Articles producció científica> Bioquímica i Biotecnologia

Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates

  • Datos identificativos

    Identificador: imarina:6386662
    Autores:
    Torres-Fuentes, CAlaiz, MVioque, J
    Resumen:
    A chickpea protein hydrolysate produced with pepsin and pancreatin was used for the affinity purification of chickpea chelating peptides. Three chelating peptide fractions were obtained after affinity chromatography with immobilised copper. These peptide fractions showed a higher chelating activity and histidine contents than the original protein hydrolysate. Chelating activity was positively correlated with the histidine content of the purified fractions. Different subfractions were also obtained after gel filtration chromatography from the affinity purified peptide fractions. Some of these subfractions showed a higher chelating activity and histidine contents than the original fractions. These results suggest that a combination of high His contents, around 20-30%, and small peptide size provide the best chelating activities. Thus sequential purification with affinity and gel filtration chromatography is a useful procedure for the purification of chickpea peptides with high chelating activity. These results show that a range of chelating peptides are generated during digestion of the chickpea proteins that, after metal chelation, may prevent the generation of reactive oxygen species (ROS) and favour metal absorption. © 2011 Elsevier Ltd. All rights reserved.
  • Otros:

    Autor según el artículo: Torres-Fuentes, C; Alaiz, M; Vioque, J
    Departamento: Bioquímica i Biotecnologia
    Autor/es de la URV: Torres Fuentes, Cristina
    Palabras clave: Protein hydrolysate Pepsin Pancreatin Chickpea Chelating peptides pepsin pancreatin chickpea chelating peptides
    Resumen: A chickpea protein hydrolysate produced with pepsin and pancreatin was used for the affinity purification of chickpea chelating peptides. Three chelating peptide fractions were obtained after affinity chromatography with immobilised copper. These peptide fractions showed a higher chelating activity and histidine contents than the original protein hydrolysate. Chelating activity was positively correlated with the histidine content of the purified fractions. Different subfractions were also obtained after gel filtration chromatography from the affinity purified peptide fractions. Some of these subfractions showed a higher chelating activity and histidine contents than the original fractions. These results suggest that a combination of high His contents, around 20-30%, and small peptide size provide the best chelating activities. Thus sequential purification with affinity and gel filtration chromatography is a useful procedure for the purification of chickpea peptides with high chelating activity. These results show that a range of chelating peptides are generated during digestion of the chickpea proteins that, after metal chelation, may prevent the generation of reactive oxygen species (ROS) and favour metal absorption. © 2011 Elsevier Ltd. All rights reserved.
    Áreas temáticas: Zootecnia / recursos pesqueiros Saúde coletiva Química Odontología Nutrition & dietetics Nutrição Medicine (miscellaneous) Medicina veterinaria Medicina ii Medicina i Materiais Matemática / probabilidade e estatística Interdisciplinar Geociências Food science & technology Food science Farmacia Ensino Engenharias iv Engenharias iii Engenharias ii Engenharias i Enfermagem Educação física Ciências biológicas iii Ciências biológicas ii Ciências biológicas i Ciências ambientais Ciências agrárias i Ciência de alimentos Ciência da computação Chemistry, applied Biotecnología Biodiversidade Astronomia / física Analytical chemistry Administração pública e de empresas, ciências contábeis e turismo
    Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 03088146
    Direcció de correo del autor: cristina.torres@urv.cat
    Identificador del autor: 0000-0002-2917-6910
    Fecha de alta del registro: 2024-02-11
    Versión del articulo depositado: info:eu-repo/semantics/submittedVersion
    Enlace a la fuente original: https://www.sciencedirect.com/science/article/abs/pii/S0308814611006698?via%3Dihub
    Referencia al articulo segun fuente origial: Food Chemistry. 129 (2): 485-490
    Referencia de l'ítem segons les normes APA: Torres-Fuentes, C; Alaiz, M; Vioque, J (2011). Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates. Food Chemistry, 129(2), 485-490. DOI: 10.1016/j.foodchem.2011.04.103
    URL Documento de licencia: https://repositori.urv.cat/ca/proteccio-de-dades/
    DOI del artículo: 10.1016/j.foodchem.2011.04.103
    Entidad: Universitat Rovira i Virgili
    Año de publicación de la revista: 2011
    Tipo de publicación: Journal Publications
  • Palabras clave:

    Analytical Chemistry,Chemistry, Applied,Food Science,Food Science & Technology,Medicine (Miscellaneous),Nutrition & Dietetics
    Protein hydrolysate
    Pepsin
    Pancreatin
    Chickpea
    Chelating peptides
    pepsin
    pancreatin
    chickpea
    chelating peptides
    Zootecnia / recursos pesqueiros
    Saúde coletiva
    Química
    Odontología
    Nutrition & dietetics
    Nutrição
    Medicine (miscellaneous)
    Medicina veterinaria
    Medicina ii
    Medicina i
    Materiais
    Matemática / probabilidade e estatística
    Interdisciplinar
    Geociências
    Food science & technology
    Food science
    Farmacia
    Ensino
    Engenharias iv
    Engenharias iii
    Engenharias ii
    Engenharias i
    Enfermagem
    Educação física
    Ciências biológicas iii
    Ciências biológicas ii
    Ciências biológicas i
    Ciências ambientais
    Ciências agrárias i
    Ciência de alimentos
    Ciência da computação
    Chemistry, applied
    Biotecnología
    Biodiversidade
    Astronomia / física
    Analytical chemistry
    Administração pública e de empresas, ciências contábeis e turismo
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