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Purification and partial biochemical characterization of polyphenol oxidase from mamey (Pouteria sapota).
Phytochemistry 2011; 72(1):82-8P

Abstract

While a long shelf life for fruit products is highly desired, enzymatic browning is the main cause of quality loss in fruits and is therefore a main problem for the food industry. In this study polyphenol oxidase (PPO), the main enzyme responsible for browning was isolated from mamey fruit (Pouteria sapota) and characterized biochemically. Two isoenzymes (PPO 1 and PPO 2) were obtained upon ammonium sulfate precipitation and hydrophobic and ion exchange chromatography; PPO 1 was purified up to 6.6-fold with 0.28% yield, while PPO 2 could not be characterized as enzyme activity was completely lost after 24 h of storage. PPO 1 molecular weight was estimated to be 16.1 and 18 kDa by gel filtration and SDS-PAGE, respectively, indicating that the native state of the PPO 1 is a monomer. The optimum pH for PPO 1 activity was 7. The PPO 1 was determined to be maximum thermally stable up to 35°C. Kinetic constants for PPO 1 were K(m)=44 mM and K(m)=1.3 mM using catechol and pyrogallol as substrate, respectively. The best substrates for PPO 1 were pyrogallol, 4-methylcatechol and catechol, while ascorbic acid and sodium metabisulfite were the most effective inhibitors.

Authors+Show Affiliations

Escuela Nacional de Ciencias Biológicas, Departamento de Ingeniería Bioquímica Instituto Politécnico Nacional, México, DF, Mexico.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21087780

Citation

Palma-Orozco, Gisela, et al. "Purification and Partial Biochemical Characterization of Polyphenol Oxidase From Mamey (Pouteria Sapota)." Phytochemistry, vol. 72, no. 1, 2011, pp. 82-8.
Palma-Orozco G, Ortiz-Moreno A, Dorantes-Alvarez L, et al. Purification and partial biochemical characterization of polyphenol oxidase from mamey (Pouteria sapota). Phytochemistry. 2011;72(1):82-8.
Palma-Orozco, G., Ortiz-Moreno, A., Dorantes-Alvarez, L., Sampedro, J. G., & Nájera, H. (2011). Purification and partial biochemical characterization of polyphenol oxidase from mamey (Pouteria sapota). Phytochemistry, 72(1), pp. 82-8. doi:10.1016/j.phytochem.2010.10.011.
Palma-Orozco G, et al. Purification and Partial Biochemical Characterization of Polyphenol Oxidase From Mamey (Pouteria Sapota). Phytochemistry. 2011;72(1):82-8. PubMed PMID: 21087780.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and partial biochemical characterization of polyphenol oxidase from mamey (Pouteria sapota). AU - Palma-Orozco,Gisela, AU - Ortiz-Moreno,Alicia, AU - Dorantes-Alvarez,Lidia, AU - Sampedro,José G, AU - Nájera,Hugo, Y1 - 2010/11/17/ PY - 2010/03/19/received PY - 2010/09/13/revised PY - 2010/10/16/accepted PY - 2010/11/20/entrez PY - 2010/11/23/pubmed PY - 2011/2/22/medline SP - 82 EP - 8 JF - Phytochemistry JO - Phytochemistry VL - 72 IS - 1 N2 - While a long shelf life for fruit products is highly desired, enzymatic browning is the main cause of quality loss in fruits and is therefore a main problem for the food industry. In this study polyphenol oxidase (PPO), the main enzyme responsible for browning was isolated from mamey fruit (Pouteria sapota) and characterized biochemically. Two isoenzymes (PPO 1 and PPO 2) were obtained upon ammonium sulfate precipitation and hydrophobic and ion exchange chromatography; PPO 1 was purified up to 6.6-fold with 0.28% yield, while PPO 2 could not be characterized as enzyme activity was completely lost after 24 h of storage. PPO 1 molecular weight was estimated to be 16.1 and 18 kDa by gel filtration and SDS-PAGE, respectively, indicating that the native state of the PPO 1 is a monomer. The optimum pH for PPO 1 activity was 7. The PPO 1 was determined to be maximum thermally stable up to 35°C. Kinetic constants for PPO 1 were K(m)=44 mM and K(m)=1.3 mM using catechol and pyrogallol as substrate, respectively. The best substrates for PPO 1 were pyrogallol, 4-methylcatechol and catechol, while ascorbic acid and sodium metabisulfite were the most effective inhibitors. SN - 1873-3700 UR - https://www.unboundmedicine.com/medline/citation/21087780/Purification_and_partial_biochemical_characterization_of_polyphenol_oxidase_from_mamey__Pouteria_sapota__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0031-9422(10)00391-2 DB - PRIME DP - Unbound Medicine ER -