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PARTIAL PURIFICATION AND CHARACTERIZATION OF PECTIN METHYLESTERASE FROM ORANGE ( CITRUS SINENSIS ) CV. PERA‐RIO
Author(s) -
DO AMARAL SILVIA HELENA,
DE ASSIS SANDRA APARECIDA,
DE FARIA OLIVEIRA OLGA MARIA MASCARENHAS
Publication year - 2005
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2005.00036.x
Subject(s) - chemistry , orange (colour) , citrus × sinensis , sephadex , chromatography , pectin , pectinesterase , enzyme , pera , pectinase , orange g , size exclusion chromatography , food science , biochemistry , adsorption , organic chemistry
The enzyme pectin methylesterase (PME) from orange was extracted and partially purified by filtration on Sephadex G‐100. The extraction buffer for orange PME was borate–acetate containing 0.4 M NaCl. Orange PME showed optimum pH at 8.0 and optimum temperature at 50C. The PME enzyme was completely inactivated after 1 min of incubation at 90C. The specific activity increased in the presence of 0.15 M NaCl or 0.025 M Na2SO4, 0.10 M KCl, 0.025 M K2SO4, 0.05 and 0.1 M NH4Cl. Lithium chloride and Li2SO4inhibited the enzymatic activity at all concentrations studied. The K m and V max value of PME were 0.36 mg/mL and 5.26 µmol/mL‐mg protein, respectively.