Partial purification and characterization of pectin methylesterase from orange (Citrus sinensis) cv. Pera-rio
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/08/2005
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Resumo |
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 Li(2)SO(4)inhibited the enzymatic activity at all concentrations studied. The K-m and V(max)value of PME were 0.36 mg/mL and 5.26 mu mol/mL-mg protein, respectively. |
Formato |
367-380 |
Identificador |
http://dx.doi.org/10.1111/j.1745-4514.2005.00036.x Journal of Food Biochemistry. Oxford: Blackwell Publishing, v. 29, n. 4, p. 367-380, 2005. 0145-8884 http://hdl.handle.net/11449/37313 10.1111/j.1745-4514.2005.00036.x WOS:000230728100003 |
Idioma(s) |
eng |
Publicador |
Blackwell Publishing |
Relação |
Journal of Food Biochemistry |
Direitos |
closedAccess |
Tipo |
info:eu-repo/semantics/article |