Partial purification and characterization of pectin methylesterase from orange (Citrus sinensis) cv. Pera-rio


Autoria(s): Do Amaral, S. H.; De Assis, S. A.; Oliveira, OMMD
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/08/2005

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