant Pectin Methylesterase Purified from Citrus sinensis Fruit and Its Gene Sequence |
AU : | SAVARY (Brett J.); VASU (Prasanna); CAMERON (Randall G.); MCCOLLUM (T. Gregory); NUNEZ (Alberto) |
AF : | Eastern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, Wyndmoor/Pennsylvania 19038/Etats-Unis (1 aut., 5 aut.); Arkansas Biosciences Institute, Arkansas State University, P.O. Box 639, State University/Arkansas 72467/Etats-Unis (1 aut., 2 aut.); Food Safety and Analytical Quality Control Laboratory, Central Food Technological Research Institute, CSIR/Mysore 570 020/Inde (2 aut.); U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 2001 South Rock Road/Fort Pierce, Florida 34945/Etats-Unis (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. 2013; Vol. 61; No. 51; Pp. 12711-12719; Bibl. 44 ref. |
LA : | Anglais |
EA : | Despite the longstanding importance of the thermally tolerant pectin methylesterase (TT-PME) activity in citrus juice processing and product quality, the unequivocal identification of the protein and its corresponding gene has remained elusive. TT-PME was purified from sweet orange [Citrus sinensis (L.) Osbeck] finisher pulp (8.0 mg/1.3 kg tissue) with an improved purification scheme that provided 20-fold increased enzyme yield over previous results. Structural characterization of electrophoretically pure TT-PME by MALDI-TOF MS determined molecular masses of approximately 47900 and 53000 Da for two principal glycoisoforms. De novo sequences generated from tryptic peptides by MALDI-TOF/TOF MS matched multiple anonymous Citrus EST cDNA accessions. The complete tt-pme cDNA (1710 base pair) was cloned from a fruit mRNA library using RT- and RLM-RACE PCR. Citrus TT-PME is a novel isoform that showed higher sequence identity with the multiply glycosylated kiwifruit PME than to previously described Citrus thermally labile PME isoforms. |
CC : | 002A |
FD : | Caractérisation; Tolérance; Pectinesterase; Fruit; Séquence nucléotide; Citrus sinensis; Paroi cellulaire; Jus d'orange; Stabilité thermique; MALDI; Réaction chaîne polymérase; Purification |
FG : | Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta |
ED : | Characterization; Tolerance; Pectinesterase; Fruit; Nucleotide sequence; Citrus sinensis; Cell wall; Orange juice; Thermal stability; Matrix assisted laser desorption ionization; Polymerase chain reaction; Purification |
EG : | Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta |
SD : | Caracterización; Tolerancia; Pectinesterase; Fruto; Secuencia nucleótido; Citrus sinensis; Pared celular; Zugo naranja; Estabilidad térmica; MALDI; Reacción cadena polimerasa; Purificación |
LO : | INIST-7332.354000500768770310 |
ID : | 14-0041424 |
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Pascal:14-0041424Le document en format XML
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<term>Orange juice</term>
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<front><div type="abstract" xml:lang="en">Despite the longstanding importance of the thermally tolerant pectin methylesterase (TT-PME) activity in citrus juice processing and product quality, the unequivocal identification of the protein and its corresponding gene has remained elusive. TT-PME was purified from sweet orange [Citrus sinensis (L.) Osbeck] finisher pulp (8.0 mg/1.3 kg tissue) with an improved purification scheme that provided 20-fold increased enzyme yield over previous results. Structural characterization of electrophoretically pure TT-PME by MALDI-TOF MS determined molecular masses of approximately 47900 and 53000 Da for two principal glycoisoforms. De novo sequences generated from tryptic peptides by MALDI-TOF/TOF MS matched multiple anonymous Citrus EST cDNA accessions. The complete tt-pme cDNA (1710 base pair) was cloned from a fruit mRNA library using RT- and RLM-RACE PCR. Citrus TT-PME is a novel isoform that showed higher sequence identity with the multiply glycosylated kiwifruit PME than to previously described Citrus thermally labile PME isoforms.</div>
