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In vitro amino acid digestibility of food proteins as measured by the digestion cell technique


The digestibility of proteins and individual amino acids of nineteen selected foods was determined by anin vitro assay. Samples were hydrolysed with pepsin for 30 minutes in an acidic medium; the pH was then raised to 7.5 and the mixture poured into the dialysis bag (molecular weight cut-off 1000) of a digestion cell with pancreatin. Digestion products, mixtures of free amino acids and low molecular weight peptides which pass through the dialysis membrane, were collected for 6 hours by sodium phosphate buffer circulation. All proteins from animal sources displayed a digestibility similar to casein, except for breakfast sausage. Vegetable proteins showed intermediate digestibility, except for cereals (lower) or peanut butter (higher). Target amino acids of enzymes were generally more readily hydrolysed. However, compared to other animal proteins, glycine in milk products, valine, isoleucine, methionine and lysine in breakfast sausage and hot dog, and histidine in tuna were more easily released. Overheating of non-fat dried milk not only reduced the lysine digestibility, but also that of methionine, phenylalanine, histidine and cystine. Among vegetable proteins, wheat products were characterized by a relatively greater release of threonine, isoleucine and histidine, and peas by a lower digestibility of methionine and lysine. Proline of soy isolate and isoleucine of pinto bean were resistant to hydrolysis while arginine of pinto beans and of rice-wheat-gluten was easily released.

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Savoie, L., Charbonneau, R. & Parent, G. In vitro amino acid digestibility of food proteins as measured by the digestion cell technique. Plant Food Hum Nutr 39, 93–107 (1989).

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Key words

  • proteins
  • amino acid digestibility
  • pepsin
  • pancreatin