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Partial purification, characterisation and thermal inactivation kinetics of peroxidase and polyphenol oxidase isolated from Kalipatti sapota (Manilkara zapota).
J Sci Food Agric 2017; 97(11):3568-3575JS

Abstract

BACKGROUND

The extraction, purification, and characterisation of peroxidase (POD) and polyphenol oxidase (PPO) were studied for Kalipatti sapota fruit. The crude enzyme extract was partially purified by ammonium sulfate precipitation followed by BioGel P100 size exclusion and Unosphere Q anion-exchange chromatography.

RESULTS

Molecular weights of 20 kDa (POD) and 24 kDa (PPO) were indicated by SDS-PAGE. A single band was observed on SDS-PAGE with a fold purity of 10.38 and 7.42 for POD and PPO, respectively. Michaelis-Menten constants for POD and PPO were 22.3 and 23.0 mmol L-1 using guaiacol and catechol as substrates. Thermal inactivation kinetics was studied in the temperature range of 60-95 °C. The crude extract of POD and PPO showed D-values of 2.2-60.2 and 1.0-35.2 min; Z-values of 18.7 ± 0.4 and 16.0 ± 0.3 °C; and activation energies (Ea) of 128.6 and 151.0 kJ mol-1 , respectively.

CONCLUSION

POD and PPO showed good stability over a wide range of pH and temperature. As reflected by Z and Ea values, the fruit matrix had no significant influence towards enzyme stability. Designing of thermal process should take into consideration D- and Z-values of the enzymes along with D- and Z-values of microorganisms to obtain a product with better shelf life. © 2017 Society of Chemical Industry.

Authors+Show Affiliations

Food Engineering and Technology Department, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga, Mumbai, India.Food Engineering and Technology Department, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga, Mumbai, India.Food Engineering and Technology Department, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga, Mumbai, India.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28098357

Citation

Vishwasrao, Chandrahas, et al. "Partial Purification, Characterisation and Thermal Inactivation Kinetics of Peroxidase and Polyphenol Oxidase Isolated From Kalipatti Sapota (Manilkara Zapota)." Journal of the Science of Food and Agriculture, vol. 97, no. 11, 2017, pp. 3568-3575.
Vishwasrao C, Chakraborty S, Ananthanarayan L. Partial purification, characterisation and thermal inactivation kinetics of peroxidase and polyphenol oxidase isolated from Kalipatti sapota (Manilkara zapota). J Sci Food Agric. 2017;97(11):3568-3575.
Vishwasrao, C., Chakraborty, S., & Ananthanarayan, L. (2017). Partial purification, characterisation and thermal inactivation kinetics of peroxidase and polyphenol oxidase isolated from Kalipatti sapota (Manilkara zapota). Journal of the Science of Food and Agriculture, 97(11), pp. 3568-3575. doi:10.1002/jsfa.8215.
Vishwasrao C, Chakraborty S, Ananthanarayan L. Partial Purification, Characterisation and Thermal Inactivation Kinetics of Peroxidase and Polyphenol Oxidase Isolated From Kalipatti Sapota (Manilkara Zapota). J Sci Food Agric. 2017;97(11):3568-3575. PubMed PMID: 28098357.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Partial purification, characterisation and thermal inactivation kinetics of peroxidase and polyphenol oxidase isolated from Kalipatti sapota (Manilkara zapota). AU - Vishwasrao,Chandrahas, AU - Chakraborty,Snehasis, AU - Ananthanarayan,Laxmi, Y1 - 2017/02/22/ PY - 2016/10/20/received PY - 2016/12/17/revised PY - 2017/01/12/accepted PY - 2017/1/18/pubmed PY - 2017/12/15/medline PY - 2017/1/19/entrez KW - D-value KW - Manilkara zapota KW - peroxidase KW - polyphenol oxidase KW - size exclusion chromatography KW - thermal inactivation SP - 3568 EP - 3575 JF - Journal of the science of food and agriculture JO - J. Sci. Food Agric. VL - 97 IS - 11 N2 - BACKGROUND: The extraction, purification, and characterisation of peroxidase (POD) and polyphenol oxidase (PPO) were studied for Kalipatti sapota fruit. The crude enzyme extract was partially purified by ammonium sulfate precipitation followed by BioGel P100 size exclusion and Unosphere Q anion-exchange chromatography. RESULTS: Molecular weights of 20 kDa (POD) and 24 kDa (PPO) were indicated by SDS-PAGE. A single band was observed on SDS-PAGE with a fold purity of 10.38 and 7.42 for POD and PPO, respectively. Michaelis-Menten constants for POD and PPO were 22.3 and 23.0 mmol L-1 using guaiacol and catechol as substrates. Thermal inactivation kinetics was studied in the temperature range of 60-95 °C. The crude extract of POD and PPO showed D-values of 2.2-60.2 and 1.0-35.2 min; Z-values of 18.7 ± 0.4 and 16.0 ± 0.3 °C; and activation energies (Ea) of 128.6 and 151.0 kJ mol-1 , respectively. CONCLUSION: POD and PPO showed good stability over a wide range of pH and temperature. As reflected by Z and Ea values, the fruit matrix had no significant influence towards enzyme stability. Designing of thermal process should take into consideration D- and Z-values of the enzymes along with D- and Z-values of microorganisms to obtain a product with better shelf life. © 2017 Society of Chemical Industry. SN - 1097-0010 UR - https://www.unboundmedicine.com/medline/citation/28098357/Partial_purification_characterisation_and_thermal_inactivation_kinetics_of_peroxidase_and_polyphenol_oxidase_isolated_from_Kalipatti_sapota__Manilkara_zapota__ L2 - https://doi.org/10.1002/jsfa.8215 DB - PRIME DP - Unbound Medicine ER -