Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system

Autores
Pescuma, Micaela; Hebert, Elvira Maria; Dalgalarrondo, Michèle; Haertlé, Thomas; Mozzi, Fernanda Beatriz; Chobert, Jean Marc; Font, Graciela Maria
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An analysis of the peptides generated by hydrolysis of BLG by nonproliferating cells of the strain Lactobacillus acidophilus CRL 636 was carried out. The effect of polysaccharides (pectin, and two EPS synthesized by two Streptococcus thermophilus strains, EPS1190 and EPS804) on BLG digestibility using an in vitro gastric/pancreatic system was analyzed. Polysaccharides are commonly used in the dairy industry to improve food texture; these hydrocolloids may interact with proteins, affecting their digestibility. Nonproliferating cells of Lb. acidophilus CRL 636 were able to hydrolyze 52% of BLG. Twenty-six resulting peptides with molecular masses in the range 544-4119 Da were identified by LC-MS/MS. These peptides resulted mostly from the hydrolysis of the more accessible N-terminal part of BLG. Degradation of BLG by pepsin was poor (8%). When BLG was previously hydrolyzed by Lb. acidophilus CRL 636, peptic hydrolysis was of 54.8%, while when pectin and EPS1190 were added, hydrolysis was higher (58.2 and 57.2%, respectively). Peptides crossing 8 kDa dialysis membranes after trypsin/chymotrypsin hydrolysis were analyzed by HPSEC. The produced peptides were smaller when BLG was hydrolyzed previously by the Lb. acidophilus strain. Moreover, in the presence of pectin, the amount of the larger peptide (3.5 kDa) observed in the size exclusion chromatograms was considerably decreased. Our studies showed that prehydrolysis of BLG by Lb. acidophilus CRL 636 had a positive influence on BLG digestibility and that polysaccharides may change the peptide profile yielded by trypsin/chymotrypsin hydrolysis, releasing smaller size peptides, which are known to be less immune-reactive. Moreover, Lb. acidophilus CRL 636 was able to hydrolyze the main epitopes (41-60, 102-124, and 149-162) of BLG, reducing its allergenic content.
Fil: Pescuma, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Dalgalarrondo, Michèle. Institut National de la Recherche Agronomique; Francia
Fil: Haertlé, Thomas. Institut National de la Recherche Agronomique; Francia
Fil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Chobert, Jean Marc. Institut National de la Recherche Agronomique; Francia
Fil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Materia
Ss-Lactoglobulin
Digestive System
Exopolysaccharide
Lactic Acid Bacteria
Proteolysis
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/54448
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/54448
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic systemPescuma, MicaelaHebert, Elvira MariaDalgalarrondo, MichèleHaertlé, ThomasMozzi, Fernanda BeatrizChobert, Jean MarcFont, Graciela MariaSs-LactoglobulinDigestive SystemExopolysaccharideLactic Acid BacteriaProteolysishttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1An analysis of the peptides generated by hydrolysis of BLG by nonproliferating cells of the strain Lactobacillus acidophilus CRL 636 was carried out. The effect of polysaccharides (pectin, and two EPS synthesized by two Streptococcus thermophilus strains, EPS1190 and EPS804) on BLG digestibility using an in vitro gastric/pancreatic system was analyzed. Polysaccharides are commonly used in the dairy industry to improve food texture; these hydrocolloids may interact with proteins, affecting their digestibility. Nonproliferating cells of Lb. acidophilus CRL 636 were able to hydrolyze 52% of BLG. Twenty-six resulting peptides with molecular masses in the range 544-4119 Da were identified by LC-MS/MS. These peptides resulted mostly from the hydrolysis of the more accessible N-terminal part of BLG. Degradation of BLG by pepsin was poor (8%). When BLG was previously hydrolyzed by Lb. acidophilus CRL 636, peptic hydrolysis was of 54.8%, while when pectin and EPS1190 were added, hydrolysis was higher (58.2 and 57.2%, respectively). Peptides crossing 8 kDa dialysis membranes after trypsin/chymotrypsin hydrolysis were analyzed by HPSEC. The produced peptides were smaller when BLG was hydrolyzed previously by the Lb. acidophilus strain. Moreover, in the presence of pectin, the amount of the larger peptide (3.5 kDa) observed in the size exclusion chromatograms was considerably decreased. Our studies showed that prehydrolysis of BLG by Lb. acidophilus CRL 636 had a positive influence on BLG digestibility and that polysaccharides may change the