Effect of enzyme‐assisted hydrolysis on brewer's spent grain protein solubilization – peptide composition and sensory properties

dc.contributor.authorKriisa Marie
dc.contributor.authorTaivosalo Anastassia
dc.contributor.authorFöste Maike
dc.contributor.authorKütt Mary-Liis
dc.contributor.authorViirma Maret
dc.contributor.authorPriidik Reimo
dc.contributor.authorKorzeniowska Malgorzata
dc.contributor.authorTian Ye
dc.contributor.authorLaaksonen Oskar
dc.contributor.authorYang Baoru
dc.contributor.authorVilu Raivo
dc.contributor.organizationfi=elintarviketieteet|en=Food Sciences|
dc.contributor.organization-code1.2.246.10.2458963.20.15178954341
dc.converis.publication-id175085153
dc.converis.urlhttps://research.utu.fi/converis/portal/Publication/175085153
dc.date.accessioned2025-08-28T00:38:35Z
dc.date.available2025-08-28T00:38:35Z
dc.description.abstract<p> This study aimed to valorize brewer's spent grain (BSG) from a side-stream into protein ingredients suitable for human consumption. The impact of protease treatments was studied for solubilizing BSG proteins. Treatment with Protamex or simultaneous co-incubation of Protamex and Flavourzyme solubilized up to 60% of the total protein in BSG, whereas co-incubation with Flavourzyme increased the availability of hydrophobic amino acids (Val, Phe, Ala, Leu, Ile) in extracts. The scale-up of protease treatments demonstrated comparable solubilized protein fractions in 0.1 L and 10 L reaction volumes. Thorough sequence-based peptide analysis by liquid chromatography-ion mobility-mass spectrometry resulted in the identification of 479 and 451 water-soluble peptides in the hydrolysates obtained with Protamex or co-incubation of Protamex and Flavourzyme, respectively. Main cutting sites on BSG proteins were identified between Leu-Gln, Tyr-Phe, Pro-X (Protamex), complementing with a variety of cutting sites mainly next to Gln, Pro, Ile, and Phe when combined with Flavourzyme. Uniform protease activity throughout the entire B-hordein sequence and the formation of peptides with varying sequence lengths did not increase the bitterness of the hydrolysates compared to the BSG sample with water extraction. These results support the characterization of enzymatic treatments in plant-based materials and the production of hydrolysates with desired composition. <br></p>
dc.identifier.eissn2772-5022
dc.identifier.jour-issn2772-5022
dc.identifier.olddbid206101
dc.identifier.oldhandle10024/189128
dc.identifier.urihttps://www.utupub.fi/handle/11111/41606
dc.identifier.urlhttps://doi.org/10.1016/j.afres.2022.100108
dc.identifier.urnURN:NBN:fi-fe2022081153875
dc.language.isoen
dc.okm.affiliatedauthorTian, Ye
dc.okm.affiliatedauthorLaaksonen, Oskar
dc.okm.affiliatedauthorYang, Baoru
dc.okm.discipline1182 Biochemistry, cell and molecular biologyen_GB
dc.okm.discipline1182 Biokemia, solu- ja molekyylibiologiafi_FI
dc.okm.internationalcopublicationinternational co-publication
dc.okm.internationalityInternational publication
dc.okm.typeA1 ScientificArticle
dc.publisherElsevier BV
dc.publisher.countryNetherlandsen_GB
dc.publisher.countryAlankomaatfi_FI
dc.publisher.country-codeNL
dc.relation.articlenumber100108
dc.relation.doi10.1016/j.afres.2022.100108
dc.relation.ispartofjournalApplied Food Research
dc.relation.issue1
dc.relation.volume2
dc.source.identifierhttps://www.utupub.fi/handle/10024/189128
dc.titleEffect of enzyme‐assisted hydrolysis on brewer's spent grain protein solubilization – peptide composition and sensory properties
dc.year.issued2022

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