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Alginate as a protease inhibitor in vitro and in a model gut system; selective inhibition of pepsin but not trypsin.

Chater PI, Wilcox MD, Brownlee IA, Pearson JP - Carbohydr Polym (2015)

Bottom Line: Alginates were shown to reduce pepsin activity by up to 53.9% (±9.5SD) in vitro.Limited inhibition of trypsin was shown.Significant inhibition of proteolysis was shown in the gastric phase of digestion, but not the small intestinal phase.

View Article: PubMed Central - PubMed

Affiliation: Institute for Cell and Molecular Biosciences (ICaMB), Medical School, Newcastle University, Catherine Cookson Building, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom. Electronic address: peter.chater@ncl.ac.uk.

No MeSH data available.


Related in: MedlinePlus

(a–c) pH dependent viscosity interaction of alginates with BSA (10 mg/ml) and casein (10 mg/ml) across the pH range (n = 3). (a) H120L (2.5 mg/ml) molecular weight = 397,000, (b) LFR560 (2.5 mg/ml) molecular weight = 34,700, (c) SF200 (2.5 mg/ml) molecular weight = 387,000.
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fig0015: (a–c) pH dependent viscosity interaction of alginates with BSA (10 mg/ml) and casein (10 mg/ml) across the pH range (n = 3). (a) H120L (2.5 mg/ml) molecular weight = 397,000, (b) LFR560 (2.5 mg/ml) molecular weight = 34,700, (c) SF200 (2.5 mg/ml) molecular weight = 387,000.

Mentions: In the control alginate solution the samples showed behaviour typical of a pH dependent gel with specific viscosity increasing at lower pH's as an acid gel was formed. Addition of BSA or casein to the mixture caused a visible precipitate to form in samples titrated to acidic pH, but not in samples at neutral pH. From the pH dependent specific viscosity plot of H120L and BSA/Casein in Fig. 3a, at a pH around neutral there was little or no difference in viscosity of supernatant with the addition of BSA or casein. However in the samples with BSA and casein present, at lower pHs the viscosity of the supernatant approached zero as a precipitate had formed between alginate and the protein which has settled to the bottom of the tube, bringing the viscous alginate component out of solution.


Alginate as a protease inhibitor in vitro and in a model gut system; selective inhibition of pepsin but not trypsin.

Chater PI, Wilcox MD, Brownlee IA, Pearson JP - Carbohydr Polym (2015)

(a–c) pH dependent viscosity interaction of alginates with BSA (10 mg/ml) and casein (10 mg/ml) across the pH range (n = 3). (a) H120L (2.5 mg/ml) molecular weight = 397,000, (b) LFR560 (2.5 mg/ml) molecular weight = 34,700, (c) SF200 (2.5 mg/ml) molecular weight = 387,000.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4539341&req=5

fig0015: (a–c) pH dependent viscosity interaction of alginates with BSA (10 mg/ml) and casein (10 mg/ml) across the pH range (n = 3). (a) H120L (2.5 mg/ml) molecular weight = 397,000, (b) LFR560 (2.5 mg/ml) molecular weight = 34,700, (c) SF200 (2.5 mg/ml) molecular weight = 387,000.
Mentions: In the control alginate solution the samples showed behaviour typical of a pH dependent gel with specific viscosity increasing at lower pH's as an acid gel was formed. Addition of BSA or casein to the mixture caused a visible precipitate to form in samples titrated to acidic pH, but not in samples at neutral pH. From the pH dependent specific viscosity plot of H120L and BSA/Casein in Fig. 3a, at a pH around neutral there was little or no difference in viscosity of supernatant with the addition of BSA or casein. However in the samples with BSA and casein present, at lower pHs the viscosity of the supernatant approached zero as a precipitate had formed between alginate and the protein which has settled to the bottom of the tube, bringing the viscous alginate component out of solution.

Bottom Line: Alginates were shown to reduce pepsin activity by up to 53.9% (±9.5SD) in vitro.Limited inhibition of trypsin was shown.Significant inhibition of proteolysis was shown in the gastric phase of digestion, but not the small intestinal phase.

View Article: PubMed Central - PubMed

Affiliation: Institute for Cell and Molecular Biosciences (ICaMB), Medical School, Newcastle University, Catherine Cookson Building, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom. Electronic address: peter.chater@ncl.ac.uk.

No MeSH data available.


Related in: MedlinePlus