Isoenzymes of lipolytic acyl hydrolase and esterase in potato tuber |
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Authors: | T Galliard S Dennis |
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Institution: | Agricultural Research Council Food Research Institute, Colney Lane, Norwich, NOR 7OF U.K. |
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Abstract: | Five varieties of potato (Solanum tuberosum) were shown by gel- and free-flow-electrophoresis to exhibit multiple forms of lipolytic acyl hydrolase (LAH) and esterase enzymes. The electrophoretic patterns of LAH and esterase activities and protein differed with the variety and were characteristic for a given variety. In the variety (Golden Wonder) with the highest LAH activity (p-nitrophenylpalmitate as substrate), this was 200-fold greater than the esterase activity (p-nitrophenylacetate as substrate) and isoenzyme patterns for both enzymes were the most complex. In the variety with a very low LAH activity (Désirée), the LAH and esterase activities were similar and more simple isoenzyme patterns for these enzymes were observed. |
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Keywords: | Solanacae potato lipolytic acyl hydrolase esterase isoenzymes |
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