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<fC01 i1="01" l="ENG"><s0>Despite the longstanding importance of the thermally tolerant pectin methylesterase (TT-PME) activity in citrus juice processing and product quality, the unequivocal identification of the protein and its corresponding gene has remained elusive. TT-PME was purified from sweet orange [Citrus sinensis (L.) Osbeck] finisher pulp (8.0 mg/1.3 kg tissue) with an improved purification scheme that provided 20-fold increased enzyme yield over previous results. Structural characterization of electrophoretically pure TT-PME by MALDI-TOF MS determined molecular masses of approximately 47900 and 53000 Da for two principal glycoisoforms. De novo sequences generated from tryptic peptides by MALDI-TOF/TOF MS matched multiple anonymous Citrus EST cDNA accessions. The complete tt-pme cDNA (1710 base pair) was cloned from a fruit mRNA library using RT- and RLM-RACE PCR. Citrus TT-PME is a novel isoform that showed higher sequence identity with the multiply glycosylated kiwifruit PME than to previously described Citrus thermally labile PME isoforms.</s0>
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<s5>12</s5>
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<s5>24</s5>
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<s5>26</s5>
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<s5>26</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Reacción cadena polimerasa</s0>
<s5>26</s5>
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<fC03 i1="12" i2="X" l="FRE"><s0>Purification</s0>
<s5>35</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Purification</s0>
<s5>35</s5>
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<fC03 i1="12" i2="X" l="SPA"><s0>Purificación</s0>
<s5>35</s5>
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<s2>FE</s2>
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<s2>FE</s2>
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<s2>FE</s2>
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<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>
<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>048</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 14-0041424 INIST</NO>
<ET>Structural Characterization of the Thermally Tolerant Pectin Methylesterase Purified from Citrus sinensis Fruit and Its Gene Sequence</ET>
<AU>SAVARY (Brett J.); VASU (Prasanna); CAMERON (Randall G.); MCCOLLUM (T. Gregory); NUNEZ (Alberto)</AU>
<AF>Eastern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, Wyndmoor/Pennsylvania 19038/Etats-Unis (1 aut., 5 aut.); Arkansas Biosciences Institute, Arkansas State University, P.O. Box 639, State University/Arkansas 72467/Etats-Unis (1 aut., 2 aut.); Food Safety and Analytical Quality Control Laboratory, Central Food Technological Research Institute, CSIR/Mysore 570 020/Inde (2 aut.); U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 2001 South Rock Road/Fort Pierce, Florida 34945/Etats-Unis (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. 2013; Vol. 61; No. 51; Pp. 12711-12719; Bibl. 44 ref.</SO>
<LA>Anglais</LA>
<EA>Despite the longstanding importance of the thermally tolerant pectin methylesterase (TT-PME) activity in citrus juice processing and product quality, the unequivocal identification of the protein and its corresponding gene has remained elusive. TT-PME was purified from sweet orange [Citrus sinensis (L.) Osbeck] finisher pulp (8.0 mg/1.3 kg tissue) with an improved purification scheme that provided 20-fold increased enzyme yield over previous results. Structural characterization of electrophoretically pure TT-PME by MALDI-TOF MS determined molecular masses of approximately 47900 and 53000 Da for two principal glycoisoforms. De novo sequences generated from tryptic peptides by MALDI-TOF/TOF MS matched multiple anonymous Citrus EST cDNA accessions. The complete tt-pme cDNA (1710 base pair) was cloned from a fruit mRNA library using RT- and RLM-RACE PCR. Citrus TT-PME is a novel isoform that showed higher sequence identity with the multiply glycosylated kiwifruit PME than to previously described Citrus thermally labile PME isoforms.</EA>
<CC>002A</CC>
<FD>Caractérisation; Tolérance; Pectinesterase; Fruit; Séquence nucléotide; Citrus sinensis; Paroi cellulaire; Jus d'orange; Stabilité thermique; MALDI; Réaction chaîne polymérase; Purification</FD>
<FG>Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta</FG>
<ED>Characterization; Tolerance; Pectinesterase; Fruit; Nucleotide sequence; Citrus sinensis; Cell wall; Orange juice; Thermal stability; Matrix assisted laser desorption ionization; Polymerase chain reaction; Purification</ED>
<EG>Carboxylic ester hydrolases; Esterases; Hydrolases; Enzyme; Rutaceae; Dicotyledones; Angiospermae; Spermatophyta</EG>
<SD>Caracterización; Tolerancia; Pectinesterase; Fruto; Secuencia nucleótido; Citrus sinensis; Pared celular; Zugo naranja; Estabilidad térmica; MALDI; Reacción cadena polimerasa; Purificación</SD>
<LO>INIST-7332.354000500768770310</LO>
<ID>14-0041424</ID>
</server>
</inist>
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