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William S. Conway - One of the best experts on this subject based on the ideXlab platform.
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Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
Mycologia, 2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active from pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-70 C with 50 C maximum. The purified isozyme was inhibited by the divalent cations Ca 2+ , Mg 2+ ,M n 2+ and Fe 2+ and analysis of enzymatic hydrolysis products revealed polygalacturonic acid monomers and oligomers. The purified enzyme has an isoelectric point of 5.3 and is not associated with a glycosylated protein. The PG isozyme macerated fruit tissue plugs in vitro and produced ,1.2-fold more soluble polyuronides from pear than from apple tissue, which further substantiates the role of PG in postharvest decay. Data from this study show for the first time that the purified PG produced in decayed Anjou pear by P. solitum, a weakly virulent fungus, is different from that PG produced by the same fungus in decayed apple.
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Short title: Penicillium solitum polygalacturonase isozyme Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-
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Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed 'Golden Delicious' apple fruit.
Phytopathology, 2009Co-Authors: Wayne M. Jurick, Ivana Vico, Bruce D. Whitaker, Wojciech J. Janisiewicz, James L. Mcevoy, William S. ConwayAbstract:Jurick, W. M., II, Vico, I., McEvoy, J. L., Whitaker, B. D., Janisiewicz, W., and Conway, W. S. 2009. Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed ‘Golden Delicious’ apple fruit. Phytopathology 99:636-641. Polygalacturonase (PG) was extracted and purified from decayed ‘Golden Delicious’ apple fruit inoculated with Penicillium solitum. Ammonium sulfate, gel filtration, and cation exchange chromatography were used to purify the enzyme. Both chromatographic methods revealed a single peak corresponding to PG activity. The purified PG most likely originates from the fungus because PG activity from healthy and wounded apple tissue was undetectable. Analysis of cation exchangepurified material using sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 50-kDa band. The enzyme was active over a broad pH range (3 to 7), with optimal activity between pH 4 and 5. PG was highly active at 20 and 37°C but was also detectable at 2, 50, and 75°C. Divalent cations affected PG enzyme activity; Mg and Fe increased, whereas Ca and Mn reduced activity in vitro. Thin-layer chromatographic separation of hydrolysis products and data from a PG plate activity assay based on staining with ruthenium red showed that the enzyme exhibits both exo and endo activity. Purified PG incubated with intact apple fruit tissue in vitro caused a 30% reduction in mass after 48 h, suggesting a role in P. solitum-mediated decay of apple fruit.
Wayne M. Jurick - One of the best experts on this subject based on the ideXlab platform.
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Genome Sequence of Penicillium solitum RS1, Which Causes Postharvest Apple Decay
Genome announcements, 2016Co-Authors: Wayne M. Jurick, Guohua Yin, Joan W. Bennett, Verneta L. Gaskins, Yanbin Yin, Daniel R. SheltonAbstract:ABSTRACT Penicillium species cause postharvest decay, commonly known as blue mold, in pome fruits, such as apples and pears. To devise novel strategies to prevent and reduce economic losses during storage, the genome sequence of Penicillium solitum RS1 is reported here for the first time.
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Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
Mycologia, 2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active from pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-70 C with 50 C maximum. The purified isozyme was inhibited by the divalent cations Ca 2+ , Mg 2+ ,M n 2+ and Fe 2+ and analysis of enzymatic hydrolysis products revealed polygalacturonic acid monomers and oligomers. The purified enzyme has an isoelectric point of 5.3 and is not associated with a glycosylated protein. The PG isozyme macerated fruit tissue plugs in vitro and produced ,1.2-fold more soluble polyuronides from pear than from apple tissue, which further substantiates the role of PG in postharvest decay. Data from this study show for the first time that the purified PG produced in decayed Anjou pear by P. solitum, a weakly virulent fungus, is different from that PG produced by the same fungus in decayed apple.
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Short title: Penicillium solitum polygalacturonase isozyme Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-
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Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed 'Golden Delicious' apple fruit.
