4.7 Article

Effect of temperature and/or pressure on tomato pectinesterase activity

期刊

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 48, 期 2, 页码 551-558

出版社

AMER CHEMICAL SOC
DOI: 10.1021/jf990569n

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tomato pectinesterase; thermal stability; pressure stability; kinetics; activation

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The activity of tomato pectinesterase (PE) was studied as a function of pressure (0.1-900 MPa) and temperature (20-75 degrees C). Tomato PE was rather heat labile at atmospheric pressure (inactivation in the temperature domain 57-65 degrees C), but it was very pressure resistant. Even at 900 MPa and 60 degrees C the inactivation was slower as compared to the same treatment at atmospheric pressure. At atmospheric pressure, optimal catalytic activity of PE was found at neutral pH and a temperature of 55 degrees C. Increasing pressure up to 300 MPa increased the enzyme activity as compared to atmospheric pressure. A maximal enzyme activity was found at 100-200 MPa combined with a temperature of 60-65 degrees C. The presence of Ca(2+) ions (60 mM) decreased the enzyme activity at atmospheric pressure in the temperature range 45-60 degrees C but increased enzyme activity at elevated pressure (up to 300 MPa). Maximal enzyme activity in the presence of Ca(2+) ions was noted at 200- 300 MPa in combination with a temperature of 65-70 degrees C.

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