β-Lactoglobulin/polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of different molecular weight cut-offs

The effects of gum arabic, low methylated (LM) pectin or xylan at levels of 0 and 50 wt.% on beta-lactoglobulin (β-lg) digestibility were studied as well as the interactions between the two macromolecules during in vitro hydrolysis. The proteolysis was performed in a system involving a two-step hydr...

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Veröffentlicht in:Biochimica et biophysica acta 2004-01, Vol.1670 (2), p.105-112
Hauptverfasser: Mou.écoucou, J, Villaume, C, Sanchez, C, Méjean, L
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Villaume, C
Sanchez, C
Méjean, L
description The effects of gum arabic, low methylated (LM) pectin or xylan at levels of 0 and 50 wt.% on beta-lactoglobulin (β-lg) digestibility were studied as well as the interactions between the two macromolecules during in vitro hydrolysis. The proteolysis was performed in a system involving a two-step hydrolysis: either pepsin alone, or pepsin followed by a trypsin/chymotrypsin (T/C) mixture in dialysis bags with molecular weight cut-offs (MWCO) 1000 or 8000 Da. Digestibility was estimated by the N release and by a SDS-PAGE electrophoresis of retentates from the two dialysis bags after hydrolysis. Turbidimetric measurements monitored the structural evolution of mixtures during the two-step hydrolysis. Results showed that β-lg was almost resistant to peptic digestion and that polysaccharides increased the N release despite a reduction of pepsin activity. This is due to the formation of electrostatic complexes between polysaccharides and β-lg, which reduced β-lg aggregation, increasing its solubility. The polysaccharides reduced significantly the β-lg T/C digestibility as determined using a dialysis bag with a MWCO 1000 Da, without a modification of their enzymatic activities. No significant effect of polysaccharides on the β-lg digestibility was detected using the dialysis bag with a MWCO 8000 Da. The electrophoresis pattern did not show differences in the profile of retentates in relation with the dialysis bag used. This suggests that non-specific interactions could occur during the second step of hydrolysis between polysaccharides and amino acids or peptides smaller than 8000 Da.
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The proteolysis was performed in a system involving a two-step hydrolysis: either pepsin alone, or pepsin followed by a trypsin/chymotrypsin (T/C) mixture in dialysis bags with molecular weight cut-offs (MWCO) 1000 or 8000 Da. Digestibility was estimated by the N release and by a SDS-PAGE electrophoresis of retentates from the two dialysis bags after hydrolysis. Turbidimetric measurements monitored the structural evolution of mixtures during the two-step hydrolysis. Results showed that β-lg was almost resistant to peptic digestion and that polysaccharides increased the N release despite a reduction of pepsin activity. This is due to the formation of electrostatic complexes between polysaccharides and β-lg, which reduced β-lg aggregation, increasing its solubility. The polysaccharides reduced significantly the β-lg T/C digestibility as determined using a dialysis bag with a MWCO 1000 Da, without a modification of their enzymatic activities. No significant effect of polysaccharides on the β-lg digestibility was detected using the dialysis bag with a MWCO 8000 Da. The electrophoresis pattern did not show differences in the profile of retentates in relation with the dialysis bag used. This suggests that non-specific interactions could occur during the second step of hydrolysis between polysaccharides and amino acids or peptides smaller than 8000 Da.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>14738992</pmid><doi>10.1016/j.bbagen.2003.10.017</doi><tpages>8</tpages></addata></record>
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subjects Beta-lactoglobulin/polysaccharide interaction
Chymotrypsin
Computer Science
Dialysis
Digestion
Electrophoresis, Polyacrylamide Gel
Enzymatic activity
Food Additives - chemistry
Food Additives - pharmacology
Gum Arabic - pharmacology
Humans
Hydrogen-Ion Concentration
Hydrolysis
In Vitro Techniques
Lactoglobulins - chemistry
Lactoglobulins - metabolism
Life Sciences
N release
Nephelometry and Turbidimetry
Nitrogen - chemistry
Pectins - pharmacology
Pepsin A
Polysaccharides - chemistry
Polysaccharides - pharmacology
Trypsin
Turbidity
Xylans - pharmacology
title β-Lactoglobulin/polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of different molecular weight cut-offs
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