Author(s):
Fuciños, C. ; Fuciños, Pablo ; Estévez, Natalia ; Pastrana, Lorenzo M. ; Vicente, A. A. ; Rúa, María Luisa
Date: 2019
Persistent ID: https://hdl.handle.net/1822/56384
Origin: RepositóriUM - Universidade do Minho
Project/scholarship:
info:eu-repo/grantAgreement/FCT/5876/147337/PT;
info:eu-repo/grantAgreement/FCT/5876-PPCDTI/126270/PT
;
info:eu-repo/grantAgreement/FCT/COMPETE/126270/PT;
Subject(s): Whey proteins; alfa-Lactalbumin; Purification; AEC chromatography; Nanotubes; Protein gels; α-Lactalbumin; Science & Technology
Description
A one-step anion-exchange chromatography method (NaCl gradient elution on a DEAE Sepharose Fast Flow gel column) was developed to purify -lactalbumin (-LA) from whey protein isolate. -LA nearly 100% pure (based on the total protein content) was obtained with a yield of about 39%. Besides pure -LA, which was the main objective of this work, highly pure -lactoglobulin was also obtained with a yield of about 59%. The high purity of the obtained -LA samples allowed its use to synthesise protein nanotubes with excellent gelation properties for their use as food thickeners and bioactive carriers. The samples purity degree obtained (based on the total protein content) was critical in the formation of proper nanotubes instead of random aggregates, which produced opaque and weak gels, less useful for food applications.
Clara Fuciños gratefully acknowledge her Postdoctoral grant (I2C 2014) from Consellería de Cultura, Educación e Ordenación Universitaria(XuntadeGalicia,Spain).Thisstudywassupportedbythe Portuguese Foundation for Science and Technology (FCT, Portugal) under the scope of the strategic funding of UID/BIO/04469/2013 unit and the Project RECI/BBB-EBI/0179/2012 (FCOMP-01-0124-FEDER027462).
info:eu-repo/semantics/publishedVersion
