Characterization of Pectin Methylesterase from Aspergillus niger
نویسندگان
چکیده
The present study was undertaken to evaluate the characteristics of pectin methylesterase produced from Aspergillus niger. enzyme had a molecular weight 59.668 kDa. exhibited maximum activity at 45°C. lost most its initial after 20 min incubation 75°C. Optimal and stability occurred pH 4, with more than 90 % retained 10 5. Michaelis constant (Km) found equal (1) mg/ml, whereas, velocity (Vmax) (1000) μmol/min. catalyzed reaction by activation energy 9.66 Kcal/mol. 24% 13% during two months storage at4°C -20 °C, respectively. activated NaCl, KCl CaCl2 concentration 25 mM inhibited MgSO4, polygalacturonic acid, methanol, IAA EDTA.
منابع مشابه
Tandem mass spectrometric analysis of aspergillus niger pectin methylesterase: mode of action on fully methyl-esterified oligogalacturonates.
The substrate specificity and the mode of action of Aspergillus niger pectin methylesterase (PME) was determined using both fully methyl-esterified oligogalacturonates with degrees of polymerization (DP) 2-6 and chemically synthesized monomethyl trigalacturonates. The enzymic activity on the different substrates and a preliminary characterization of the reaction products were performed by using...
متن کاملFunctional characterization of pectin methylesterase inhibitor (PMEI) in wheat.
Pectin, one of the main components of plant cell wall, is deesterified by the pectin methylesterase (PME). PME activity is regulated by inhibitor proteins known as the pectin methylesterase inhibitor (PMEI), which plays a key role in wounding, osmotic stress, senescence and seed development. However, the role of PMEI in many plant species still remains to be elucidated, especially in wheat. To ...
متن کاملPectin methylesterase, metal ions and plant cell-wall extension. Hydrolysis of pectin by plant cell-wall pectin methylesterase.
The hydrolysis of p-nitrophenyl acetate catalysed by pectin methylesterase is competitively inhibited by pectin and does not require metal ions to occur. The results suggest that the activastion by metal ions may be explained by assuming that they interact with the substrate rather than with the enzyme. With pectin used as substrate, metal ions are required in order to allow the hydrolysis to o...
متن کاملPARTIAL PURIFICATION AND CHARACTERIZATION OF B-GALACTOSIDASE FROM ASPERGILLUS NIGER UV-5
The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of ...
متن کاملConstitutive expression, purification and characterisation of pectin methylesterase from Aspergillus niger in Pichia pastoris for potential application in the fruit juice industry.
BACKGROUND Pectin methylesterase (PME) catalyses the hydrolysis of the methyl ester of pectin, yielding free carboxyl groups and methanol. PME is widely used in the food, cosmetic and pharmaceutical industries. RESULTS PME from Aspergillus niger was constitutively expressed to a high level in the yeast Pichia pastoris. The recombinant PME was purified by a combination of ammonium sulfate frac...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Ma?alla? Tikr?t li-l-?ul?m al-zir??a??
سال: 2023
ISSN: ['2664-0597', '1813-1646']
DOI: https://doi.org/10.25130/tjas.19.2.8