Phaseolin diversity as a possible strategy to improve the nutritional value of common beans (Phaseolus vulgaris)

This article proposes a new way to improve the protein quality of the common bean (Phaseolus vulgaris). It is based on the natural variability found in the different types of phaseolin, its main storage protein (40 50% of the total protein). Despite the fact that it is deficient in methionine content, phaseolin still represents the main source of that amino acid in the seed. More than 40 genetic variants, differing in subunit number (2 6) and molecular weight (40 54 kDa) have been analyzed. The similarity of the amino acid composition among phaseolins, suggests that a nutritional improvement cannot be expected from that side. Conversely, important variation in phaseolin susceptibility to proteolysis (ranging from 57% to 96% after cooking) has been observed, increasing the theoretical availability of methionine by up to 37%. Therefore, breeding programs based on highly-digestible phaseolin types could lead to the production of beans with higher protein quality

Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats

Phaseolus vulgaris phaseolin has been shown to stimulate faecal losses of endogenous N in rats. Experiments with purified phaseolin were carried out in rats to test the hypothesis that these losses reflect intestinal disorders. Phaseolin composition varies depending on its constitutive subunits. Therefore, three phaseolin types (S, T, I) were tested. Phaseolin T was incorporated in varying levels (0, 33, 67 or 100% of the dietary protein) as raw material in experiment 1. In experiment 2, the three phaseolin types were incorporated at 50%, with or without previous thermic treatment. Raw casein was the basal protein source and was also heated in experiment 2. Faecal digestibility of phaseolin and gut integrity were evaluated in both experiments. The incorporation level or type of phaseolin had little effect on gross anatomy of gut segments but these factors influenced the weight and pH of fresh contents of the stomach and caecum (P<0·05). Raw phaseolin T incorporated at various levels led to an enlargement of duodenal villi together with a tendency for increased crypt depth in the jejunum (P=0·06). Activities of both alkaline phosphatase in the duodenum and aminopeptidase N in the ileum decreased (P<0·05) after thermal treatment of casein while they increased (P<0·05) for heat-treated phaseolin S and T, respectively. In conclusion, raw phaseolin had no effect on the tissue weight of gut segments and induced limited alterations in the small intestine. Differences due to phaseolin level or type were limited too

Phaseolin type and heat treatment influence the biochemistry of protein digestion in the rat intestine

The study aimed to investigate the in vivo digestion of Phaseolus vulgaris phaseolin types differing in their subunit pattern composition. Diets contained either casein as the sole source of protein or a mixture (1:1) of casein and pure Sanilac (S), Tendergreen (T) or Inca (I) phaseolin either unheated or heated. Rats were fed for 11 d with the experimental diets. Their ileal content and mucosa were collected and prepared for electrophoresis, Western blotting, densitometry and MS. Differences in digestion among native phaseolin types were observed for intact phaseolin at molecular weights (MW) of 47 50·5 kDa and for an undigested fragment at MW of 19 21·5 kDa in ileal digesta. In both cases, the concentration of these protein bands was lower for I phaseolin than for S or T phaseolin (P < 0·05). In the mucosa, the concentration of a protein band at MW of 20·5 21·5 kDa was lower for S phaseolin as compared to T or I phaseolin (P < 0·001). The presence of phaseolin subunits and their fragments was confirmed by Western blotting. MS analysis revealed the presence of undigested ? and ? subunit fragments from phaseolin and endogenous proteins (anionic trypsin I and pancreatic ?-amylase) in ileal digesta. Thermal treatment improved digestion (P < 0·01), acting on both dietary and endogenous protein components. In conclusion, this study provides evidence for differences in intestinal digestion among phaseolin types, S phaseolin being more resistant and I phaseolin more susceptible. These differences were affected by the origin of the phaseolin subunit precursor. Heat treatment enhanced phaseolin digestion

Phaseolin from Phaseolus vulgaris bean modulates gut mucin flow and gene expression in rats

Dietary protein might modulate mucin flow and intestinal mucin gene expression. Since unheated phaseolin from Phaseolus vulgaris bean is resistant to digestion and increases gut endogenous protein losses, we hypothesised that unheated phaseolin influences mucin flow and gene expression, and that phaseolin heat treatment reverses these effects. The hypothesis was tested using a control diet containing casein as the sole protein source and three other diets with casein being replaced by 33 and 67 % of unheated and 67 % of heated phaseolin. The rats were fed for 6 d and euthanised. Digesta and faeces were collected for determining digestibility and mucin flow. Gut tissues were collected for mucin (Muc1, Muc2, Muc3 and Muc4) and Trefoil factor 3 (Tff3) gene expressions. Colonic mucin flow decreased linearly with increasing the dietary level of unheated phaseolin (P < 0·05). Unheated phaseolin increased N flow in ileum, colon and faeces (P < 0·05), and reduced apparent N digestibility linearly (P < 0·01). Heat treatment reversed all these changes (P < 0·05 to < 0·001), except mucin flow. The expressions of Muc mRNA in gut tissues were influenced by dietary phaseolin level (ileum and colon: Muc3 and Muc4) and thermal treatment (ileum: Muc2; colon: Muc2, Muc3, Muc4 and Tff3) (P < 0·05 to 0·001). In conclusion, phaseolin modulates mucin flow and Muc gene expression along the intestines differentially