Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Dennis K, Hansen"'
Autor:
Betül Yesiltas, Pedro J. García-Moreno, Rasmus K. Mikkelsen, Simon Gregersen Echers, Dennis K. Hansen, Mathias Greve-Poulsen, Grethe Hyldig, Egon B. Hansen, Charlotte Jacobsen
Publikováno v:
Antioxidants, Vol 12, Iss 8, p 1622 (2023)
This work studies the emulsifying and antioxidant properties of potato protein hydrolysates (PPHs) fractions obtained through enzymatic hydrolysis of potato protein using trypsin followed by ultrafiltration. Unfractionated (PPH1) and fractionated (PP
Externí odkaz:
https://doaj.org/article/699ef0ec5a744611b8f8945e1eb58295
Autor:
Simon Gregersen Echers, Ali Jafarpour, Betül Yesiltas, Pedro J. García-Moreno, Mathias Greve-Poulsen, Dennis K. Hansen, Charlotte Jacobsen, Michael Toft Overgaard, Egon Bech Hansen
Publikováno v:
Echers, S G, Jafarpour, A, Yesiltas, B, García-Moreno, P J, Greve-Poulsen, M, Hansen, D K, Jacobsen, C, Overgaard, M T & Hansen, E B 2023, ' Targeted hydrolysis of native potato protein : A novel workflow for obtaining hydrolysates with improved interfacial properties ', Food Hydrocolloids, vol. 137, 108299 . https://doi.org/10.1016/j.foodhyd.2022.108299
Gregersen Echers, S, Jafarpour, A, Yesiltas, B, García Moreno, P J, Greve-Poulsen, M, Hansen, D K, Jacobsen, C, Overgaard, M T & Hansen, E B 2023, ' Targeted hydrolysis of native potato protein: A novel workflow for obtaining hydrolysates with improved interfacial properties ', Food Hydrocolloids, vol. 137, 108299 . https://doi.org/10.1016/j.foodhyd.2022.108299
Gregersen Echers, S, Jafarpour, A, Yesiltas, B, García Moreno, P J, Greve-Poulsen, M, Hansen, D K, Jacobsen, C, Overgaard, M T & Hansen, E B 2023, ' Targeted hydrolysis of native potato protein: A novel workflow for obtaining hydrolysates with improved interfacial properties ', Food Hydrocolloids, vol. 137, 108299 . https://doi.org/10.1016/j.foodhyd.2022.108299
Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel workflow for producing a potato protein hydrolysate with improved emulsifying and foaming
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::687fa3a39e586905274ec28496f65824
https://orbit.dtu.dk/en/publications/0978fa08-9480-4b38-93dd-dc436e78b0d7
https://orbit.dtu.dk/en/publications/0978fa08-9480-4b38-93dd-dc436e78b0d7
Autor:
Martin Willemoës, Anders Lønstrup Hansen, Ramon Crehuet, Signe F. Simonsen, Johanna M Koivisto, Dennis K. Hansen, Zehui Dong
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Hansen, A L, Koivisto, J M, Simonsen, S, Dong, Z, Crehuet, R, Hansen, D K & Willemoës, M 2021, ' Identification of a Catalytic Nucleophile-Activating Network in the endo-α-N-Acetylgalactosaminidase of Family GH101 ', Biochemistry, vol. 60, no. 45, pp. 3398-3407 . https://doi.org/10.1021/acs.biochem.1c00596
instname
Hansen, A L, Koivisto, J M, Simonsen, S, Dong, Z, Crehuet, R, Hansen, D K & Willemoës, M 2021, ' Identification of a Catalytic Nucleophile-Activating Network in the endo-α-N-Acetylgalactosaminidase of Family GH101 ', Biochemistry, vol. 60, no. 45, pp. 3398-3407 . https://doi.org/10.1021/acs.biochem.1c00596
Bifidobacterium longum endo-α-N-acetylgalactosaminidase (GH101), EngBF, is highly specific toward the mucin Core 1 glycan, Galβ1-3GalNAc. Apart from the side chains involved in the retaining mechanism of EngBF, Asp-682 is important for the activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97f6230cca750b68e434efedd39b2615
https://doi.org/10.1021/acs.biochem.1c00596
https://doi.org/10.1021/acs.biochem.1c00596
Autor:
Dennis K. Hansen, Anders Lønstrup Hansen, Johanna M. Koivisto, Bashar Shuoker, Maher Abou Hachem, Jakob R. Winther, Martin Willemoës
Publikováno v:
Hansen, D K, Hansen, A L, Koivisto, J M, Shuoker, B, Abou Hachem, M, Winther, J R & Willemoës, M 2022, ' Engineering Bifidobacterium longum Endo-α-N-acetylgalactosaminidase for Neu5Acα2-3Galβ1-3GalNAc reactivity on Fetuin ', Archives of Biochemistry and Biophysics, vol. 725, 109280 . https://doi.org/10.1016/j.abb.2022.109280
Endo-α-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) belongs to the glycoside hydrolase family GH101 and has a strict preference towards the mucin type glycan, Galβ1-3GalNAc, which is O-linked to serine or threonine residues on glyc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56665503e2d5af14b65c3e234df79eee
https://orbit.dtu.dk/en/publications/4da792a3-bdc0-4b74-ab78-debe806318e3
https://orbit.dtu.dk/en/publications/4da792a3-bdc0-4b74-ab78-debe806318e3
Autor:
Anders Lønstrup, Hansen, Johanna M, Koivisto, Signe, Simonsen, Zehui, Dong, Ramon, Crehuet, Dennis K, Hansen, Martin, Willemoës
Publikováno v:
Biochemistry. 60(45)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dcd4e8f770c71342e253c60c9db3e310
https://pubmed.ncbi.nlm.nih.gov/34694774
https://pubmed.ncbi.nlm.nih.gov/34694774
Publikováno v:
Carbohydrate research. 480
Often glycosidase assays are based on small-molecule compounds where a glycan of interest is linked to a chromophore allowing for easy detection of cleavage of the glycoside bond. However, such compounds only resemble part of the more complex substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::437284e91065f7c56142a61fa9543fcb
https://pubmed.ncbi.nlm.nih.gov/31176190
https://pubmed.ncbi.nlm.nih.gov/31176190