Comparison of bioactive peptides prepared from sheep cheese whey using a food‐grade bacterial and a fungal protease preparation

Summary Novel bacterial (HT) and fungal (FPII) food‐grade protease preparations were evaluated for their ability to hydrolyse sheep cheese whey (SCW) and the generation of bioactive peptides. Both protease preparations hydrolysed the whey proteins to small peptides over 24‐h hydrolysis time, but the...

Full description

Saved in:
Bibliographic Details
Published in:International journal of food science & technology 2017-05, Vol.52 (5), p.1252-1259
Main Authors: Welsh, Grace, Ryder, Kate, Brewster, Jodi, Walker, Christina, Mros, Sonya, Bekhit, Alaa El‐Din A., McConnell, Michelle, Carne, Alan
Format: Article
Language:English
Subjects:
Angiotensin‐I converting enzyme‐inhibitor
antioxidant
Bacteria
bioactive
Biocompatibility
Cheese
Hydrolysates
Peptides
Protease
Sheep
sheep cheese whey
Whey
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3
cites cdi_FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3
container_end_page 1259
container_issue 5
container_start_page 1252
container_title International journal of food science & technology
container_volume 52
creator Welsh, Grace
Ryder, Kate
Brewster, Jodi
Walker, Christina
Mros, Sonya
Bekhit, Alaa El‐Din A.
McConnell, Michelle
Carne, Alan
description Summary Novel bacterial (HT) and fungal (FPII) food‐grade protease preparations were evaluated for their ability to hydrolyse sheep cheese whey (SCW) and the generation of bioactive peptides. Both protease preparations hydrolysed the whey proteins to small peptides over 24‐h hydrolysis time, but the time course hydrolysis profiles were different as evaluated by SDS‐PAGE. The HT whey hydrolysate had considerably higher antioxidant and angiotensin‐I converting enzyme (ACE)‐inhibitor activity than the FPII hydrolysate. Neither hydrolysate was cytotoxic towards Vero cells. OFFGEL electrophoresis of the small peptide pool fraction (
doi_str_mv 10.1111/ijfs.13392
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1904224499</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1891884135</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3</originalsourceid><addsrcrecordid>eNqF0ctKxDAUBuAgCo6jG58g4EaEam5tk6UMXhFcqOuSpqczGTpNTVpldvoGPqNPYsa6cqFZJIR850_CQeiQklMax5ld1uGUcq7YFppQnqUJyxjdRhOiUpKkgvFdtBfCkhDCeC4m6H3mVp32NrgWuxqX1mnT2xfAHXS9rSDgzkMEUOHauxUOC4AOmzgHwK8LWOMh2HaONa6dqz7fPuZeV4DLmALe6gbrttocDu08bjrvetCxcgzVvXXtPtqpdRPg4GedoqfLi8fZdXJ3f3UzO79LjCCCJZSAAmFyTbmGTADTTLCcm1pkBnKT15limUzLFHJaVYarqgTFZWnSXEnNSj5Fx2NufMTzAKEvVjYYaBrdghtCQVW8hgmh1P9UKiqloDyN9OgXXbrBt_EjUUmZESKZjOpkVMa7EDzUReftSvt1QUmxaVyxaVzx3biI6YhfbQPrP2Rxc3v5MNZ8AZB-nU8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1888600828</pqid></control><display><type>article</type><title>Comparison of bioactive peptides prepared from sheep cheese whey using a food‐grade bacterial and a fungal protease preparation</title><source>Wiley</source><source>Oxford University Press Open Access</source><creator>Welsh, Grace ; Ryder, Kate ; Brewster, Jodi ; Walker, Christina ; Mros, Sonya ; Bekhit, Alaa El‐Din A. ; McConnell, Michelle ; Carne, Alan</creator><creatorcontrib>Welsh, Grace ; Ryder, Kate ; Brewster, Jodi ; Walker, Christina ; Mros, Sonya ; Bekhit, Alaa El‐Din A. ; McConnell, Michelle ; Carne, Alan</creatorcontrib><description>Summary Novel bacterial (HT) and fungal (FPII) food‐grade protease preparations were evaluated for their ability to hydrolyse sheep cheese whey (SCW) and the generation of bioactive peptides. Both protease preparations hydrolysed the whey proteins to small peptides over 24‐h hydrolysis time, but the time course hydrolysis profiles were different as evaluated by SDS‐PAGE. The HT whey hydrolysate had considerably higher antioxidant and angiotensin‐I converting enzyme (ACE)‐inhibitor activity than the FPII hydrolysate. Neither hydrolysate was cytotoxic towards Vero cells. OFFGEL electrophoresis of the small peptide pool fraction (&lt;15 amino acids) of each hydrolysate indicated differences in the pI distribution of the bioactive peptides. This likely reflects the diverse hydrolytic specificity of the proteases. Although the antioxidant activity of both hydrolysates was not significantly affected by simulated gastrointestinal digestion, the loss of ACE‐inhibitor activity was greater with the FPII hydrolysate. Workflow for preparation and analysis of sheep cheese whey hydrolysates.