Biochemical changes and in-vitro protein digestibility of the endosperm of germinating dolichos lablab. protein digestive capacity and efficiency can be identified with the toolsets of peptidomics, metabolomics, microbial sequencing and multiplexed protein analysis of fecal and urine samples. By monitoring individual protein digestive function, the protein component of diets can be tailored via protein source and processing selection to match individual needs to minimize colonic putrefaction and, thus, optimize gut health. and (Macfarlane et al., 1986; Shen et al., 2010; An et al., 2014). Increasing protein in the colon correlates with increased putrefactive bacteria and metabolites (Toden et al., 2007; Lubbs et al., 2009) and reduced carbohydrate-fermenting bacteria such as (Duncan et al., PF-00562271 2007). Unlike carbohydrate-based fiber fermentation in the colon, which is considered beneficial or benign, microbial protein putrefaction could be detrimental (Davila et al., 2013). In fermenting fiber, commensal microbes produce beneficial metabolites, including short-chain fatty acids (e.g., butyrate, which serves as the primary energy source for the colonic epithelium (Roediger, 1980; Roediger, 1982; Hamer et al., 2008)) and certain vitamins (LeBlanc et al., 2013). Beyond serving as an energy source, the short-chain fatty acids produced also lower the intraluminal pH, which inhibits the growth of some pathogens (Byrne and Dankert, 1979). Like fiber fermentation, putrefaction leads to some short-chain fatty acid production. However, unlike fiber fermentation, putrefactive bacteria also produce an array of metabolic byproducts including ammonia, PF-00562271 sulfides, phenols (e.g. reduce colonic epithelial cell viability (Pedersen et al., 2002), increase intestinal permeability (Ng and Tonzetich, 1984; Jowett et al., 2004; Hughes et al., 2008; McCall et al., 2009), provoke DNA damage (Attene-Ramos et al., 2006) and inhibit colonocyte cellular respiration and proliferation (Roediger et al., 1993; Leschelle et al., 2005; Medani et al., 2011; Andriamihaja et al., 2015). Increasing protein intake by humans from 15.4% to 23.8% of the diet for one week, while maintaining resistant carbohydrate intake, increased fecal and urinary markers of putrefactionincluding ammonia, valeric acid, urinary have higher protein digestibility than unfermented soybeans. secretes proteases that break down proteins in fermented soy (Chancharoonpong et al., 2012). When fed to piglets, also degrades AA and releases ammonia, which increases the pHhence Dalkali fermentation (Parkouda et al., 2009). Soybeans are fermented by to produce Japanese natto (Wang and Fung, 1996). The degradation of proteins in alkali fermentations likely means that these proteins have increased digestibility. Bacterial protein degradation also can degrade trypsin inhibitors, thus improving overall protein digestibility (Hong et al., 2004). Fermentation of rye flour with lactic acid bacteria sourdough cultures hydrolyzes prolamins (a group of plant storage proteins high in proline and similar to gluten). This fermentation approach could reduce reactivity in humans with celiac disease by degrading prolamin epitopes that may contaminate a gluten-free diet (De Angelis et al., 2006). Similarly, a 24-hour lactic acid bacterial fermentation of wheat flour degraded gliadin and did not increase intestinal permeability in celiac patients (Di Cagno et al., 2004). Indeed, specific species with the ability to degrade the immunotoxic peptides related to celiac responses have been identified (Duar et al., 2015). A 48-hour fermentation of wheat flour with three Enterococcus strains and degraded 98% of the gluten protein (Mhir et al., 2009). Fermentation approaches not only reduces the allergenicity of some proteins but also improves overall protein digestibility. Future personalization of protein digestibility to protein digestive capacity can take advantage of naturally pre-digested foods to match the protein digestibility requirements of individuals with lower digestive capacity. Hydrolysates Proteins can be hydrolyzed, either extensively or partially, via treatment with proteases, acid or alkali (Clemente, 2000). Acid and alkali hydrolyses are difficult to control and they can modify/destroy AA, which lowers the nutritional quality of a product. As proteases do not alter the AA, they are PF-00562271 preferred for making hydrolysates. Common protein sources used for preparing nutritional hydrolysates are bovine milk and soybeans (Chiang et al., 1999). Hydrolyzed foods have a variety of uses, including in infant formulas, nutritional supplements for the elderly and sports nutrition products. Other Processing Plxnc1 A PF-00562271 variety of other processing methods, including soaking, germination, dehulling, pressure cooking, high pressure processing, extrusion,.