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Cellular and Molecular Life Sciences, Vol. 40, No. 8. (1 August 1984), pp. 842-843, doi:10.1007/bf01951984 Key: citeulike:11289005
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Summary Trichoderma reesei pectinesterase (isoelectric point 8.3–9.5; pH-optimum 7.6) catalyzes deesterification of pectin by giving rise to blocks of free carboxyl groups in the macromolecule; a mode similar to that observed with higher plant pectinesterases which also have I p and pH-optima in the alkaline region.
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