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Cited by 141 publications
(93 citation statements)
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References 32 publications
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“…The protocol followed was derived from prior reports (19,20,21). Lyophilized powders of enzymes and comparator proteins (α-casein from bovine milk, β-lactoglobulin from bovine milk, trypsin inhibitor from Glycine max) as well as reagents were purchased from Sigma-Aldrich.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…The protocol followed was derived from prior reports (19,20,21). Lyophilized powders of enzymes and comparator proteins (α-casein from bovine milk, β-lactoglobulin from bovine milk, trypsin inhibitor from Glycine max) as well as reagents were purchased from Sigma-Aldrich.…”
Section: Methodsmentioning
confidence: 99%
“…We evaluated the digestibility of colicin proteins in the human GI tract using treatments with simulated gastric and intestinal fluids (SGF and SIF, respectively). Sequential exposure studies using physiological enzyme-to-substrate ratios were conducted to mimic the natural human GI tract conditions (19)(20)(21). For these studies, the colicins were first exposed to either SGF without or with pepsin, at a pepsin-to-colicin ratio of 1:20 on a weight basis, followed by exposure of the resultant hydrolysate products to SIF supplemented with trypsin and chymotrypsin at a ratio of 1:4:400 (trypsin:chymotrypsin:colicin peptides, on a weight basis).…”
Section: Gastric and Intestinal Proteases Digest Plant-produced Colicmentioning
confidence: 99%
“…11−13 However, while pepsin stability as a part of an allergenicity assessment would still seem reasonable for the purpose of safety evaluation of most food proteins, we now know that for some allergenic proteins, this approach would be misleading. The milk allergen β-casein (Bos d 8) 7,14,15 as well as the peanut allergen Ara h 1 9,10 have several times been shown to be easily digestible food allergens.…”
Section: ■ Introductionmentioning
confidence: 99%
“…Certainly from the perspective of comparison it is useful to use a consistent activity of enzyme such as the 2,000 U/mL given above and a consistent protein concentration. For example in a ring trial comparing the digestion of milk proteins β-lactoglobulin and β-casein in different laboratories (Mandalari et al 2009a ), two regimes were used, a high and a low protease activity. The high protease used a pepsin activity of 10,560 U/mL based on haemoglobin as a substrate and a substrate concentration of 0.25 mg/mL, equivalent to a pepsin activity of 42,240 U/ mg substrate.…”
Section: Static Models For Protein Hydrolysismentioning
confidence: 99%