</description><identifier>ISSN: 0950-5423</identifier><identifier>EISSN: 1365-2621</identifier><identifier>DOI: 10.1111/ijfs.13392</identifier><language>eng</language><publisher>Oxford: Wiley Subscription Services, Inc</publisher><subject>Angiotensin‐I converting enzyme‐inhibitor ; antioxidant ; Bacteria ; bioactive ; Biocompatibility ; Cheese ; Hydrolysates ; Peptides ; Protease ; Sheep ; sheep cheese whey ; Whey</subject><ispartof>International journal of food science &amp; technology, 2017-05, Vol.52 (5), p.1252-1259</ispartof><rights>2017 Institute of Food Science and Technology</rights><rights>International Journal of Food Science and Technology © 2017 Institute of Food Science and Technology</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3</citedby><cites>FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids></links><search><creatorcontrib>Welsh, Grace</creatorcontrib><creatorcontrib>Ryder, Kate</creatorcontrib><creatorcontrib>Brewster, Jodi</creatorcontrib><creatorcontrib>Walker, Christina</creatorcontrib><creatorcontrib>Mros, Sonya</creatorcontrib><creatorcontrib>Bekhit, Alaa El‐Din A.</creatorcontrib><creatorcontrib>McConnell, Michelle</creatorcontrib><creatorcontrib>Carne, Alan</creatorcontrib><title>Comparison of bioactive peptides prepared from sheep cheese whey using a food‐grade bacterial and a fungal protease preparation</title><title>International journal of food science &amp; technology</title><description>Summary Novel bacterial (HT) and fungal (FPII) food‐grade protease preparations were evaluated for their ability to hydrolyse sheep cheese whey (SCW) and the generation of bioactive peptides. Both protease preparations hydrolysed the whey proteins to small peptides over 24‐h hydrolysis time, but the time course hydrolysis profiles were different as evaluated by SDS‐PAGE. The HT whey hydrolysate had considerably higher antioxidant and angiotensin‐I converting enzyme (ACE)‐inhibitor activity than the FPII hydrolysate. Neither hydrolysate was cytotoxic towards Vero cells. OFFGEL electrophoresis of the small peptide pool fraction (&lt;15 amino acids) of each hydrolysate indicated differences in the pI distribution of the bioactive peptides. This likely reflects the diverse hydrolytic specificity of the proteases. Although the antioxidant activity of both hydrolysates was not significantly affected by simulated gastrointestinal digestion, the loss of ACE‐inhibitor activity was greater with the FPII hydrolysate. Workflow for preparation and analysis of sheep cheese whey hydrolysates.</description><subject>Angiotensin‐I converting enzyme‐inhibitor</subject><subject>antioxidant</subject><subject>Bacteria</subject><subject>bioactive</subject><subject>Biocompatibility</subject><subject>Cheese</subject><subject>Hydrolysates</subject><subject>Peptides</subject><subject>Protease</subject><subject>Sheep</subject><subject>sheep cheese whey</subject><subject>Whey</subject><issn>0950-5423</issn><issn>1365-2621</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNqF0ctKxDAUBuAgCo6jG58g4EaEam5tk6UMXhFcqOuSpqczGTpNTVpldvoGPqNPYsa6cqFZJIR850_CQeiQklMax5ld1uGUcq7YFppQnqUJyxjdRhOiUpKkgvFdtBfCkhDCeC4m6H3mVp32NrgWuxqX1mnT2xfAHXS9rSDgzkMEUOHauxUOC4AOmzgHwK8LWOMh2HaONa6dqz7fPuZeV4DLmALe6gbrttocDu08bjrvetCxcgzVvXXtPtqpdRPg4GedoqfLi8fZdXJ3f3UzO79LjCCCJZSAAmFyTbmGTADTTLCcm1pkBnKT15limUzLFHJaVYarqgTFZWnSXEnNSj5Fx2NufMTzAKEvVjYYaBrdghtCQVW8hgmh1P9UKiqloDyN9OgXXbrBt_EjUUmZESKZjOpkVMa7EDzUReftSvt1QUmxaVyxaVzx3biI6YhfbQPrP2Rxc3v5MNZ8AZB-nU8</recordid><startdate>201705</startdate><enddate>201705</enddate><creator>Welsh, Grace</creator><creator>Ryder, Kate</creator><creator>Brewster, Jodi</creator><creator>Walker, Christina</creator><creator>Mros, Sonya</creator><creator>Bekhit, Alaa El‐Din A.