Enhancement of angiotensin I converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of corn gluten hydrolysate using ultrafiltration membranes

Jin Man Kim, Jong Hyun Whang, Hyung Joo Suh

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29 Citations (Scopus)

Abstract

In this study, we attempted to enhance angiotensin I converting enzyme (ACE) inhibitory activity using an ultrafiltration (UF) membrane and to improve the emulsifying and foaming properties of fractions. ACE inhibitory activities of the corn gluten hydrolysate prepared by Flavourzyme had the same trend as protein contents and the IC50 value was 0.18 mg solid after 8 h hydrolysis. The hydrolysate was separated by using two kinds of UF membrane (10 and 5 kDa cut-off membranes) and three fractions, >10 kDa, 5-10 kDa, and <5 kDa, were obtained. The yields of these three fractions were 58.3%, 27.2% and 14.5% as dry matter, respectively. The IC50 value (the concentration of ACE inhibitor required to inhibit 50% of the ACE activity under specific conditions) of the <5 kDa fraction was 0.05 mg solid and was approximately fourfold that of the original, 5-10, and >10 kDa fractions. The average hydrophobicity of the <5 kDa fraction was slightly lower than that of the others according to the hydrophobicity index of Nozaki and Tanford, but according to the Krigbaum and Meirovitch index, that of the <5 kDa fraction was slightly higher than those of the others, showing there might be no significant differences among the fractions. The emulsifying activity and emulsion stability in the <5 kDa fraction was higher than those in the other fractions. Two fractions, <5 kDa and >10 kDa, showed poor foaming capacity at below pH 6.0. The foam stabilities of two fractions (<5 kDa and >10 kDa) increased with increasing pH, but that of 5-10 kDa decreased with increasing pH. The UF treatment was an effective method for the enhancement of ACE inhibitory activity with improvement of functional properties.

Original languageEnglish
Pages (from-to)133-138
Number of pages6
JournalEuropean Food Research and Technology
Volume218
Issue number2
DOIs
Publication statusPublished - 2004 Jan 1

Fingerprint

corn gluten
foaming properties
emulsifying properties
Glutens
peptidyl-dipeptidase A
Ultrafiltration
Enzyme activity
Peptidyl-Dipeptidase A
ultrafiltration
hydrolysates
Zea mays
Membranes
foaming capacity
Hydrophobicity
foams
hydrophobicity
Hydrophobic and Hydrophilic Interactions
Inhibitory Concentration 50
functional properties
inhibitory concentration 50

Keywords

  • Angiotensin I converting enzyme
  • Corn gluten
  • Emulsifying and foaming properties
  • Flavourzyme

ASJC Scopus subject areas

  • Food Science

Cite this

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title = "Enhancement of angiotensin I converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of corn gluten hydrolysate using ultrafiltration membranes",
abstract = "In this study, we attempted to enhance angiotensin I converting enzyme (ACE) inhibitory activity using an ultrafiltration (UF) membrane and to improve the emulsifying and foaming properties of fractions. ACE inhibitory activities of the corn gluten hydrolysate prepared by Flavourzyme had the same trend as protein contents and the IC50 value was 0.18 mg solid after 8 h hydrolysis. The hydrolysate was separated by using two kinds of UF membrane (10 and 5 kDa cut-off membranes) and three fractions, >10 kDa, 5-10 kDa, and <5 kDa, were obtained. The yields of these three fractions were 58.3{\%}, 27.2{\%} and 14.5{\%} as dry matter, respectively. The IC50 value (the concentration of ACE inhibitor required to inhibit 50{\%} of the ACE activity under specific conditions) of the <5 kDa fraction was 0.05 mg solid and was approximately fourfold that of the original, 5-10, and >10 kDa fractions. The average hydrophobicity of the <5 kDa fraction was slightly lower than that of the others according to the hydrophobicity index of Nozaki and Tanford, but according to the Krigbaum and Meirovitch index, that of the <5 kDa fraction was slightly higher than those of the others, showing there might be no significant differences among the fractions. The emulsifying activity and emulsion stability in the <5 kDa fraction was higher than those in the other fractions. Two fractions, <5 kDa and >10 kDa, showed poor foaming capacity at below pH 6.0. The foam stabilities of two fractions (<5 kDa and >10 kDa) increased with increasing pH, but that of 5-10 kDa decreased with increasing pH. The UF treatment was an effective method for the enhancement of ACE inhibitory activity with improvement of functional properties.",
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N2 - In this study, we attempted to enhance angiotensin I converting enzyme (ACE) inhibitory activity using an ultrafiltration (UF) membrane and to improve the emulsifying and foaming properties of fractions. ACE inhibitory activities of the corn gluten hydrolysate prepared by Flavourzyme had the same trend as protein contents and the IC50 value was 0.18 mg solid after 8 h hydrolysis. The hydrolysate was separated by using two kinds of UF membrane (10 and 5 kDa cut-off membranes) and three fractions, >10 kDa, 5-10 kDa, and <5 kDa, were obtained. The yields of these three fractions were 58.3%, 27.2% and 14.5% as dry matter, respectively. The IC50 value (the concentration of ACE inhibitor required to inhibit 50% of the ACE activity under specific conditions) of the <5 kDa fraction was 0.05 mg solid and was approximately fourfold that of the original, 5-10, and >10 kDa fractions. The average hydrophobicity of the <5 kDa fraction was slightly lower than that of the others according to the hydrophobicity index of Nozaki and Tanford, but according to the Krigbaum and Meirovitch index, that of the <5 kDa fraction was slightly higher than those of the others, showing there might be no significant differences among the fractions. The emulsifying activity and emulsion stability in the <5 kDa fraction was higher than those in the other fractions. Two fractions, <5 kDa and >10 kDa, showed poor foaming capacity at below pH 6.0. The foam stabilities of two fractions (<5 kDa and >10 kDa) increased with increasing pH, but that of 5-10 kDa decreased with increasing pH. The UF treatment was an effective method for the enhancement of ACE inhibitory activity with improvement of functional properties.

AB - In this study, we attempted to enhance angiotensin I converting enzyme (ACE) inhibitory activity using an ultrafiltration (UF) membrane and to improve the emulsifying and foaming properties of fractions. ACE inhibitory activities of the corn gluten hydrolysate prepared by Flavourzyme had the same trend as protein contents and the IC50 value was 0.18 mg solid after 8 h hydrolysis. The hydrolysate was separated by using two kinds of UF membrane (10 and 5 kDa cut-off membranes) and three fractions, >10 kDa, 5-10 kDa, and <5 kDa, were obtained. The yields of these three fractions were 58.3%, 27.2% and 14.5% as dry matter, respectively. The IC50 value (the concentration of ACE inhibitor required to inhibit 50% of the ACE activity under specific conditions) of the <5 kDa fraction was 0.05 mg solid and was approximately fourfold that of the original, 5-10, and >10 kDa fractions. The average hydrophobicity of the <5 kDa fraction was slightly lower than that of the others according to the hydrophobicity index of Nozaki and Tanford, but according to the Krigbaum and Meirovitch index, that of the <5 kDa fraction was slightly higher than those of the others, showing there might be no significant differences among the fractions. The emulsifying activity and emulsion stability in the <5 kDa fraction was higher than those in the other fractions. Two fractions, <5 kDa and >10 kDa, showed poor foaming capacity at below pH 6.0. The foam stabilities of two fractions (<5 kDa and >10 kDa) increased with increasing pH, but that of 5-10 kDa decreased with increasing pH. The UF treatment was an effective method for the enhancement of ACE inhibitory activity with improvement of functional properties.

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