peptide profile yielded by trypsin/chymotrypsin hydrolysis, releasing smaller size peptides, which are known to be less immune-reactive. Moreover, Lb. acidophilus CRL 636 was able to hydrolyze the main epitopes (41-60, 102-124, and 149-162) of BLG, reducing its allergenic content.Fil: Pescuma, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Dalgalarrondo, Michèle. Institut National de la Recherche Agronomique; FranciaFil: Haertlé, Thomas. Institut National de la Recherche Agronomique; FranciaFil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Chobert, Jean Marc. Institut National de la Recherche Agronomique; FranciaFil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaAmerican Chemical Society2009-06-24info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/54448Pescuma, Micaela; Hebert, Elvira Maria; Dalgalarrondo, Michèle; Haertlé, Thomas; Mozzi, Fernanda Beatriz; et al.; Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system; American Chemical Society; Journal of Agricultural and Food Chemistry; 57; 12; 24-6-2009; 5571-55770021-85611520-5118CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/jf9006505info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/jf9006505info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:06:40Zoai:ri.conicet.gov.ar:11336/54448instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:06:41.035CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
title Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
spellingShingle Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
Pescuma, Micaela
Ss-Lactoglobulin
Digestive System
Exopolysaccharide
Lactic Acid Bacteria
Proteolysis
title_short Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
title_full Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
title_fullStr Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
title_full_unstemmed Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
title_sort Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system
dc.creator.none.fl_str_mv Pescuma, Micaela
Hebert, Elvira Maria
Dalgalarrondo, Michèle
Haertlé, Thomas
Mozzi, Fernanda Beatriz
Chobert, Jean Marc
Font, Graciela Maria
author Pescuma, Micaela
author_facet Pescuma, Micaela
Hebert, Elvira Maria
Dalgalarrondo, Michèle
Haertlé, Thomas
Mozzi, Fernanda Beatriz
Chobert, Jean Marc
Font, Graciela Maria
author_role author
author2 Hebert, Elvira Maria
Dalgalarrondo, Michèle
Haertlé, Thomas
Mozzi, Fernanda Beatriz
Chobert, Jean Marc
Font, Graciela Maria
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Ss-Lactoglobulin
Digestive System
Exopolysaccharide
Lactic Acid Bacteria
Proteolysis
topic Ss-Lactoglobulin
Digestive System
Exopolysaccharide
Lactic Acid Bacteria
Proteolysis
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv An analysis of the peptides generated by hydrolysis of BLG by nonproliferating cells of the strain Lactobacillus acidophilus CRL 636 was carried out. The effect of polysaccharides (pectin, and two EPS synthesized by two Streptococcus thermophilus strains, EPS1190 and EPS804) on BLG digestibility using an in vitro gastric/pancreatic system was analyzed. Polysaccharides are commonly used in the dairy industry to improve food texture; these hydrocolloids may interact with proteins, affecting their digestibility. Nonproliferating cells of Lb. acidophilus CRL 636 were able to hydrolyze 52% of BLG. Twenty-six resulting peptides with molecular masses in the range 544-4119 Da were identified by LC-MS/MS. These peptides resulted mostly from the hydrolysis of the more accessible N-terminal part of BLG. Degradation of BLG by pepsin was poor (8%). When BLG was previously hydrolyzed by Lb. acidophilus CRL 636, peptic hydrolysis was of 54.8%, while when pectin and EPS1190 were added, hydrolysis was higher (58.2 and 57.2%, respectively). Peptides crossing 8 kDa dialysis membranes after trypsin/chymotrypsin hydrolysis were analyzed by HPSEC. The produced peptides were smaller when BLG was hydrolyzed previously by the Lb. acidophilus strain. Moreover, in the presence of pectin, the amount of the larger peptide (3.5 kDa) observed in the size exclusion chromatograms was considerably decreased. Our studies showed that prehydrolysis of BLG by Lb. acidophilus CRL 636 had a positive influence on BLG digestibility and that polysaccharides may change the peptide profile yielded by trypsin/chymotrypsin hydrolysis, releasing smaller size peptides, which are known to be less immune-reactive. Moreover, Lb. acidophilus CRL 636 was able to hydrolyze the main epitopes (41-60, 102-124, and 149-162) of BLG, reducing its allergenic content.
