Thermal-Induced Autolysis Enzymes Inactivation, Protein Degradation and Physical Properties of Sea Cucumber, Cucumaria frondosa

dc.contributor.authorZhang, Qian
dc.contributor.authorLiu, Ru
dc.contributor.authorGeirsdóttir, Margrét
dc.contributor.authorLi, Shiyu
dc.contributor.authorTomasson, Tumi
dc.contributor.authorXiong, Shanbai
dc.contributor.authorLi, Xiuchen
dc.contributor.authorGudjónsdóttir, María
dc.contributor.departmentFaculty of Food Science and Nutrition
dc.date.accessioned2025-11-20T09:01:56Z
dc.date.available2025-11-20T09:01:56Z
dc.date.issued2022-04-25
dc.descriptionFunding Information: Funding: This work was supported by the Fisheries Training Programme of United Nations University (UNU-FTP2017), Research and Demonstration of Efficient Clean Production Mode of Important Marine Fish in Liaoning Province (2020JH1/10200002), National Key R&D Program of China (2019YFD0901800), Project of Education Department of Liaoning Province (JL202011), Project of Ocean and Fisheries Department of Liaoning Province (201722), Key Laboratory of Environment Controlled Aquaculture (Dalian Ocean University) Ministry of Education (202203); National Key R&D Program of China (2020YFD0900600). Funding Information: Acknowledgments: The authors would like to express their heartfelt gratitude to United Nations University Fisheries Training Programme (now GRÓ Fisheries Training Programme, United Nations Education, Scientific and Cultural Organization) and Matis for supporting this research. Special thanks go to Tumi Tomasson, Thor Asgeirsson, Mary Frances Davidson, Julie Ingham, Stefan Ulfarsson, and Lilja Bjork Jonsdottir, for their enthusiastic guidance and assistance during the experiment. Publisher Copyright: © 2022 by the authors. Licensee MDPI, Basel, Switzerland.en
dc.description.abstractThe main objective is to effectively denature the autolysis enzymes of C. frondosa on the premise of avoiding the quality deterioration caused by overheating. The effects of the different thermal treatments (blanching at 40–80◦ C for 45 min, boiling and steaming at 100◦ C for 15–120 min) on the cooking yield, moisture content, protein degradation, texture, and enzyme inactivation were studied, and the inner relationship was investigated by multivariate analysis. The autolysis enzymes of C. frondosa were thermally stable and cannot be denatured completely by blanching. Boiling and steaming could efficiently inactivate the enzymes but overheating for 60–120 min reduced the cooking yield and texture quality. Boiling at 100◦ C for 45 min was suitable for pre-treatment, with cooking yield of 70.3% and protein content of 78.5%. Steaming at 100◦ C for at least 30 min was preferable for long-term storage and instant food, in which the relative activity was only 3.2% with better palatability.en
dc.description.versionPeer revieweden
dc.format.extent2937487
dc.format.extent
dc.identifier.citationZhang, Q, Liu, R, Geirsdóttir, M, Li, S, Tomasson, T, Xiong, S, Li, X & Gudjónsdóttir, M 2022, 'Thermal-Induced Autolysis Enzymes Inactivation, Protein Degradation and Physical Properties of Sea Cucumber, Cucumaria frondosa', Processes, vol. 10, no. 5, 847. https://doi.org/10.3390/pr10050847en
dc.identifier.doi10.3390/pr10050847
dc.identifier.issn2227-9717
dc.identifier.other69177337
dc.identifier.otherae11b834-828d-403b-bb09-dd93186f475a
dc.identifier.other85129621305
dc.identifier.otherunpaywall: 10.3390/pr10050847
dc.identifier.urihttps://hdl.handle.net/20.500.11815/6989
dc.language.isoen
dc.relation.ispartofseriesProcesses; 10(5)en
dc.relation.urlhttps://www.scopus.com/pages/publications/85129621305en
dc.rightsinfo:eu-repo/semantics/openAccessen
dc.subjectautolysis enzymeen
dc.subjectCucumaria frondosaen
dc.subjectinactivationen
dc.subjectprotein denaturationen
dc.subjecttextureen
dc.subjectthermal processingen
dc.subjectBioengineeringen
dc.subjectChemical Engineering (miscellaneous)en
dc.subjectProcess Chemistry and Technologyen
dc.titleThermal-Induced Autolysis Enzymes Inactivation, Protein Degradation and Physical Properties of Sea Cucumber, Cucumaria frondosaen
dc.type/dk/atira/pure/researchoutput/researchoutputtypes/contributiontojournal/articleen

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