1970Agricultural and Biological ChemistryOpen access

Studies on the Pectolytic Enzyme

Hiroki Nakagawa, Yoshinobu Yanagawa, Hidetarô TAKEHANA

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Abstract

Pectinesterase was extracted from the pulp of tomato fruit (Lycopersicum esculentum var.Hikari) pericarp with 250mM potassium phosphate buffer, pH 8.0, and purified about 60 folds by means of ammonium sulfate fractionation, chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 column.The enzyme preparation thus obtained was confirmed to be homogeneous state both ultracentrifugationally and disk electrophoretically.The sedimentation coefficient of this enzyme was calculated to be 3.17 S.

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Pectinesterase was extracted from the pulp of tomato fruit (Lycopersicum esculentum var.Hikari) pericarp with 250mM potassium phosphate buffer, pH 8.0, and purified about 60 folds by means of ammonium sulfate fractionation, chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 column.The enzyme preparation thus obtained was confirmed to be homogeneous state both ultracentrifugationally and disk electrophoretically.The sedimentation coefficient of this enzyme was calculated to be 3.17 S.

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Available abstract

Pectinesterase was extracted from the pulp of tomato fruit (Lycopersicum esculentum var.Hikari) pericarp with 250mM potassium phosphate buffer, pH 8.0, and purified about 60 folds by means of ammonium sulfate fractionation, chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 column.The enzyme preparation thus obtained was confirmed to be homogeneous state both ultracentrifugationally and disk electrophoretically.The sedimentation coefficient of this enzyme was calculated to be 3.17 S.

Key concepts: Chemistry, Chromatography, Pectinesterase, Sephadex, Size-exclusion chromatography, Pectinase, Ammonium sulfate, Fractionation

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