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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

Correlation of alginate structural patterns; (a) F[M], (b) F[GG], (c) F[GGG], (d) F[MM], (e) F[MGM], and (f) n(G > 1) the G-block length against level of pepsin inhibition with 5 mg/ml alginate. Pepsin activity is shown as a percentage of control pepsin activity. The error bars show the standard deviation of six replicates (n = 6).
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fig0010: Correlation of alginate structural patterns; (a) F[M], (b) F[GG], (c) F[GGG], (d) F[MM], (e) F[MGM], and (f) n(G > 1) the G-block length against level of pepsin inhibition with 5 mg/ml alginate. Pepsin activity is shown as a percentage of control pepsin activity. The error bars show the standard deviation of six replicates (n = 6).

Mentions: The structure and biophysical properties of alginates are not just dictated by F[G] frequency, but also by the arrangement of contiguous blocks of M and G residues. Levels of pepsin inhibition were compared against the frequency of the structural patterns; F[M], F[GG], F[MM], F[GGG], F[MGM] and F[GM/MG] and also against n(G > 1), the G-block length (Fig. 2). Similar significant relationships between structure and inhibition were observed, where higher levels of mannuronic acid brought about significantly higher levels of pepsin inhibition. As the G-block length increases, a significant reduction in the inhibition of pepsin was observed, showing a negative correlation between inhibition and n(G > 1).


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)

Correlation of alginate structural patterns; (a) F[M], (b) F[GG], (c) F[GGG], (d) F[MM], (e) F[MGM], and (f) n(G > 1) the G-block length against level of pepsin inhibition with 5 mg/ml alginate. Pepsin activity is shown as a percentage of control pepsin activity. The error bars show the standard deviation of six replicates (n = 6).
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

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

fig0010: Correlation of alginate structural patterns; (a) F[M], (b) F[GG], (c) F[GGG], (d) F[MM], (e) F[MGM], and (f) n(G > 1) the G-block length against level of pepsin inhibition with 5 mg/ml alginate. Pepsin activity is shown as a percentage of control pepsin activity. The error bars show the standard deviation of six replicates (n = 6).
Mentions: The structure and biophysical properties of alginates are not just dictated by F[G] frequency, but also by the arrangement of contiguous blocks of M and G residues. Levels of pepsin inhibition were compared against the frequency of the structural patterns; F[M], F[GG], F[MM], F[GGG], F[MGM] and F[GM/MG] and also against n(G > 1), the G-block length (Fig. 2). Similar significant relationships between structure and inhibition were observed, where higher levels of mannuronic acid brought about significantly higher levels of pepsin inhibition. As the G-block length increases, a significant reduction in the inhibition of pepsin was observed, showing a negative correlation between inhibition and n(G > 1).

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