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UV-C light promotes the reductive cleavage of disulfide bonds in β-Lactoglobulin and improves in vitro gastric digestion

  • Published:2023-06 Issue: Volume:168 Page:112729
  • ISSN:0963-9969
  • Container-title:Food Research International
  • language:en
  • Short-container-title:Food Research International

Author:

da Silva Juliana F.,Morais Aline T. do B.,Santos Willy G.,M. Ahrné Lilia,Cardoso Daniel R.ORCID

Funder

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Innovationsfonden

Fundação de Amparo à Pesquisa do Estado de São Paulo

Publisher

Elsevier BV

Subject

Food Science

Reference56 articles.

1. Tryptophan 19 residue is the origin of bovine β-lactoglobulin fluorescence;Albani;Journal of Pharmaceutical and Biomedical Analysis,2014

2. Preventive role of lens antioxidant defense mechanism against riboflavin-mediated sunlight damaging of lens crystallins;Anbaraki;International Journal of Biological Macromolecules,2016

3. Barth, A. (2007). Infrared spectroscopy of proteins. 1767, 1073–1101 10.1016/j.bbabio.2007.06.004.

4. Excited states and free radicals in biology and medicine: Contributions from flash photolysis and pulse radiolysis;Bensasson,1993

5. Excited state chemistry of aromatic amino acids and related peptides. III. Tryptophan;Bent;Journal of the American Chemical Society,1975
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