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Elucidation of different cold-adapted Atlantic cod (Gadus morhua) trypsin X isoenzymes

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dc.contributor Háskóli Íslands
dc.contributor University of Iceland
dc.contributor.author Stefánsson, Bjarki
dc.contributor.author Sandholt, Gunnar Birgir
dc.contributor.author Guðmundsdóttir, Ágústa
dc.date.accessioned 2016-12-05T16:20:01Z
dc.date.available 2016-12-05T16:20:01Z
dc.date.issued 2017-01
dc.identifier.citation Stefansson, B., Sandholt, G. B., & Gudmundsdottir, Á. (2017). Elucidation of different cold-adapted Atlantic cod (Gadus morhua) trypsin X isoenzymes. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1865(1), 11–19. doi:10.1016/j.bbapap.2016.10.005
dc.identifier.issn 1570-9639
dc.identifier.uri https://hdl.handle.net/20.500.11815/153
dc.description.abstract Trypsins from Atlantic cod (Gadus morhua), consisting of several isoenzymes, are highly active cold-adapted serine proteases. These trypsins are isolated for biomedical use in an eco-friendly manner from underutilized seafood by-products. Our group has explored the biochemical properties of trypsins and their high potential in biomedicine. For broader utilization of cod trypsins, further characterization of biochemical properties of the individual cod trypsin isoenzymes is of importance. For that purpose, a benzamidine purified trypsin isolate from Atlantic cod was analyzed. Anion exchange chromatography revealed eight peaks containing proteins around 24 kDa with tryptic activity. Based on mass spectrometric analysis, one isoenzyme gave the best match to cod trypsin I and six isoenzymes gave the best match to cod trypsin X. Amino terminal sequencing of two of these six trypsin isoenzymes showed identity to cod trypsin X. Three sequence variants of trypsin X were identified by cDNA analysis demonstrating that various forms of this enzyme exist. One trypsin X isoenzyme was selected for further characterization based on abundance and stability. Stepwise increase in catalytic efficiency (kcat/Km) of this trypsin X isoenzyme was obtained with substrates containing one to three amino acid residues. The study demonstrates that the catalytic efficiency of this trypsin X isoenzyme is comparable to that of cod trypsin I, the most abundant and highly active isoenzyme in the benzamidine cod trypsin isolate. Differences in pH stability and sensitivity to inhibitors of the trypsin X isoenzyme compared to cod trypsin I were detected that may be important for practical use.
dc.description.sponsorship Research funded by AVS R&D Fund of Ministry of Fisheries and Agriculture in Iceland (R069-08, R11 028-11, R14 044-14) | Science and Technology Development Fund (120852-0611, 131804-0611)
dc.format.extent 11-19
dc.language.iso en
dc.publisher Elsevier BV
dc.relation.ispartofseries Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;1865(1)
dc.rights info:eu-repo/semantics/openAccess
dc.subject Biophysics
dc.subject Analytical Chemistry
dc.subject Biochemistry
dc.subject Molecular Biology
dc.subject Lífefnafræði
dc.subject Efnagreining
dc.subject Lífeðlisfræði
dc.subject Sameindalíffræði
dc.subject Biomedicine
dc.subject Lífvísindi
dc.subject Atlantic cod
dc.subject Atlantshafslax
dc.title Elucidation of different cold-adapted Atlantic cod (Gadus morhua) trypsin X isoenzymes
dc.type info:eu-repo/semantics/article
dc.description.version Ritrýnt tímarit
dc.description.version Peer Reviewed
dc.description.version Pre-Print
dc.identifier.journal Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
dc.identifier.doi 10.1016/j.bbapap.2016.10.005
dc.contributor.department Matvæla- og næringarfræðideild (HÍ)
dc.contributor.department Faculty of Food Science and Nutrition (UI)
dc.contributor.school Heilbrigðisvísindasvið (HÍ)
dc.contributor.school School of Health Sciences (UI)

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