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.
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.
Nixtamalized maize flours elaborated by four factories in Mexico were used for tortilla preparation. Samples were stored at 4 degrees C for up to 72 h and their in vitro starch digestibility features were evaluated. Moisture content was different between flour and tortilla but no evident relation could be established. Protein and lipid levels were lower in tortillas than in flour but ash content was not different in both samples. A decrease in available starch content was observed upon 48 h cold storage (4 degrees C), changes that were concomitant with increased total resistant starch (RS) levels. These changes were due mainly to retrogradation, as suggested by the increased retrograded resistant starch (RRS) levels recorded in stored tortillas; in some samples, RRS represented up to 100% of total RS. The digestion (alpha-amylolysis) rate (DR) of freshly prepared tortillas differed for the various samples. Although the amylolysis patterns for fresh and 72 h-stored tortillas were similar, lower DR values were shown for the stored materials. The differences found among the various tortilla samples may be due to variations in processing conditions during commercial maize flour preparation, and to the use of different maize varieties.