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dc.contributor.authorSáez, Laura
dc.contributor.authorMurphy, Eoin
dc.contributor.authorFitzGerald, Richard J
dc.contributor.authorKelly, Philip
dc.date.accessioned2020-06-16T11:47:27Z
dc.date.available2020-06-16T11:47:27Z
dc.date.issued2019-08-26
dc.identifier.citationSáez, L.; Murphy, E.; FitzGerald, R.J.; Kelly, P. Exploring the Use of a Modified High-Temperature, Short-Time Continuous Heat Exchanger with Extended Holding Time (HTST-EHT) for Thermal Inactivation of Trypsin Following Selective Enzymatic Hydrolysis of the β-Lactoglobulin Fraction in Whey Protein Isolate. Foods 2019, 8, 367. doi:https://doi.org/10.3390/foods8090367en_US
dc.identifier.issn2304-8158
dc.identifier.urihttp://hdl.handle.net/11019/1983
dc.descriptionpeer-revieweden_US
dc.description.abstractTryptic hydrolysis of whey protein isolate under specific incubation conditions including a relatively high enzyme:substrate (E:S) ratio of 1:10 is known to preferentially hydrolyse β-lactoglobulin (β-LG), while retaining the other major whey protein fraction, i.e., α-lactalbumin (α-LA) mainly intact. An objective of the present work was to explore the effects of reducing E:S (1:10, 1:30, 1:50, 1:100) on the selective hydrolysis of β-LG by trypsin at pH 8.5 and 25 °C in a 5% (w/v) WPI solution during incubation periods ranging from 1 to 7 h. In addition, the use of a pilot-scale continuous high-temperature, short-time (HTST) heat exchanger with an extended holding time (EHT) of 5 min as a means of inactivating trypsin to terminate hydrolysis was compared with laboratory-based acidification to <pH 3 by the addition of HCl, and batch sample heating in a water bath at 85 °C. An E:S of 1:10 resulted in 100% and 30% of β-LG and α-LA hydrolysis, respectively, after 3 h, while an E:S reduction to 1:30 and 1:50 led >90% β-LG hydrolysis after respective incubation periods of 4 and 6 h, with <5% hydrolysis of α-LA in the case of 1:50. Continuous HTST-EHT treatment was shown to be an effective inactivation process allowing for the maintenance of substrate selectivity. However, HTST-EHT heating resulted in protein aggregation, which negatively impacts the downstream recovery of intact α-LA. An optimum E:S was determined to be 1:50, with an incubation time ranging from 3 h to 7 h leading to 90% β-LG hydrolysis and minimal degradation of α-LA. Alternative batch heating by means of a water bath to inactivate trypsin caused considerable digestion of α-LA, while acidification to <pH 3.0 restricted subsequent functional applications of the protein.en_US
dc.language.isoenen_US
dc.publisherMDPIen_US
dc.relation.ispartofseriesFoods;Vol. 8 (9)
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subjectHydrolysisen_US
dc.subjectWPIen_US
dc.subjectthermal inactivationen_US
dc.subjecttrypsinen_US
dc.subjectα-lactalbuminen_US
dc.subjectβ-lactoglobulinen_US
dc.titleExploring the Use of a Modified High-Temperature, Short-Time Continuous Heat Exchanger with Extended Holding Time (HTST-EHT) for Thermal Inactivation of Trypsin Following Selective Enzymatic Hydrolysis of the β-Lactoglobulin Fraction in Whey Protein Isolate.en_US
dc.typeArticleen_US
dc.identifier.doihttps://doi.org/10.3390/foods8090367
dc.contributor.sponsorEnterprise Irelanden_US
dc.contributor.sponsorGrantNumberTC20130001en_US
refterms.dateFOA2020-06-16T11:47:27Z
dc.source.journaltitleFoods (Basel, Switzerland)


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