2021
DOI: 10.1016/j.ijbiomac.2021.05.014
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Pea cell wall integrity controls the starch and protein digestion properties in the INFOGEST in vitro simulation

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Cited by 27 publications
(10 citation statements)
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“…In the intestinal phase, the DH% of all lentil protein fractions increased dramatically during the initial 30 min but leveled off toward the end of digestion. The final DH% values of lentil protein fractions in the intestinal phase were in the range of 24.25%−30.93%, which were comparable to the other reported pulse proteins, such as 22.5% for lentil protein 40 and 31.0% for pea protein, 42 but were notably lower than that of animal proteins (e.g., 52% for whey proteins). 17 In general, factors such as protease inhibitors, including trypsin inhibitors and tannins, are responsible for the lower digestibility of plant proteins when compared to animal proteins.…”
Section: Digestibility Of Lentil Protein Fractionssupporting
confidence: 79%
See 1 more Smart Citation
“…In the intestinal phase, the DH% of all lentil protein fractions increased dramatically during the initial 30 min but leveled off toward the end of digestion. The final DH% values of lentil protein fractions in the intestinal phase were in the range of 24.25%−30.93%, which were comparable to the other reported pulse proteins, such as 22.5% for lentil protein 40 and 31.0% for pea protein, 42 but were notably lower than that of animal proteins (e.g., 52% for whey proteins). 17 In general, factors such as protease inhibitors, including trypsin inhibitors and tannins, are responsible for the lower digestibility of plant proteins when compared to animal proteins.…”
Section: Digestibility Of Lentil Protein Fractionssupporting
confidence: 79%
“…17 In general, factors such as protease inhibitors, including trypsin inhibitors and tannins, are responsible for the lower digestibility of plant proteins when compared to animal proteins. 19,42 Comparing the digestibility of the lentil protein fractions, LL yielded the highest DH%, while LA had the lowest. There are two potential causes of the lower protein digestibility of albumin when compared to globulin.…”
Section: Digestibility Of Lentil Protein Fractionsmentioning
confidence: 99%
“…β, and γ) [31]. The polypeptides at 20 and ≤14 kDa visible in GDCPC and GIDCPC might correspond to fragments resulting from the action of digestive enzymes on vicilin [32]. The protein profiles of the fractions higher than 10 kDa obtained from GDCPC (lane 8) and GIDCPC (lane 12) were similar to those of their corresponding complete digests (lanes 7 and 11).…”
Section: Characterization Of Chachafruto Seed Protein Concentrate (Cp...mentioning
confidence: 74%
“…The band ≈ 50 kDa might be assigned to vicilin, an oligomeric protein made of three polypeptide subunits (α, β, and γ) [31]. The polypeptides at 20 and ≤14 kDa visible in GDCPC and GIDCPC might correspond to fragments resulting from the action of digestive enzymes on vicilin [32]. β, and γ) [31].…”
Section: Characterization Of Chachafruto Seed Protein Concentrate (Cp...mentioning
confidence: 99%
“…The influence of cooking time on the microstructural and linked in vitro macronutrient digestibility of several pulse types has been studied, revealing important intrinsic differences between pulse types [15], as elaborated below. Most commonly, since individual cotyledon cells can be considered a representative fraction of disintegrated cooked pulse seeds, isolated cotyledon cells (ICC) are considered [20][21][22][23][24][25][26][27][28][29][30]. Since this approach entails the omission of certain fractions (such as cell clusters, fiber-rich seed coat material, and ruptured cells), it can be considered a reductionist approach [30,31].…”
Section: Introductionmentioning
confidence: 99%