</creator><creator>McConnell, Michelle</creator><creator>Carne, Alan</creator><general>Wiley Subscription Services, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>SOI</scope><scope>7QL</scope><scope>M7N</scope></search><sort><creationdate>201705</creationdate><title>Comparison of bioactive peptides prepared from sheep cheese whey using a food‐grade bacterial and a fungal protease preparation</title><author>Welsh, Grace ; Ryder, Kate ; Brewster, Jodi ; Walker, Christina ; Mros, Sonya ; Bekhit, Alaa El‐Din A. ; McConnell, Michelle ; Carne, Alan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Angiotensin‐I converting enzyme‐inhibitor</topic><topic>antioxidant</topic><topic>Bacteria</topic><topic>bioactive</topic><topic>Biocompatibility</topic><topic>Cheese</topic><topic>Hydrolysates</topic><topic>Peptides</topic><topic>Protease</topic><topic>Sheep</topic><topic>sheep cheese whey</topic><topic>Whey</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Welsh, Grace</creatorcontrib><creatorcontrib>Ryder, Kate</creatorcontrib><creatorcontrib>Brewster, Jodi</creatorcontrib><creatorcontrib>Walker, Christina</creatorcontrib><creatorcontrib>Mros, Sonya</creatorcontrib><creatorcontrib>Bekhit, Alaa El‐Din A.</creatorcontrib><creatorcontrib>McConnell, Michelle</creatorcontrib><creatorcontrib>Carne, Alan</creatorcontrib><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics &amp; Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology &amp; Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>International journal of food science &amp; technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Welsh, Grace</au><au>Ryder, Kate</au><au>Brewster, Jodi</au><au>Walker, Christina</au><au>Mros, Sonya</au><au>Bekhit, Alaa El‐Din A.</au><au>McConnell, Michelle</au><au>Carne, Alan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of bioactive peptides prepared from sheep cheese whey using a food‐grade bacterial and a fungal protease preparation</atitle><jtitle>International journal of food science &amp; technology</jtitle><date>2017-05</date><risdate>2017</risdate><volume>52</volume><issue>5</issue><spage>1252</spage><epage>1259</epage><pages>1252-1259</pages><issn>0950-5423</issn><eissn>1365-2621</eissn><abstract>Summary Novel bacterial (HT) and fungal (FPII) food‐grade protease preparations were evaluated for their ability to hydrolyse sheep cheese whey (SCW) and the generation of bioactive peptides. Both protease preparations hydrolysed the whey proteins to small peptides over 24‐h hydrolysis time, but the time course hydrolysis profiles were different as evaluated by SDS‐PAGE. The HT whey hydrolysate had considerably higher antioxidant and angiotensin‐I converting enzyme (ACE)‐inhibitor activity than the FPII hydrolysate. Neither hydrolysate was cytotoxic towards Vero cells. OFFGEL electrophoresis of the small peptide pool fraction (&lt;15 amino acids) of each hydrolysate indicated differences in the pI distribution of the bioactive peptides. This likely reflects the diverse hydrolytic specificity of the proteases. Although the antioxidant activity of both hydrolysates was not significantly affected by simulated gastrointestinal digestion, the loss of ACE‐inhibitor activity was greater with the FPII hydrolysate. Workflow for preparation and analysis of sheep cheese whey hydrolysates.</abstract><cop>Oxford</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1111/ijfs.13392</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0950-5423
ispartof International journal of food science & technology, 2017-05, Vol.52 (5), p.1252-1259
issn 0950-5423
1365-2621
language eng
recordid cdi_proquest_miscellaneous_1904224499
source Wiley; Oxford University Press Open Access
subjects Angiotensin‐I converting enzyme‐inhibitor
antioxidant
Bacteria
bioactive
Biocompatibility
Cheese
Hydrolysates
Peptides
Protease
Sheep
sheep cheese whey
Whey
title Comparison of bioactive peptides prepared from sheep cheese whey using a food‐grade bacterial and a fungal protease preparation
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T15%3A32%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Comparison%20of%20bioactive%20peptides%20prepared%20from%20sheep%20cheese%20whey%20using%20a%20food%E2%80%90grade%20bacterial%20and%20a%20fungal%20protease%20preparation&rft.jtitle=International%20journal%20of%20food%20science%20&%20technology&rft.au=Welsh,%20Grace&rft.date=2017-05&rft.volume=52&rft.issue=5&rft.spage=1252&rft.epage=1259&rft.pages=1252-1259&rft.issn=0950-5423&rft.eissn=1365-2621&rft_id=info:doi/10.1111/ijfs.13392&rft_dat=%3Cproquest_cross%3E1891884135%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4042-10e9e4c7a13ae64e2a24273cf46ce7c7f692685b5e71ddc39dbe938bc5798a2b3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1888600828&rft_id=info:pmid/&rfr_iscdi=true