Abstract
ABSTRACTThermostable pectinesterase was estimated to represent 98% of total activity extracted from Marsh grapefruit pulp by 1M NaCl without pH adjustment or 17% when extracted with 1M NaCl, 0.25M Tris‐Cl‐ pH 8.0. Total units of pectinesterase solubilized were less in 1M NaCl at endogenous pH values than at pH 8.0, but total thermostable pectinesterase units remained constant. No conversion of thermostable to heat sensitive isozymes was observed. Preparative isoelectric focusing indicated that most activity focused at alkaline pH values. The constant specific activity suggested co‐migration of basic proteins.
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