Acute effect of soybean beta-conglycinin hydrolysate ingestion on appetite sensations in healthy humans.

A hydrolysate prepared from soybean beta-conglycinin reduced food intake through cholecystokinin release in rats; however, effects of the hydrolysate on human appetites are unknown. In this study, healthy volunteers ingested 3g of the beta-conglycinin hydrolysate (BconB) and/or a soy protein hydrolysate (HN) contained in a beverage or in a jelly. Appetite profiles (hunger, fullness and prospective consumption) after the ingestion and palatability of test jellies were recorded. Fullness was rated higher, and hunger was rated lower after BconB ingestion as compared to HN ingestion. These results demonstrate that 3g of BconB is effective to enhance fullness and reduce hunger sensations in healthy humans.

Soybean ß-conglycinin bromelain hydrolysate stimulates cholecystokinin secretion by enteroendocrine STC-1 cells to suppress the appetite of rats under meal-feeding conditions.

A peptic digest of soybean ß-conglycinin (BconP) suppresses the appetite in rats through cholecystokinin (CCK) secretion by enteroendocrine cells. We investigate in this study more appetite-suppressing hydrolysates. ß-Conglycinin hydrolyzed with food-processing proteases thermolysin (BconT), bromelain (BconB), chymotrypsin, protease S, and protease M was examined for CCK-secreting activity in a CCK-producing cell line for comparison with BconP. The potent CCK-releasing hydrolysates were then tested for their suppression of the food intake by rats. BconB, BconT, and BconP stimulated high CCK secretion, with the highest by BconB. Orogastric preloading by BconB, but not by BconT, suppressed the 60-min food intake. A meal-feeding trial twice a day in the morning (a.m.) and evening (p.m.) for 10 d showed that BconB preloading before every meal attenuated the p.m. meal size, but not that a.m., resulting in an overall reduction of the daily meal size. These results demonstrate that the bromelain hydrolysate of ß-conglycinin having potent CCK-releasing activity suppressed the appetite of rats under meal-feeding conditions.

Structural studies by stepwise enzymatic degradation of the main backbone of soybean soluble polysaccharides consisting of galacturonan and rhamnogalacturonan.

Soybean soluble polysaccharides (SSPS) extracted from soybean cotyledons are acidic polysaccharides and have a pectin-like structure. The results of a structural analysis of SSPS by using polygalacturonase (PGase) and rhamnogalacturonase (RGase) clarified that the main backbone consisted of galacturonan (GN) and rhamnogalacturonan (RG), which were composed of the diglycosyl repeating unit, -4)-alpha-D-GalpA-(1-->2)-alpha-L-Rhap-(1-. The side chains of beta-1,4-galactans, branched with fucose and arabinose residues, were linked to the C-4 side of rhamnose residues in the RG regions. The degree of polymerization (dps) of GN, which linked the RG regions together, was estimated to be about 4-10 residues, and some were modified with xylose residues on the C-3 side of the galacturonates. The dps of GN at the reducing end of SSPS was estimated to be about 7-9 residues. Moreover, the fragment of the basic structure of the RG region, -[4)-alpha-D-GalpA-(1-->2)-alpha-L-Rhap-(1-]2-, some of which had long-chain beta-1,4-galactans branched on the C-4 side of rhamnose residues, were liberated from SSPS by the RGase treatment. The dps of the galactan side chain was estimated to be about 43-47 residues by an analysis of the digestion products from the beta-galactosidase treatment.