Processed Vegetable Protein Mixtures for Human Consumption in Developing Countries

β -Glucosidase activity and bioconversion of isoflavones during fermentation of soymilk

“…There are 12 main isoflavone components, including three free aglycone isoflavones (daidzein, genistein and glycitin) and their respective glucosidic, malonyl glucosidic and acetyl glucosidic conjugates, In general, isoflavones in soybeans exist mainly as glucoside forms and rarely as aglycone forms unless they have been fermented . Soymilk is the watery extract of soybeans that is an inexpensive source of protein and calories for human consumption . To improve the quality, nutritive value and sensory properties of soymilk, fermentation with lactic acid bacteria (LAB) has been the alternative way to minimize phytate contents, antinutrients, etc.…”

Biological effects of isolated trypsin inhibitor from winged bean (Psophocarpus tetragonolobus) on rats

“…As far as we know, this is the only study of its kind where sufficient quantities of trypsin inhibitor were isolated from winged bean by affinity column chromatography, its in vitro activity was confirmed, and it was fed to rats under controlled conditions. In general, plant proteins have lower digestibility and amino acid availability resulting from factors inherent in the seed and the decrease resulting from processing (Bressani and Elias, 1968). It is interesting to note that the PER of the heated bean gioup (AWB) was lower than the WBTI group, yet no pancreatic hypertrophy was observed in AWB.…”

Cereal proteins: Chemistry and food applications

“…A recent review gave an excellent account of the amino acid composition of plant proteins in general as it relates to their quality. 222 It must be pointed out at the outset that cereal proteins in general are deficient in one or more essential amino acids, the most limiting essential amino acid being lysine for all cereal proteins. In many instances the primary deficiency of one amino acid, namely lysine, is further intensified by a secondary deficiency of other amino acids, e.g., threonine and/or tryptophan.…”