Digestibility in vitro and available lysine contents of Indian oilseed meals.

Experiments with untreated and autoclaved meals of mowra (Bassia latifolia), pisa (Actinodaphne hookeri) and undi (Calophyllum inophyllum) are reported. The three meals were digested by pepsin to approximately the same extent as casein. While pisa and undi meals were fairly rapidly degraded by trypsin, mowra meal was cleaved slowly, but did not possess any trysin inhibiting activity. Destruction and inactivation of amino acids were caused by autoclaving the meals. The presence of naturally occurring trypsin-resistant bonds in mowra meal protein is inferred. The nutritional significance of the amounts of FDNB-reactive lysine units in these meals is discussed.