Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides

Research output: Contribution to journalJournal articlepeer-review

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Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides. / Zhang, Yuhao; Olsen, Karsten; Grossi, Alberto Blak; Otte, Jeanette Anita Held.

In: Food Chemistry, Vol. 141, No. 3, 2013, p. 2343-2354.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Zhang, Y, Olsen, K, Grossi, AB & Otte, JAH 2013, 'Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides', Food Chemistry, vol. 141, no. 3, pp. 2343-2354. https://doi.org/10.1016/j.foodchem.2013.05.058

APA

Zhang, Y., Olsen, K., Grossi, A. B., & Otte, J. A. H. (2013). Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides. Food Chemistry, 141(3), 2343-2354. https://doi.org/10.1016/j.foodchem.2013.05.058

Vancouver

Zhang Y, Olsen K, Grossi AB, Otte JAH. Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides. Food Chemistry. 2013;141(3):2343-2354. https://doi.org/10.1016/j.foodchem.2013.05.058

Author

Zhang, Yuhao ; Olsen, Karsten ; Grossi, Alberto Blak ; Otte, Jeanette Anita Held. / Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides. In: Food Chemistry. 2013 ; Vol. 141, No. 3. pp. 2343-2354.

Bibtex

@article{ff1bac5f090b442799614f9011dc08b6,
title = "Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides",
abstract = "Bovine collagen was pre-treated (boiled or high pressure (HP)-treated) and then hydrolysed by 6 proteases. The degree of hydrolysis (DH) and the angiotensin-converting enzyme (ACE)-inhibitory activity of hydrolysates were measured. All enzymes used were able to partly degrade collagen and release ACEinhibitory peptides. The highest ACE-inhibitory activity was obtained with Alcalase. Pretreatment significantly influenced the DH and ACE-inhibition. For most enzymes, boiling for 5 min resulted in a significantly higher DH and ACE-inhibitory activity. With Alcalase and collagenase, hydrolysis and release of ACE-inhibitory peptides occurred without any pretreatment, but HP-treatment significantly improved the DH and ACE-inhibitory activity. HP did not markedly affect the hydrolysis with the other enzymes. The major peptides obtained with Alcalase were identified; all were released from the triple helix structure of collagen. Many of these peptides had C-terminal sequences similar to known ACE-inhibitory peptides. The present results suggest that collagen-rich food materials are good substrates for the release of potent ACE-inhibitory peptides, when proper pre-treatment and enzymatic treatment is applied.",
author = "Yuhao Zhang and Karsten Olsen and Grossi, {Alberto Blak} and Otte, {Jeanette Anita Held}",
year = "2013",
doi = "10.1016/j.foodchem.2013.05.058",
language = "English",
volume = "141",
pages = "2343--2354",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides

AU - Zhang, Yuhao

AU - Olsen, Karsten

AU - Grossi, Alberto Blak

AU - Otte, Jeanette Anita Held

PY - 2013

Y1 - 2013

N2 - Bovine collagen was pre-treated (boiled or high pressure (HP)-treated) and then hydrolysed by 6 proteases. The degree of hydrolysis (DH) and the angiotensin-converting enzyme (ACE)-inhibitory activity of hydrolysates were measured. All enzymes used were able to partly degrade collagen and release ACEinhibitory peptides. The highest ACE-inhibitory activity was obtained with Alcalase. Pretreatment significantly influenced the DH and ACE-inhibition. For most enzymes, boiling for 5 min resulted in a significantly higher DH and ACE-inhibitory activity. With Alcalase and collagenase, hydrolysis and release of ACE-inhibitory peptides occurred without any pretreatment, but HP-treatment significantly improved the DH and ACE-inhibitory activity. HP did not markedly affect the hydrolysis with the other enzymes. The major peptides obtained with Alcalase were identified; all were released from the triple helix structure of collagen. Many of these peptides had C-terminal sequences similar to known ACE-inhibitory peptides. The present results suggest that collagen-rich food materials are good substrates for the release of potent ACE-inhibitory peptides, when proper pre-treatment and enzymatic treatment is applied.

AB - Bovine collagen was pre-treated (boiled or high pressure (HP)-treated) and then hydrolysed by 6 proteases. The degree of hydrolysis (DH) and the angiotensin-converting enzyme (ACE)-inhibitory activity of hydrolysates were measured. All enzymes used were able to partly degrade collagen and release ACEinhibitory peptides. The highest ACE-inhibitory activity was obtained with Alcalase. Pretreatment significantly influenced the DH and ACE-inhibition. For most enzymes, boiling for 5 min resulted in a significantly higher DH and ACE-inhibitory activity. With Alcalase and collagenase, hydrolysis and release of ACE-inhibitory peptides occurred without any pretreatment, but HP-treatment significantly improved the DH and ACE-inhibitory activity. HP did not markedly affect the hydrolysis with the other enzymes. The major peptides obtained with Alcalase were identified; all were released from the triple helix structure of collagen. Many of these peptides had C-terminal sequences similar to known ACE-inhibitory peptides. The present results suggest that collagen-rich food materials are good substrates for the release of potent ACE-inhibitory peptides, when proper pre-treatment and enzymatic treatment is applied.

U2 - 10.1016/j.foodchem.2013.05.058

DO - 10.1016/j.foodchem.2013.05.058

M3 - Journal article

C2 - 23870967

VL - 141

SP - 2343

EP - 2354

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

IS - 3

ER -

ID: 46254752