Authors: Li, Renjie, Lund, Pernille, Nielsen, Søren B., Lund, Marianne N.

Superior Title: Li , R , Lund , P , Nielsen , S B & Lund , M N 2022 , ' Formation of whey protein aggregates by partial hydrolysis and reduced thermal treatment ' , Food Hydrocolloids , vol. 124 , 107206 . https://doi.org/10.1016/j.foodhyd.2021.107206

Subject Terms: Aggregates, Disulfide bond, Particle size, Protease, Thermal stability, Whey proteins

File Description: application/pdf

Availability: https://doi.org/10.1016/j.foodhyd.2021.107206
https://curis.ku.dk/portal/da/publications/formation-of-whey-protein-aggregates-by-partial-hydrolysis-and-reduced-thermal-treatment(9d6f7913-f822-45e8-b4e7-a05958d4ea59).html
https://curis.ku.dk/ws/files/288784165/1_s2.0_S0268005X21006226_main.pdf

Authors: Raza, Husnain, Ameer, Kashif, Zaaboul, Farah, Sharif, Hafiz Rizwan, Ali, Barkat, Shoaib, Muhammad, Akhtar, Wasim, Zhang, Lianfu

Superior Title: Raza , H , Ameer , K , Zaaboul , F , Sharif , H R , Ali , B , Shoaib , M , Akhtar , W & Zhang , L 2019 , ' Efectos del molino de bolas en las propiedades fisicoquímicas, térmicas y funcionales del polvo de garbanzo (Cicer arietinum L.) extruido ' , CYTA - Journal of Food , bind 17 , nr. 1 , s. 563-573 . https://doi.org/10.1080/19476337.2019.1617352

Subject Terms: chickpeas, extrusion, functional properties, Particle size, thermal stability

Availability: https://doi.org/10.1080/19476337.2019.1617352
https://curis.ku.dk/portal/da/publications/efectos-del-molino-de-bolas-en-las-propiedades-fisicoquimicas-termicas-y-funcionales-del-polvo-de-garbanzo-cicer-arietinum-l-extruido(8b05bd70-089d-4920-90b7-3ced42c51e77).html
http://www.scopus.com/inward/record.url?scp=85075110611&partnerID=8YFLogxK

Authors: Augustijn, Dillen, Mahapatra, Sujata, Streicher, Werner, Svilenov, Hristo, Kulakova, Alina, Pohl, Christin, Rinnan, Åsmund

Superior Title: Augustijn , D , Mahapatra , S , Streicher , W , Svilenov , H , Kulakova , A , Pohl , C & Rinnan , Å 2019 , ' Novel non-linear curve fitting to resolve protein unfolding transitions in intrinsic fluorescence differential scanning fluorimetry ' , European Journal of Pharmaceutics and Biopharmaceutics , vol. 142 , pp. 506-517 . https://doi.org/10.1016/j.ejpb.2019.06.001

Subject Terms: Biotherapeutics, Differential scanning fluorimetry, Intrinsic fluorescence DSF, Multivariate data analysis, Non-linear curve fitting, Protein screening, Thermal stability screening

File Description: application/pdf

Availability: https://doi.org/10.1016/j.ejpb.2019.06.001
https://curis.ku.dk/portal/da/publications/novel-nonlinear-curve-fitting-to-resolve-protein-unfolding-transitions-in-intrinsic-fluorescence-differential-scanning-fluorimetry(60971cf8-4f9f-48ac-b36b-adb3001143b2).html
https://curis.ku.dk/ws/files/248514768/Novel_Non_linear_Curve_Fitting_to_Resolve_Protein_Unfolding_Transitions_in_Intrinsic_Fluorescence_Differential_Scanning_Fluorimetry.pdf

Authors: Calvarro, Julia, Pérez-Palacios, Trinidad, Ruiz Carrascal, Jorge

Superior Title: Calvarro , J , Pérez-Palacios , T & Ruiz Carrascal , J 2016 , ' Modification of gelatin functionality for culinary applications by using transglutaminase ' , International Journal of Gastronomy and Food Science , vol. 5 , pp. 27-32 . https://doi.org/10.1016/j.ijgfs.2016.11.001

