Effect of pH on pulsed light inactivation of polyphenol oxidase

The inactivation of diverse food enzymes by pulsed light (PL) has been described before, including the inactivation of polyphenol oxidase (PPO) (at pH 6.5). Since the pH affects the conformation of enzymes, it may influence the inactivation of enzymes by PL. The aim of this work was to evaluate the...

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Detalles Bibliográficos
Autores: Pellicer, José Antonio, Gabaldón, José Antonio, Gómez López, Vicente Manuel
Tipo de recurso: artículo
Fecha de publicación:2021
País:España
Institución:Universidad Católica San Antonio de Murcia (UCAM)
Repositorio:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
OAI Identifier:oai:repositorio.ucam.edu:10952/8731
Acceso en línea:http://hdl.handle.net/10952/8731
Access Level:acceso abierto
Palabra clave:Pulsed light
Polyphenol oxidase
pH
Enzyme inactivation
Structure function
Descripción
Sumario:The inactivation of diverse food enzymes by pulsed light (PL) has been described before, including the inactivation of polyphenol oxidase (PPO) (at pH 6.5). Since the pH affects the conformation of enzymes, it may influence the inactivation of enzymes by PL. The aim of this work was to evaluate the effect of pH on the kinetics of the PL-inactivation and associated structural changes of a case enzyme. To this, PPO was treated by PL at different pHs (4.0–6.5) and its inactivation kinetics and changes in its structure were evaluated by spectrophotometric and spectrofluorometric methods. The inactivation proceeded faster at low pH and was highly correlated with the decrease in peak intrinsic fluorescence intensity. Phase diagrams and parameter A evolution indicated the absence of intermediate unfolded states during the course of the inactivation. No protein aggregation was detected by turbidimetry. Results indicate that although a low pH favors the PL-inactivation of PPO, the mechanism of inactivation is pH-independent. Beyond the specific outcome for PPO, the results are evidence of a general pH-independence in the mechanism of enzyme inactivation by PL in the pH range 4.0–6.5 and acidification can be a strategy to decrease treatment times during PL processing.