Enzymatic production of protein hydrolysates from steelhead (Oncorhynchus mykiss) skin gelatin as inhibitors of dipeptidyl-peptidase IV and angiotensin-I converting enzyme. (January 2017)
- Record Type:
- Journal Article
- Title:
- Enzymatic production of protein hydrolysates from steelhead (Oncorhynchus mykiss) skin gelatin as inhibitors of dipeptidyl-peptidase IV and angiotensin-I converting enzyme. (January 2017)
- Main Title:
- Enzymatic production of protein hydrolysates from steelhead (Oncorhynchus mykiss) skin gelatin as inhibitors of dipeptidyl-peptidase IV and angiotensin-I converting enzyme
- Authors:
- Cheung, Imelda W.Y.
Li-Chan, Eunice C.Y. - Abstract:
- Highlights: Gelatin hydrolysates with ACE and DPP-IV inhibitory activity were produced. Bioactivity was enhanced by either ultrafiltration or sequential enzyme hydrolysis. The <3 kDa fraction of hydrolysates produced by pepsin, Corolase®N or papain showed strong ACE and DPP-IV inhibition. ACE inhibitory activity of some hydrolysates improved after second hydrolysis with CorolaseN. Hydrolysis with papain followed by either ultrafiltration or CorolaseN yielded strong dual bioactivity. Abstract: The objective of this study was to generate protein hydrolysates with dual in vitro inhibitory activities against dipeptidyl-peptidase IV (DPP-IV) and angiotensin-I converting enzyme (ACE), by proteolytic enzymes acting either individually or sequentially on steelhead skin gelatin. The results showed strong dual bioactivity in the low molecular weight (<3 kDa) fractions obtained by ultrafiltration of hydrolysates produced using the enzymes pepsin, CorolaseN or papain. Alternatively, unfractionated hydrolysates exhibiting high ACE and DPP-IV inhibitory activities as well as yields could be attained by strategic selection of two enzymes for successive hydrolysis of gelatin. In particular, hydrolysates produced using 4% papain for 2 h followed either by ultrafiltration or by a second hydrolysis with 1% CorolaseN for 2 h, presented potent dual activity as ACE and DPP-IV inhibitors, and should be investigated further as potential functional food ingredients or nutraceuticals for theHighlights: Gelatin hydrolysates with ACE and DPP-IV inhibitory activity were produced. Bioactivity was enhanced by either ultrafiltration or sequential enzyme hydrolysis. The <3 kDa fraction of hydrolysates produced by pepsin, Corolase®N or papain showed strong ACE and DPP-IV inhibition. ACE inhibitory activity of some hydrolysates improved after second hydrolysis with CorolaseN. Hydrolysis with papain followed by either ultrafiltration or CorolaseN yielded strong dual bioactivity. Abstract: The objective of this study was to generate protein hydrolysates with dual in vitro inhibitory activities against dipeptidyl-peptidase IV (DPP-IV) and angiotensin-I converting enzyme (ACE), by proteolytic enzymes acting either individually or sequentially on steelhead skin gelatin. The results showed strong dual bioactivity in the low molecular weight (<3 kDa) fractions obtained by ultrafiltration of hydrolysates produced using the enzymes pepsin, CorolaseN or papain. Alternatively, unfractionated hydrolysates exhibiting high ACE and DPP-IV inhibitory activities as well as yields could be attained by strategic selection of two enzymes for successive hydrolysis of gelatin. In particular, hydrolysates produced using 4% papain for 2 h followed either by ultrafiltration or by a second hydrolysis with 1% CorolaseN for 2 h, presented potent dual activity as ACE and DPP-IV inhibitors, and should be investigated further as potential functional food ingredients or nutraceuticals for the management of hypertension and diabetes. … (more)
- Is Part Of:
- Journal of functional foods. Volume 28(2017)
- Journal:
- Journal of functional foods
- Issue:
- Volume 28(2017)
- Issue Display:
- Volume 28, Issue 2017 (2017)
- Year:
- 2017
- Volume:
- 28
- Issue:
- 2017
- Issue Sort Value:
- 2017-0028-2017-0000
- Page Start:
- 254
- Page End:
- 264
- Publication Date:
- 2017-01
- Subjects:
- Gelatin hydrolysate -- Enzymatic hydrolysis -- Dipeptidyl-peptidase IV inhibitory activity -- Angiotensin-I converting enzyme inhibitory activity -- Ultrafiltration
Functional foods -- Analysis -- Periodicals
Food -- Biotechnology -- Periodicals
Nutrition -- Periodicals
613.2 - Journal URLs:
- http://www.sciencedirect.com/science/journal/17564646 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.jff.2016.10.030 ↗
- Languages:
- English
- ISSNs:
- 1756-4646
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4986.807000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2487.xml