Literature DB >> 15113178

Inactivation kinetics of purified tomato polygalacturonase by thermal and high-pressure processing.

Diana Fachin1, Chantal Smout, Isabel Verlent, Binh Ly Nguyen, Ann M Van Loey, Marc E Hendrickx.   

Abstract

Tomato polygalacturonase (PG) was extracted from ripe tomatoes and purified by cation exchange and gel filtration chromatography. Cation exchange chromatography yielded two peaks with PG activity: the first peak was identified as PG2 (the heat labile form) and the second one as PG1 (the heat stable form). Both PG2 and PG1 presented a molar mass of 42 kDa when analyzed by SDS-PAGE and an isoelectric point >9.3. Thermal inactivation of purified tomato PG2, at pH 4.4, in the temperature range from 53 to 63 degrees C, followed first-order kinetics. Combined pressure-temperature inactivation of tomato PG2 was studied at 5-55 degrees C/100-600MPa. Under all pressure-temperature conditions, PG2 inactivation followed first-order kinetics. Purified tomato PG1, although more thermostable than PG2, showed a pressure stability very similar to that of PG2. These results indicate that high-pressure processing is an efficient alternative to inactivate tomato PG without the need for applying high temperatures.

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Year:  2004        PMID: 15113178     DOI: 10.1021/jf030531h

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  1 in total

Review 1.  Effect of pulsed light treatment on enzymes and protein allergens associated with their structural changes: a review.

Authors:  Abeer S Alhendi
Journal:  J Food Sci Technol       Date:  2020-11-18       Impact factor: 3.117

  1 in total

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