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Plant Physiology 71:132-135 (1983)
© 1983 American Society of Plant Biologists

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{beta}-Galactosidases in Ripening Tomatoes 1

Russell Pressey

Richard B. Russell Agricultural Research Center, Agricultural Research Service, United States Department of Agriculture, Athens, Georgia 30613

Tomatoes (Lycopersicon esculentum L.) contained a high level of {beta}-galactosidase activity which was due to three forms of the enzyme. During tomato ripening, the sum of their activities remained relatively constant, but the levels of the individual forms of {beta}-galactosidase changed markedly. The three enzymes were separated by a combination of chromatography of DEAE-Sephadex A-50 and Sephadex G-100. During ripening of tomatoes, {beta}-galactosidases I and III levels decreased but the {beta}-galactosidase II level increased more than 3-fold. The three enzymes were optimally active near pH 4, and all were inhibited by galactose and galactonolactone. However, the enzymes differed in molecular weight, Km value with p-nitrophenyl-{beta}-galactoside, and stability with respect to pH and temperature. {beta}-Galactosidase II was the only enzyme capable of hydrolyzing a polysaccharide that was isolated from tomatoes and that consisted primarily of {beta}-1, 4-linked galactose. The ability of {beta}-galactosidase II to degrade the galactan and the increase in its activity during tomato ripening suggest a possible role for this enzyme in tomato softening.

1 Mention of a trademark, proprietary product, or vendor does not constitute a guarantee or warranty of the product by the United States Department of Agriculture and does not imply its approval to the exclusion of other products or vendors that may also be suitable.




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