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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 spec
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