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dc.contributor.authorNatthaphon Mongkonkamthornen_US
dc.contributor.authorYuwares Malilaen_US
dc.contributor.authorJoe M. Regensteinen_US
dc.contributor.authorSutee Wangtueaien_US
dc.date.accessioned2022-10-16T06:58:48Z-
dc.date.available2022-10-16T06:58:48Z-
dc.date.issued2021-01-01en_US
dc.identifier.issn15470636en_US
dc.identifier.issn10498850en_US
dc.identifier.other2-s2.0-85117230208en_US
dc.identifier.other10.1080/10498850.2021.1974138en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85117230208&origin=inwarden_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/75361-
dc.description.abstractThe hydrolysates of tuna dark meat with high angiotensin I-converting enzyme (ACE) inhibitory and antioxidant activities were prepared using three enzymes. The effect of concentration (0.5–3.0%, w/w) and hydrolysis time (30–180 min) on yield, degree of hydrolysis (DH), ACE inhibitory activities, and antioxidant capacity was determined. The optimum conditions were the same: 180 min extraction while the concentration of alcalase, neutrase, and flavourzyme were 2.43, 2.62, and 2.62% (w/w), respectively. The hydrolysate resulted in the range of 36.5–50.0% for DH, 5.79–7.71% for yield, 0.29–1.11, 0.28–0.53, and 0.24–0.31 mg/mL IC50 values with 2,2-diphenyi-l-picrylhydrazyl radical (DPPH), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS), and ACE inhibitory activity, respectively, and 0.41–1.35 FeSO4/g for ferric reducing antioxidant power (FRAP). The hydrolysates showed high solubility. Emulsion stability and emulsifying activity index decreased, while foam stability and expansion increased with increasing concentration. Hydrolysates using flavourzyme were fractioned using ultrafiltration membranes. The <1 kDa fraction had significantly higher ACE inhibitory and antioxidant activities.en_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.titleEnzymatic Hydrolysis Optimization for Preparation of Tuna Dark Meat Hydrolysate with Antioxidant and Angiotensin I-Converting Enzyme (ACE) Inhibitory Activitiesen_US
dc.typeJournalen_US
article.title.sourcetitleJournal of Aquatic Food Product Technologyen_US
article.volume30en_US
article.stream.affiliationsCornell University College of Agriculture and Life Sciencesen_US
article.stream.affiliationsThailand National Center for Genetic Engineering and Biotechnologyen_US
article.stream.affiliationsChiang Mai Universityen_US
Appears in Collections:CMUL: Journal Articles

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