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High-Pressure Inactivation of Enzymes: A Review on Its Recent Applications on Fruit Purees and Juices

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WILEY
DOI: 10.1111/1541-4337.12071

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enzyme kinetics; high-pressure processing; polyphenoloxidase; peroxidase; pectinmethylesterase

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  1. Indian Inst. of Technology, Kharagpur

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In the last 2 decades high-pressure processing (HPP) has established itself as one of the most suitable nonthermal technologies applied to fruit products for the extension of shelf-life. Several oxidative and pectic enzymes are responsible for deterioration in color, flavor, and texture in fruit purees and juices (FP&J). The effect of HPP on the activities of polyphenoloxidase, peroxidase, -glucosidase, pectinmethylesterase, polygalacturonase, lipoxygenase, amylase, and hydroperoxide lyase specific to FP&J have been studied by several researchers. In most of the cases, partial inactivation of the target enzymes was possible under the experimental domain, although their pressure sensitivity largely depended on the origin and their microenvironmental condition. The variable sensitivity of different enzymes also reflects on their kinetics. Several empirical models have been established to describe the kinetics of an enzyme specific to a FP&J. The scientific literature in the last decade illustrating the effects of HPP on enzymes in FP&J, enzymatic action on those products, mechanism of enzyme inactivation during high pressure, their inactivation kinetics, and several intrinsic and extrinsic factors influencing the efficacy of HPP is critically reviewed in this article. In addition, process optimization of HPP targeting specific enzymes is of great interest from an industrial approach. This review will give a fair idea about the target enzymes specific to FP&J and the optimum conditions needed to achieve sufficient inactivation during HPP treatment.

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