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Partial purification, characterization and kinetics of thermal inactivation of pectin methylesterase and polygalacturonase enzymes from Indian lemon (Citrus limon (L.)
The extraction, purification, and characterization of PME and PG were studied for lemon fruit. Enzymes were partially purified by anion-exchange chromatography using UNOsphere™ Q anion exchanger for lemon PME and DEAE Cellulose anion exchanger for lemon PG. A single band with a fold purity of 20.95...
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Published in: | Journal of food measurement & characterization 2021-06, Vol.15 (3), p.2705-2715 |
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description | The extraction, purification, and characterization of PME and PG were studied for lemon fruit. Enzymes were partially purified by anion-exchange chromatography using UNOsphere™ Q anion exchanger for lemon PME and DEAE Cellulose anion exchanger for lemon PG. A single band with a fold purity of 20.95 and 15.75 for PME and PG respectively was observed on SDS-PAGE. Molecular weights of partially purified fractions of PME and PG as exhibited by SDS-PAGE were 48 kDa and 95 kDa respectively. Optimum pH and temperature of partially purified lemon PME and PG were pH 9, pH 5 and 45 °C. The crude PME and PG extracts exhibited D-values of 120.57–63.79 and 185.72–29.18 min; Z-values of 15.11 and 16.50 °C; and activation energies (E
a
) of 58.23 and 57.18 kJ/mol, respectively. The enzyme stability was not significantly influenced by the fruit matrix as reflected by Z and E
a
values. D and Z-values of both the enzymes and microorganisms should be considered while designing thermal treatments to obtain a product with better shelf life. |
doi_str_mv | 10.1007/s11694-021-00835-8 |
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a
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a
values. 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Enzymes were partially purified by anion-exchange chromatography using UNOsphere™ Q anion exchanger for lemon PME and DEAE Cellulose anion exchanger for lemon PG. A single band with a fold purity of 20.95 and 15.75 for PME and PG respectively was observed on SDS-PAGE. Molecular weights of partially purified fractions of PME and PG as exhibited by SDS-PAGE were 48 kDa and 95 kDa respectively. Optimum pH and temperature of partially purified lemon PME and PG were pH 9, pH 5 and 45 °C. The crude PME and PG extracts exhibited D-values of 120.57–63.79 and 185.72–29.18 min; Z-values of 15.11 and 16.50 °C; and activation energies (E
a
) of 58.23 and 57.18 kJ/mol, respectively. The enzyme stability was not significantly influenced by the fruit matrix as reflected by Z and E
a
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subjects | Anion exchanging Anion-exchange chromatography Cellulose Chemistry Chemistry and Materials Science Chemistry/Food Science Engineering Enzymes Food Science Fruits Gel electrophoresis Inactivation Lemons Microorganisms Original Paper Pectin Pectinesterase pH effects Polygalacturonase Purification Shelf life Sodium lauryl sulfate |
title | Partial purification, characterization and kinetics of thermal inactivation of pectin methylesterase and polygalacturonase enzymes from Indian lemon (Citrus limon (L.) |
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