Subject Terms: Culinary, Foams, Gelatin, Gels, Thermal stability, Transglutaminase

File Description: application/pdf

Availability: https://doi.org/10.1016/j.ijgfs.2016.11.001
https://curis.ku.dk/portal/da/publications/modification-of-gelatin-functionality-for-culinary-applications-by-using-transglutaminase(e68d4def-77e7-4631-a356-0974de5faeac).html
https://curis.ku.dk/ws/files/172098299/Modification_of_gelatin_functionality_for_culinary_applications_by_using_transglutaminase.pdf

Authors: Laganovska, K., Olsteins, D., Smits, K., Bite, Bikse, L.

Superior Title: Laganovska , K , Olsteins , D , Smits , K , Bite & Bikse , L 2021 , ' Formation of translucent nanostructured zirconia ceramics ' , Journal of the European Ceramic Society , vol. 41 , no. 13 , pp. 6641-6648 . https://doi.org/10.1016/j.jeurceramsoc.2021.06.005

Subject Terms: Translucent ceramics, Nanostructured ceramics, Pore formation, Zirconia, Up-conversion, THERMAL-STABILITY, TETRAGONAL ZIRCONIA, TRANSPARENT, LUMINESCENCE, STABILIZATION, POWDERS

Availability: https://doi.org/10.1016/j.jeurceramsoc.2021.06.005
https://curis.ku.dk/portal/da/publications/formation-of-translucent-nanostructured-zirconia-ceramics(867c0aab-8369-4f27-a1ea-05dbed01995f).html

Authors: Sosnowska, Malwina Ewa, Jankiewicz, Urszula, Kutwin, Marta, Chwalibog, André, Gałązka, Agnieszka

Superior Title: Sosnowska , M E , Jankiewicz , U , Kutwin , M , Chwalibog , A & Gałązka , A 2018 , ' Influence of salts and metal nanoparticles on the activity and thermal stability of a recombinant chitinase from Stenotrophomonas maltophilia N4 ' , Enzyme and Microbial Technology , vol. 116 , pp. 6-15 . https://doi.org/10.1016/j.enzmictec.2018.05.003

Subject Terms: Chitinase, Nanoparticles, Thermal stability, Transmission electron microscope

Availability: https://doi.org/10.1016/j.enzmictec.2018.05.003
https://curis.ku.dk/portal/da/publications/influence-of-salts-and-metal-nanoparticles-on-the-activity-and-thermal-stability-of-a-recombinant-chitinase-from-stenotrophomonas-maltophilia-n4(cca71da8-98b2-4f9a-a449-bd47504c6c01).html

Authors: Feng, Tao, Nyffenegger, Christian, Højrup, Peter, Vidal Melgosa, Silvia, Yan, Kok-Phen, Fangel, Jonatan Ulrik, Meyer, Anne S., Kirpekar, Finn, Willats, William George Tycho, Mikkelsen, Jørn Dalgaard

Superior Title: Feng , T , Nyffenegger , C , Højrup , P , Vidal Melgosa , S , Yan , K-P , Fangel , J U , Meyer , A S , Kirpekar , F , Willats , W G T & Mikkelsen , J D 2014 , ' Characterization of an extensin-modifying metalloprotease : N -terminal processing and substrate cleavage pattern of Pectobacterium carotovorum Prt1 ' , Applied Microbiology and Biotechnology , vol. 98 , no. 24 , pp. 10077-10089 . https://doi.org/10.1007/s00253-014-5877-2

Subject Terms: Potato lectin, Plant extension, Glycan microarray, Proline preference, Thermal stability, Autolytic processing

Availability: https://doi.org/10.1007/s00253-014-5877-2
https://curis.ku.dk/portal/da/publications/characterization-of-an-extensinmodifying-metalloprotease(da559689-c46d-4cd4-b028-7d00a3537a5e).html