Fil: Pescuma, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Dalgalarrondo, Michèle. Institut National de la Recherche Agronomique; Francia
Fil: Haertlé, Thomas. Institut National de la Recherche Agronomique; Francia
Fil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Chobert, Jean Marc. Institut National de la Recherche Agronomique; Francia
Fil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
description An analysis of the peptides generated by hydrolysis of BLG by nonproliferating cells of the strain Lactobacillus acidophilus CRL 636 was carried out. The effect of polysaccharides (pectin, and two EPS synthesized by two Streptococcus thermophilus strains, EPS1190 and EPS804) on BLG digestibility using an in vitro gastric/pancreatic system was analyzed. Polysaccharides are commonly used in the dairy industry to improve food texture; these hydrocolloids may interact with proteins, affecting their digestibility. Nonproliferating cells of Lb. acidophilus CRL 636 were able to hydrolyze 52% of BLG. Twenty-six resulting peptides with molecular masses in the range 544-4119 Da were identified by LC-MS/MS. These peptides resulted mostly from the hydrolysis of the more accessible N-terminal part of BLG. Degradation of BLG by pepsin was poor (8%). When BLG was previously hydrolyzed by Lb. acidophilus CRL 636, peptic hydrolysis was of 54.8%, while when pectin and EPS1190 were added, hydrolysis was higher (58.2 and 57.2%, respectively). Peptides crossing 8 kDa dialysis membranes after trypsin/chymotrypsin hydrolysis were analyzed by HPSEC. The produced peptides were smaller when BLG was hydrolyzed previously by the Lb. acidophilus strain. Moreover, in the presence of pectin, the amount of the larger peptide (3.5 kDa) observed in the size exclusion chromatograms was considerably decreased. Our studies showed that prehydrolysis of BLG by Lb. acidophilus CRL 636 had a positive influence on BLG digestibility and that polysaccharides may change the peptide profile yielded by trypsin/chymotrypsin hydrolysis, releasing smaller size peptides, which are known to be less immune-reactive. Moreover, Lb. acidophilus CRL 636 was able to hydrolyze the main epitopes (41-60, 102-124, and 149-162) of BLG, reducing its allergenic content.
publishDate 2009
dc.date.none.fl_str_mv 2009-06-24
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/54448
Pescuma, Micaela; Hebert, Elvira Maria; Dalgalarrondo, Michèle; Haertlé, Thomas; Mozzi, Fernanda Beatriz; et al.; Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system; American Chemical Society; Journal of Agricultural and Food Chemistry; 57; 12; 24-6-2009; 5571-5577
0021-8561
1520-5118
CONICET Digital
CONICET
url http://hdl.handle.net/11336/54448
identifier_str_mv Pescuma, Micaela; Hebert, Elvira Maria; Dalgalarrondo, Michèle; Haertlé, Thomas; Mozzi, Fernanda Beatriz; et al.; Effect of exopolysaccharides on the hydrolysis of ß-lactoglobulin by lactobacillus acidophilus CRL 636 in an in vitro gastric/pancreatic system; American Chemical Society; Journal of Agricultural and Food Chemistry; 57; 12; 24-6-2009; 5571-5577
0021-8561
1520-5118
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/jf9006505
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/jf9006505
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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