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Zymograms of a crude protein extract from S. cerevisiae strain SCPP containing endopolygalacturonase were studied and compared to the purified enzyme by determining their physico-chemical properties. The results obtained with crude extract were similar to those of the purified enzyme. The endopolygalacturonase from both sources displayed a pH optimum between 3.0 and 4.0, and was active at temperatures between 4 and 50°C on a large panel of substrates. These characteristics make this S. cerevisiae endopolygalacturonase an attractive tool for the beverage industry. Journal of Industrial Microbiology & Biotechnology (2000) 24, 296–300.
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Belarbi et al. (2000) studied this question.
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