Hydrolysis of Whey Protein Isolate with Bacillus licheniformis Protease: Aggregating Capacities of Peptide Fractions

N.P. Creusot, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

20 Citations (Scopus)

Abstract

In a previous study, peptides aggregating at pH 7.0 derived from a whey protein hydrolysate made with Bacillus licheniformis protease were fractionated and identified. The objective of the present work was to investigate the solubility of the fractionated aggregating pepticles, as a function of concentration, and their aggregating capacities toward added intact proteins. The amount of aggregated material and the composition of the aggregates obtained were measured by nitrogen concentration and size exclusion chromatography, respectively. The results showed that of the four fractions obtained from the aggregating pepticles, two were insoluble, while the other two consisted of 1:1 mixture of low and high solubility pepticles. Therefore, insoluble pepticles coaggregated, assumedly via hydrophobic interactions, other relatively more soluble pepticles. It was also shown that aggregating pepticles could aggregate intact protein nonspecifically since the same peptides were involved in the aggregation of whey proteins, beta-casein, and bovine serum albumin. Both insoluble and partly insoluble pepticles were required for the aggregation of intact protein. These results are of interest for the applications of protein hydrolysates, as mixtures of intact protein and pepticles are often present in these applications.
LanguageEnglish
Pages10332-10339
JournalJournal of Agricultural and Food Chemistry
Volume56
Issue number21
DOIs
Publication statusPublished - 2008

Fingerprint

Bacillus licheniformis
whey protein isolate
Bacilli
Protein Hydrolysates
Hydrolysis
Peptide Hydrolases
proteinases
hydrolysis
protein hydrolysates
protein aggregates
peptides
whey protein
Solubility
Peptides
solubility
Proteins
Agglomeration
proteins
hydrophobic bonding
beta-casein

Keywords

  • beta-lactoglobulin
  • milk-proteins
  • identification
  • mixtures
  • glu

Cite this

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title = "Hydrolysis of Whey Protein Isolate with Bacillus licheniformis Protease: Aggregating Capacities of Peptide Fractions",
abstract = "In a previous study, peptides aggregating at pH 7.0 derived from a whey protein hydrolysate made with Bacillus licheniformis protease were fractionated and identified. The objective of the present work was to investigate the solubility of the fractionated aggregating pepticles, as a function of concentration, and their aggregating capacities toward added intact proteins. The amount of aggregated material and the composition of the aggregates obtained were measured by nitrogen concentration and size exclusion chromatography, respectively. The results showed that of the four fractions obtained from the aggregating pepticles, two were insoluble, while the other two consisted of 1:1 mixture of low and high solubility pepticles. Therefore, insoluble pepticles coaggregated, assumedly via hydrophobic interactions, other relatively more soluble pepticles. It was also shown that aggregating pepticles could aggregate intact protein nonspecifically since the same peptides were involved in the aggregation of whey proteins, beta-casein, and bovine serum albumin. Both insoluble and partly insoluble pepticles were required for the aggregation of intact protein. These results are of interest for the applications of protein hydrolysates, as mixtures of intact protein and pepticles are often present in these applications.",
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Hydrolysis of Whey Protein Isolate with Bacillus licheniformis Protease: Aggregating Capacities of Peptide Fractions. / Creusot, N.P.; Gruppen, H.

In: Journal of Agricultural and Food Chemistry, Vol. 56, No. 21, 2008, p. 10332-10339.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Creusot, N.P.

AU - Gruppen, H.

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PY - 2008

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N2 - In a previous study, peptides aggregating at pH 7.0 derived from a whey protein hydrolysate made with Bacillus licheniformis protease were fractionated and identified. The objective of the present work was to investigate the solubility of the fractionated aggregating pepticles, as a function of concentration, and their aggregating capacities toward added intact proteins. The amount of aggregated material and the composition of the aggregates obtained were measured by nitrogen concentration and size exclusion chromatography, respectively. The results showed that of the four fractions obtained from the aggregating pepticles, two were insoluble, while the other two consisted of 1:1 mixture of low and high solubility pepticles. Therefore, insoluble pepticles coaggregated, assumedly via hydrophobic interactions, other relatively more soluble pepticles. It was also shown that aggregating pepticles could aggregate intact protein nonspecifically since the same peptides were involved in the aggregation of whey proteins, beta-casein, and bovine serum albumin. Both insoluble and partly insoluble pepticles were required for the aggregation of intact protein. These results are of interest for the applications of protein hydrolysates, as mixtures of intact protein and pepticles are often present in these applications.

AB - In a previous study, peptides aggregating at pH 7.0 derived from a whey protein hydrolysate made with Bacillus licheniformis protease were fractionated and identified. The objective of the present work was to investigate the solubility of the fractionated aggregating pepticles, as a function of concentration, and their aggregating capacities toward added intact proteins. The amount of aggregated material and the composition of the aggregates obtained were measured by nitrogen concentration and size exclusion chromatography, respectively. The results showed that of the four fractions obtained from the aggregating pepticles, two were insoluble, while the other two consisted of 1:1 mixture of low and high solubility pepticles. Therefore, insoluble pepticles coaggregated, assumedly via hydrophobic interactions, other relatively more soluble pepticles. It was also shown that aggregating pepticles could aggregate intact protein nonspecifically since the same peptides were involved in the aggregation of whey proteins, beta-casein, and bovine serum albumin. Both insoluble and partly insoluble pepticles were required for the aggregation of intact protein. These results are of interest for the applications of protein hydrolysates, as mixtures of intact protein and pepticles are often present in these applications.

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