PubMed · 14466329
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W P LOH. 1962. Gastric function tests.. https://pubmed.ncbi.nlm.nih.gov/14466329/
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Fungal mycelial proteins are promising sustainable protein sources, yet their nutritional utilization is often limited by structural constraints. This study systematically evaluated the effects of protein isolation on the proteomic composition, gastrointestinal digestion behavior, amino acid utilization, and bioactivity of Pleurotus citrinopileatus mycelial proteins. Quantitative proteomics identified 3591 proteins, of which 3374 were shared between mycelial flour (PCMF) and protein isolate (PCMPI), indicating that PCMPI primarily represents the soluble proteome fraction. In vitro digestion revealed that PCMPI exhibited significantly higher digestibility (93.98%) than PCMF (42.98%) (p < 0.05), reaching levels comparable to whey protein isolate. Enhanced enzymatic accessibility in PCMPI promoted rapid peptide generation during the gastric phase and efficient amino acid release during the intestinal phase, resulting in higher peptide (634.76 mg/g) and free amino acid levels (341.69 mg/g) at the digestion endpoint. Consequently, PCMPI achieved a balanced amino acid profile with a PDCAAS of 1.0. Moreover, its digestion products exhibited stronger antioxidant activity (IC₅₀ = 8.36 mg/mL) and ACE inhibitory activity (IC₅₀ = 15.65 mg/mL) compared with PCMF. Mechanistically, protein isolation disrupted the cell wall matrix, shifting digestion from a structure-limited to an accessibility-driven regime. Collectively, these findings demonstrate that protein isolation markedly enhances the digestibility, nutritional quality, and functional potential of mycelial proteins, supporting their application as high-value sustainable protein ingredients.
BACKGROUND: Feeding intolerance (ie, achieving and maintaining full enteral feedings) is a significant problem in preterm infants. A relation exists between feeding intolerance and incomplete lactose digestion. OBJECTIVES: We sought to identify the factors relating to lactose digestion and absorption, lactase activity, and small-intestinal mucosal growth. DESIGN: Lactose digestion and absorption, lactase-specific activity, and lumen-to-mucosa water flux as a measure of small-intestinal mucosal surface area were determined by using the triple-lumen perfusion technique on 2 occasions 3 wk apart in 10 preterm infants (x+/-SEM gestational age: 28.0+/-0.2 wk). RESULTS: Lactose digestion and absorption and lactase activity doubled between studies (P=0.035 and P=0.041, respectively). The change in digestion and absorption was related to lactase activity (P=0.034, R2=0.38). Lactase activity correlated with gestational age at birth (P=0.012, R2=0.51). The number of days of feeding explained 80% of the variability in small-intestinal mucosal surface area (P=0.001). CONCLUSIONS: To our knowledge, this is the first study to measure directly lactose digestion and absorption, lactase activity, and small-intestinal surface area in preterm infants. Changes in lactose absorption relate primarily to lactase activity rather than to mucosal growth. We showed directly a relation between enteral feeding and small-intestinal mucosal growth.
An in vitro protein digestion study, using pepsin, was carried out in uncooked and cooked sorghum and maize flour samples. The digestibility values from the uncooked samples showed that sorghum presents digestibility values similar to those of maize. In the case of the cooked samples, it was found that a wet cooking procedure promotes a decrease in sorghum protein digestibility when compared to maize. Electrophoresis was used to follow the in vitro pepsin sequential digestion procedure, and infrared spectroscopy was applied to establish its efficiency. SDS-PAGE results showed that both uncooked samples (sorghum and maize) behave in a similar way. The wet cooking procedure increases the amount of high molecular weight aggregates and promotes the appearance of two nonreducible and nondigestible 45 and 47 kDa proteins. These two protein fractions are directly related to the loss of digestibility. It was also shown that in cooked sorghum the monomers (gamma-, alpha-, and beta-) are more resistant to digestion than the corresponding uncooked samples.