Phytopathology, 2009Co-Authors: Wayne M. Jurick, Ivana Vico, Bruce D. Whitaker, Wojciech J. Janisiewicz, James L. Mcevoy, William S. ConwayAbstract:Jurick, W. M., II, Vico, I., McEvoy, J. L., Whitaker, B. D., Janisiewicz, W., and Conway, W. S. 2009. Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed ‘Golden Delicious’ apple fruit. Phytopathology 99:636-641. Polygalacturonase (PG) was extracted and purified from decayed ‘Golden Delicious’ apple fruit inoculated with Penicillium solitum. Ammonium sulfate, gel filtration, and cation exchange chromatography were used to purify the enzyme. Both chromatographic methods revealed a single peak corresponding to PG activity. The purified PG most likely originates from the fungus because PG activity from healthy and wounded apple tissue was undetectable. Analysis of cation exchangepurified material using sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 50-kDa band. The enzyme was active over a broad pH range (3 to 7), with optimal activity between pH 4 and 5. PG was highly active at 20 and 37°C but was also detectable at 2, 50, and 75°C. Divalent cations affected PG enzyme activity; Mg and Fe increased, whereas Ca and Mn reduced activity in vitro. Thin-layer chromatographic separation of hydrolysis products and data from a PG plate activity assay based on staining with ruthenium red showed that the enzyme exhibits both exo and endo activity. Purified PG incubated with intact apple fruit tissue in vitro caused a 30% reduction in mass after 48 h, suggesting a role in P. solitum-mediated decay of apple fruit.
Wojciech J. Janisiewicz - One of the best experts on this subject based on the ideXlab platform.
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Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
Mycologia, 2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active from pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-70 C with 50 C maximum. The purified isozyme was inhibited by the divalent cations Ca 2+ , Mg 2+ ,M n 2+ and Fe 2+ and analysis of enzymatic hydrolysis products revealed polygalacturonic acid monomers and oligomers. The purified enzyme has an isoelectric point of 5.3 and is not associated with a glycosylated protein. The PG isozyme macerated fruit tissue plugs in vitro and produced ,1.2-fold more soluble polyuronides from pear than from apple tissue, which further substantiates the role of PG in postharvest decay. Data from this study show for the first time that the purified PG produced in decayed Anjou pear by P. solitum, a weakly virulent fungus, is different from that PG produced by the same fungus in decayed apple.
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Short title: Penicillium solitum polygalacturonase isozyme Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-
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Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed 'Golden Delicious' apple fruit.
Phytopathology, 2009Co-Authors: Wayne M. Jurick, Ivana Vico, Bruce D. Whitaker, Wojciech J. Janisiewicz, James L. Mcevoy, William S. ConwayAbstract:Jurick, W. M., II, Vico, I., McEvoy, J. L., Whitaker, B. D., Janisiewicz, W., and Conway, W. S. 2009. Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed ‘Golden Delicious’ apple fruit. Phytopathology 99:636-641. Polygalacturonase (PG) was extracted and purified from decayed ‘Golden Delicious’ apple fruit inoculated with Penicillium solitum. Ammonium sulfate, gel filtration, and cation exchange chromatography were used to purify the enzyme. Both chromatographic methods revealed a single peak corresponding to PG activity. The purified PG most likely originates from the fungus because PG activity from healthy and wounded apple tissue was undetectable. Analysis of cation exchangepurified material using sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 50-kDa band. The enzyme was active over a broad pH range (3 to 7), with optimal activity between pH 4 and 5. PG was highly active at 20 and 37°C but was also detectable at 2, 50, and 75°C. Divalent cations affected PG enzyme activity; Mg and Fe increased, whereas Ca and Mn reduced activity in vitro. Thin-layer chromatographic separation of hydrolysis products and data from a PG plate activity assay based on staining with ruthenium red showed that the enzyme exhibits both exo and endo activity. Purified PG incubated with intact apple fruit tissue in vitro caused a 30% reduction in mass after 48 h, suggesting a role in P. solitum-mediated decay of apple fruit.
Bruce D. Whitaker - One of the best experts on this subject based on the ideXlab platform.
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Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
Mycologia, 2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active from pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-70 C with 50 C maximum. The purified isozyme was inhibited by the divalent cations Ca 2+ , Mg 2+ ,M n 2+ and Fe 2+ and analysis of enzymatic hydrolysis products revealed polygalacturonic acid monomers and oligomers. The purified enzyme has an isoelectric point of 5.3 and is not associated with a glycosylated protein. The PG isozyme macerated fruit tissue plugs in vitro and produced ,1.2-fold more soluble polyuronides from pear than from apple tissue, which further substantiates the role of PG in postharvest decay. Data from this study show for the first time that the purified PG produced in decayed Anjou pear by P. solitum, a weakly virulent fungus, is different from that PG produced by the same fungus in decayed apple.
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Short title: Penicillium solitum polygalacturonase isozyme Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-
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Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed 'Golden Delicious' apple fruit.
