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Purification and characterization of polyphenol oxidase from cauliflower (Brassica oleracea L.).
J Agric Food Chem 2012; 60(14):3673-8JA

Abstract

Polyphenol oxidase (PPO) of cauliflower was purified to 282-fold with a recovery rate of 8.1%, using phloroglucinol as a substrate. The enzyme appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The estimated molecular weight of the enzyme was 60 and 54 kDa by SDS-PAGE and gel filtration, respectively. The purified enzyme, called phloroglucinol oxidase (PhO), oxidized phloroglucinol (K(m) = 3.3 mM) and phloroglucinolcarboxylic acid. The enzyme also had peroxidase (POD) activity. At the final step, the activity of purified cauliflower POD was 110-fold with a recovery rate of 3.2%. The PhO and POD showed the highest activity at pH 8.0 and 4.0 and were stable in the pH range of 3.0-11.0 and 5.0-8.0 at 5 °C for 20 h, respectively. The optimum temperature was 55 °C for PhO and 20 °C for POD. The most effective inhibitor for PhO was sodium diethyldithiocarbamate at 10 mM (IC(50) = 0.64 and K(i) = 0.15 mM), and the most effective inhibitor for POD was potassium cyanide at 1.0 mM (IC(50) = 0.03 and K(i) = 29 μM).

Authors+Show Affiliations

Laboratory of Food Science, Faculty of Agriculture, Saga University, Saga, Japan. faidah83@yahoo.comNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

22471879

Citation

Rahman, Andi Nur Faidah, et al. "Purification and Characterization of Polyphenol Oxidase From Cauliflower (Brassica Oleracea L.)." Journal of Agricultural and Food Chemistry, vol. 60, no. 14, 2012, pp. 3673-8.
Rahman AN, Ohta M, Nakatani K, et al. Purification and characterization of polyphenol oxidase from cauliflower (Brassica oleracea L.). J Agric Food Chem. 2012;60(14):3673-8.
Rahman, A. N., Ohta, M., Nakatani, K., Hayashi, N., & Fujita, S. (2012). Purification and characterization of polyphenol oxidase from cauliflower (Brassica oleracea L.). Journal of Agricultural and Food Chemistry, 60(14), pp. 3673-8. doi:10.1021/jf300380b.
Rahman AN, et al. Purification and Characterization of Polyphenol Oxidase From Cauliflower (Brassica Oleracea L.). J Agric Food Chem. 2012 Apr 11;60(14):3673-8. PubMed PMID: 22471879.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and characterization of polyphenol oxidase from cauliflower (Brassica oleracea L.). AU - Rahman,Andi Nur Faidah, AU - Ohta,Mayumi, AU - Nakatani,Kazuya, AU - Hayashi,Nobuyuki, AU - Fujita,Shuji, Y1 - 2012/04/03/ PY - 2012/4/5/entrez PY - 2012/4/5/pubmed PY - 2012/8/8/medline SP - 3673 EP - 8 JF - Journal of agricultural and food chemistry JO - J. Agric. Food Chem. VL - 60 IS - 14 N2 - Polyphenol oxidase (PPO) of cauliflower was purified to 282-fold with a recovery rate of 8.1%, using phloroglucinol as a substrate. The enzyme appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The estimated molecular weight of the enzyme was 60 and 54 kDa by SDS-PAGE and gel filtration, respectively. The purified enzyme, called phloroglucinol oxidase (PhO), oxidized phloroglucinol (K(m) = 3.3 mM) and phloroglucinolcarboxylic acid. The enzyme also had peroxidase (POD) activity. At the final step, the activity of purified cauliflower POD was 110-fold with a recovery rate of 3.2%. The PhO and POD showed the highest activity at pH 8.0 and 4.0 and were stable in the pH range of 3.0-11.0 and 5.0-8.0 at 5 °C for 20 h, respectively. The optimum temperature was 55 °C for PhO and 20 °C for POD. The most effective inhibitor for PhO was sodium diethyldithiocarbamate at 10 mM (IC(50) = 0.64 and K(i) = 0.15 mM), and the most effective inhibitor for POD was potassium cyanide at 1.0 mM (IC(50) = 0.03 and K(i) = 29 μM). SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/22471879/Purification_and_characterization_of_polyphenol_oxidase_from_cauliflower__Brassica_oleracea_L___ L2 - https://dx.doi.org/10.1021/jf300380b DB - PRIME DP - Unbound Medicine ER -