The Peroxidase of Dioscorea esculenta: Partial Purification and Characterisation

نویسنده

  • J. Okpuzor
چکیده

Z. Naturforsch. 54c, 496-500 (1999); received January 11/March 27. 1999 Dioscorea esculenta. Peroxidase. Ion Exchange C hrom atography. Gel Filtration We isolated two types of peroxidase from the fresh tuber of Dioscorea esculenta using a com bination of ion exchange and gel filtration chrom atography. The results showed one type to be neutral and the other to be strongly ionic. The strongly ionic type constitutes 70% of total peroxidase activity in the tissue. The apparen t m olecular weight of the neutral type is 38 kD a while the anionic type has an apparen t m olecular weight of 57 kD a. It was possible with the use of gel filtration on Sephadex G-200 followed by FPLC on phenyl superose to purify the lower size POD by a factor of 15, while the larger ionic peroxidase was purified 68 fold com pared to the crude with protein yields of 0.90% and 1.30% respectively. The ionic PO D is more therm o-stable, has a higher optim um tem perature for activity and has a higher apparent activation energy com pared to the neutral PO D from this source.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Starch and sugar conversion in Dioscorea esculenta tubers and Curcuma longa rhizomes during storage

An investigation was carried out to reveal the changes in the concentration of soluble carbohydrates under tuber dormancy in food yam (Dioscorea esculenta) tubers and in an economically important spice cum medicinal plant turmeric (Curcuma longa) rhizomes under storage. Harvested, fully matured tubers of yam and rhizomes of turmeric were stored in wooden boxes under the conditions of 28 ? 2?C t...

متن کامل

Partial Purification and Characterisation of Polyphenol Oxidase from Tomatoes (Solanum Lycopersicum)

Polyphenol oxidase (PPO) from tomatoes was extracted and partially purified through  (NH4)2SO4 precipitation, dialysis and ion exchange chromatography. The activity of polyphenol oxidase was investigated in solanum lycopersicum. Spectrophotometric method was used to assay the enzyme activity and the kinetic constants - maximum enzyme velocity (Vmax) and Michealis - Menten constant (Km). Of the ...

متن کامل

Partial Purification and Characterisation of Polyphenol Oxidase from Tomatoes (Solanum Lycopersicum)

Polyphenol oxidase (PPO) from tomatoes was extracted and partially purified through  (NH4)2SO4 precipitation, dialysis and ion exchange chromatography. The activity of polyphenol oxidase was investigated in solanum lycopersicum. Spectrophotometric method was used to assay the enzyme activity and the kinetic constants - maximum enzyme velocity (Vmax) and Michealis - Menten constant (Km). Of the ...

متن کامل

Peroxidase-polyphenol oxidase association in Dioscorea esculenta.

A crude enzyme extract from Dioscorea esculenta var. fasiculata tissue subjected to ion exchange chromatography on DEAE-Sephadex A-50 column. This procedure resolved the extract into two main protein peaks one of which eluted through the column relatively unbound while the other protein peak which remained bound to the column was eluted with 1.0 M NaCl. Both protein peaks contained polyphenol o...

متن کامل

PURIFICATION AND SOME PARTIAL CHARACTERIZATION OF PEROXIDASE ISOENZYME FROM BRASSICA OLERACEA CAPITATA L.

Acetone fractionated peroxidase from crude extract of Brassica oleracea leaves (Cabbage) was purified in three steps on chromatographic columns, using Sp-Sepharose, DEAE-Sepharose and Con A-Sepharose. The specific activity of purified main isoenzyme (BOC-POD) is 1887 u/mg protein with RZ: 3.1, which is 172 times more than the RZ of crude extract with 4.3% recovery. The molecular weight of BOC-P...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 1999