Abstract
The presence of proteinase inhibitors in legume seeds has been reported by numerous investigators and recently reviewed1. The trypsin and chymotrypsin inhibitors from soybeans, lima beans and groundnuts have been studied with respect to composition, structure and chemistry of the reactive sites2–7. Most of them have a molecular weight of about 8,000, are rich in cystine but lack cysteine and tryptophan. The Bowman-Birk inhibitor (AA) from soybeans8 and the lima bean inhibitor9,10 are double headed, with independent active sites, one against trypsin and the other against chymotrypsin. Here we present a study of a proteinase inhibitor from the seeds of the Bauhinia tree (classified as a legume11). This inhibitor has been found to be multifunctional and differs markedly from the hitherto reported trypsin inhibitors from legume seeds.
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