Phytopathology, 2009Co-Authors: Wayne M. Jurick, Ivana Vico, Bruce D. Whitaker, Wojciech J. Janisiewicz, James L. Mcevoy, William S. ConwayAbstract:Jurick, W. M., II, Vico, I., McEvoy, J. L., Whitaker, B. D., Janisiewicz, W., and Conway, W. S. 2009. Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed ‘Golden Delicious’ apple fruit. Phytopathology 99:636-641. Polygalacturonase (PG) was extracted and purified from decayed ‘Golden Delicious’ apple fruit inoculated with Penicillium solitum. Ammonium sulfate, gel filtration, and cation exchange chromatography were used to purify the enzyme. Both chromatographic methods revealed a single peak corresponding to PG activity. The purified PG most likely originates from the fungus because PG activity from healthy and wounded apple tissue was undetectable. Analysis of cation exchangepurified material using sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 50-kDa band. The enzyme was active over a broad pH range (3 to 7), with optimal activity between pH 4 and 5. PG was highly active at 20 and 37°C but was also detectable at 2, 50, and 75°C. Divalent cations affected PG enzyme activity; Mg and Fe increased, whereas Ca and Mn reduced activity in vitro. Thin-layer chromatographic separation of hydrolysis products and data from a PG plate activity assay based on staining with ruthenium red showed that the enzyme exhibits both exo and endo activity. Purified PG incubated with intact apple fruit tissue in vitro caused a 30% reduction in mass after 48 h, suggesting a role in P. solitum-mediated decay of apple fruit.
Ivana Vico - One of the best experts on this subject based on the ideXlab platform.
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Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
Mycologia, 2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active from pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-70 C with 50 C maximum. The purified isozyme was inhibited by the divalent cations Ca 2+ , Mg 2+ ,M n 2+ and Fe 2+ and analysis of enzymatic hydrolysis products revealed polygalacturonic acid monomers and oligomers. The purified enzyme has an isoelectric point of 5.3 and is not associated with a glycosylated protein. The PG isozyme macerated fruit tissue plugs in vitro and produced ,1.2-fold more soluble polyuronides from pear than from apple tissue, which further substantiates the role of PG in postharvest decay. Data from this study show for the first time that the purified PG produced in decayed Anjou pear by P. solitum, a weakly virulent fungus, is different from that PG produced by the same fungus in decayed apple.
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Short title: Penicillium solitum polygalacturonase isozyme Penicillium solitum produces a polygalacturonase isozyme in decayed Anjou pear fruit capable of macerating host tissue in vitro
2012Co-Authors: Wayne M. Jurick, Verneta L. Gaskins, Ivana Vico, Bruce D. Whitaker, Wesley M. Garrett, Wojciech J. Janisiewicz, William S. ConwayAbstract:A polygalacturonase (PG) isozyme was isolated from Penicillium solitum-decayed Anjou pear fruit and purified to homogeneity with a multistep process. Both gel filtration and cation exchange chromatography revealed a single PG activity peak, and analysis of the purified protein showed a single band with a molecular mass of 43 kDa, which is of fungal origin. The purified enzyme was active pH 3.5-6, with an optimum at pH 4.5. PG activity was detectable 0-
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Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed 'Golden Delicious' apple fruit.
Phytopathology, 2009Co-Authors: Wayne M. Jurick, Ivana Vico, Bruce D. Whitaker, Wojciech J. Janisiewicz, James L. Mcevoy, William S. ConwayAbstract:Jurick, W. M., II, Vico, I., McEvoy, J. L., Whitaker, B. D., Janisiewicz, W., and Conway, W. S. 2009. Isolation, purification, and characterization of a polygalacturonase produced in Penicillium solitum-decayed ‘Golden Delicious’ apple fruit. Phytopathology 99:636-641. Polygalacturonase (PG) was extracted and purified from decayed ‘Golden Delicious’ apple fruit inoculated with Penicillium solitum. Ammonium sulfate, gel filtration, and cation exchange chromatography were used to purify the enzyme. Both chromatographic methods revealed a single peak corresponding to PG activity. The purified PG most likely originates from the fungus because PG activity from healthy and wounded apple tissue was undetectable. Analysis of cation exchangepurified material using sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 50-kDa band. The enzyme was active over a broad pH range (3 to 7), with optimal activity between pH 4 and 5. PG was highly active at 20 and 37°C but was also detectable at 2, 50, and 75°C. Divalent cations affected PG enzyme activity; Mg and Fe increased, whereas Ca and Mn reduced activity in vitro. Thin-layer chromatographic separation of hydrolysis products and data from a PG plate activity assay based on staining with ruthenium red showed that the enzyme exhibits both exo and endo activity. Purified PG incubated with intact apple fruit tissue in vitro caused a 30% reduction in mass after 48 h, suggesting a role in P. solitum-mediated decay of apple fruit.