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Purification of Commercial Pectinase by Hydrophobic Chromatography
Author(s) -
KELLER SUSANNE E.,
JEN JOSEPH J.,
BRUNNER J. ROBERT
Publication year - 1982
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1982.tb12954.x
Subject(s) - pectinase , size exclusion chromatography , chromatography , chemistry , homogeneous , aspergillus niger , ion chromatography , hydrophilic interaction chromatography , enzyme , biochemistry , high performance liquid chromatography , physics , thermodynamics
A 70‐fold purification of a commercial pectinase from Aspergillus niger was achieved by gel filtration, ion exchange and hydrophobic chromatographic columns employed in sequence. An apparent Km of 4.5 ± 10 ‐5 M and a V M of 1.9 mM/minmg were obtained. The purified preparation reached a higher degree of purification than those reported in the literature but was not electrophoretically homogeneous. The preparation was an endo‐polygalacturonase in nature and preferred high molecular weight pectates as substrates. The pH optimum of 4.4 was not affected by the size of substrates. Hydrophobic chromatography is a useful tool for the preparation of pectic enzymes.