Limit dextrinase (EC 3.2.1.142) hydrolyses α‐1,6 glucosidic bonds in amylopectin and branched dextrins. Measurement of limit dextrinase activity during fermentation of unboiled wort at the pH of the wort has shown that its activity increases almost 10 fold during the first 10–15 h of fermentation and this increase in activity is unaffected by the presence of leupeptin, a cysteine protease inhibitor. The increase in activity seen when assays were carried out at pH 5.5 was much smaller and was reduced by leupeptin. The activity of limit dextrinase declined slowly during the latter part of the fermentation. It was established that the optimum pH for rapid extraction and assay of malt limit dextrinase in the absence of a reducing agent is approximately 4.5, but in the presence of dithiothreitol, at pH 5.5, activities 2–3 times higher can be obtained after 5 h extraction (600–700 mU/g dry weight). Limit dextrinase activities after 1 h extraction at mashing temperatures were below 20 mU/g dry weight if the mash pH was below 5.0. It is concluded that at pHs below 5.0, where limit dextrinase activity is below its optimum for activity, limit dextrinase activity increases due to dissociation of the inhibitor/enzyme complex. The protection from mashing temperatures of 65°C afforded by the inhibitor is lost at these lower pHs.

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