TY  - JOUR
  - Sullivan, LM,Kehoe, JJ,Barry, L,Buckley, MJM,Shanahan, F,Mok, KH,Brodkorb, A
  - 2014
  - August
  - British Journal of Nutrition
  - Gastric digestion of alpha-lactalbumin in adult human subjects using capsule endoscopy and nasogastric tube sampling
  - Validated
  - Altmetric: 2 ()
  - In vivo digestion Nasogastric tubes Capsule endoscopy Human and bovine alpha-lactalbumin made lethal to tumour cells (HAMLET and BAMLET) alpha-Lactalbumin TUMOR-CELLS BETA-LACTOGLOBULIN IN-VITRO OLEIC-ACID HAMLET PROTEIN LETHAL APOPTOSIS INFANTS SPECTROSCOPY
  - 112
  - 638
  - 646
  - In the present study, structural changes in the milk protein alpha-lactalbumin (alpha-LA) and its proteolysis were investigated for the potential formation of protein-fatty acid complexes during in vivo gastric digestion. Capsule endoscopy allowed visualisation of the digestion of the test drinks, with nasogastric tubes allowing sampling of the gastric contents. A total of ten healthy volunteers had nasogastric tubes inserted into the stomach and ingested test drinks containing 50 g/l of sucrose and 25 g/l of alpha-LA with and without 4 g/l of oleic acid (OA). The samples of gastric contents were collected for analysis at 3 min intervals. The results revealed a rapid decrease in the pH of the stomach of the subjects. The fasting pH of 2.31 (SD 1.19) increased to a pH maxima of pH 6.54 (SD 0.29) after ingestion, with a subsequent decrease to pH 2.22 (SD 1.91) after 21 min (n 8). Fluorescence spectroscopy and Fourier transform IR spectroscopy revealed partial protein unfolding, coinciding with the decrease in pH below the isoelectric point of alpha-LA. The activity of pepsin in the fasting state was found to be 39 (SD 12) units/ml of gastric juice. Rapid digestion of the protein occurred: after 15 min, no native protein was detected using SDS-PAGE; HPLC revealed the presence of small amounts of native protein after 24 min of gastric digestion. Mirocam (R) capsule endoscopy imaging and video clips (see the online supplementary material) revealed that gastric peristalsis resulted in a heterogeneous mixture during gastric digestion. Unfolding of alpha-LA was observed during gastric transit; however, there was no evidence of a cytotoxic complex being formed between alpha-LA and OA.
  - 10.1017/S0007114514001196
DA  - 2014/08
ER  - 

@article{V271356094,
   = {Sullivan,  LM and Kehoe,  JJ and Barry,  L and Buckley,  MJM and Shanahan,  F and Mok,  KH and Brodkorb,  A },
   = {2014},
   = {August},
   = {British Journal of Nutrition},
   = {Gastric digestion of alpha-lactalbumin in adult human subjects using capsule endoscopy and nasogastric tube sampling},
   = {Validated},
   = {Altmetric: 2 ()},
   = {In vivo digestion Nasogastric tubes Capsule endoscopy Human and bovine alpha-lactalbumin made lethal to tumour cells (HAMLET and BAMLET) alpha-Lactalbumin TUMOR-CELLS BETA-LACTOGLOBULIN IN-VITRO OLEIC-ACID HAMLET PROTEIN LETHAL APOPTOSIS INFANTS SPECTROSCOPY},
   = {112},
  pages = {638--646},
   = {{In the present study, structural changes in the milk protein alpha-lactalbumin (alpha-LA) and its proteolysis were investigated for the potential formation of protein-fatty acid complexes during in vivo gastric digestion. Capsule endoscopy allowed visualisation of the digestion of the test drinks, with nasogastric tubes allowing sampling of the gastric contents. A total of ten healthy volunteers had nasogastric tubes inserted into the stomach and ingested test drinks containing 50 g/l of sucrose and 25 g/l of alpha-LA with and without 4 g/l of oleic acid (OA). The samples of gastric contents were collected for analysis at 3 min intervals. The results revealed a rapid decrease in the pH of the stomach of the subjects. The fasting pH of 2.31 (SD 1.19) increased to a pH maxima of pH 6.54 (SD 0.29) after ingestion, with a subsequent decrease to pH 2.22 (SD 1.91) after 21 min (n 8). Fluorescence spectroscopy and Fourier transform IR spectroscopy revealed partial protein unfolding, coinciding with the decrease in pH below the isoelectric point of alpha-LA. The activity of pepsin in the fasting state was found to be 39 (SD 12) units/ml of gastric juice. Rapid digestion of the protein occurred: after 15 min, no native protein was detected using SDS-PAGE; HPLC revealed the presence of small amounts of native protein after 24 min of gastric digestion. Mirocam (R) capsule endoscopy imaging and video clips (see the online supplementary material) revealed that gastric peristalsis resulted in a heterogeneous mixture during gastric digestion. Unfolding of alpha-LA was observed during gastric transit; however, there was no evidence of a cytotoxic complex being formed between alpha-LA and OA.}},
   = {10.1017/S0007114514001196},
  source = {IRIS}
}