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Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel.
J Agric Food Chem 2001; 49(3):1446-9JA

Abstract

Polyphenol oxidase (EC 1.10.3.1, o-diphenol: oxygen oxidoreductase, PPO) of banana (Musa sapientum L.) peel was partially purified about 460-fold with a recovery of 2.2% using dopamine as substrate. The enzyme showed a single peak on Toyopearl HW55-S chromatography. However, two bands were detected by staining with Coomassie brilliant blue on PAGE: one was very clear, and the other was faint. Molecular weight for purified PPO was estimated to be about 41 000 by gel filtration. The enzyme quickly oxidized dopamine, and its Km value (Michaelis constant) for dopamine was 3.9 mM. Optimum pH was 6.5 and the PPO activity was quite stable in the range of pH 5-11 for 48 h. The enzyme had an optimum temperature at 30 degrees C and was stable up to 60 degrees C after heat treatment for 30 min. The enzyme activity was strongly inhibited by sodium diethyldithiocarbamate, potassium cyanide, L-ascorbic acid, and cysteine at 1 mM. Under a low buffer capacity, the enzyme was also strongly inhibited by citric acid and acetic acid at 10 mM.

Authors+Show Affiliations

Laboratory of Food Science, Faculty of Agriculture, Saga University, Saga 840-8502, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11312878

Citation

Yang, C P., et al. "Partial Purification and Characterization of Polyphenol Oxidase From Banana (Musa Sapientum L.) Peel." Journal of Agricultural and Food Chemistry, vol. 49, no. 3, 2001, pp. 1446-9.
Yang CP, Fujita S, Kohno K, et al. Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel. J Agric Food Chem. 2001;49(3):1446-9.
Yang, C. P., Fujita, S., Kohno, K., Kusubayashi, A., Ashrafuzzaman, M., & Hayashi, N. (2001). Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel. Journal of Agricultural and Food Chemistry, 49(3), pp. 1446-9.
Yang CP, et al. Partial Purification and Characterization of Polyphenol Oxidase From Banana (Musa Sapientum L.) Peel. J Agric Food Chem. 2001;49(3):1446-9. PubMed PMID: 11312878.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel. AU - Yang,C P, AU - Fujita,S, AU - Kohno,K, AU - Kusubayashi,A, AU - Ashrafuzzaman,M, AU - Hayashi,N, PY - 2001/4/21/pubmed PY - 2001/6/22/medline PY - 2001/4/21/entrez SP - 1446 EP - 9 JF - Journal of agricultural and food chemistry JO - J. Agric. Food Chem. VL - 49 IS - 3 N2 - Polyphenol oxidase (EC 1.10.3.1, o-diphenol: oxygen oxidoreductase, PPO) of banana (Musa sapientum L.) peel was partially purified about 460-fold with a recovery of 2.2% using dopamine as substrate. The enzyme showed a single peak on Toyopearl HW55-S chromatography. However, two bands were detected by staining with Coomassie brilliant blue on PAGE: one was very clear, and the other was faint. Molecular weight for purified PPO was estimated to be about 41 000 by gel filtration. The enzyme quickly oxidized dopamine, and its Km value (Michaelis constant) for dopamine was 3.9 mM. Optimum pH was 6.5 and the PPO activity was quite stable in the range of pH 5-11 for 48 h. The enzyme had an optimum temperature at 30 degrees C and was stable up to 60 degrees C after heat treatment for 30 min. The enzyme activity was strongly inhibited by sodium diethyldithiocarbamate, potassium cyanide, L-ascorbic acid, and cysteine at 1 mM. Under a low buffer capacity, the enzyme was also strongly inhibited by citric acid and acetic acid at 10 mM. SN - 0021-8561 UR - https://www.unboundmedicine.com/medline/citation/11312878/Partial_purification_and_characterization_of_polyphenol_oxidase_from_banana__Musa_sapientum_L___peel_ L2 - https://dx.doi.org/10.1021/jf001051i DB - PRIME DP - Unbound Medicine ER -