메뉴 건너뛰기




Volumn 99, Issue 7, 2016, Pages 5144-5154

Proteolytic activity of Enterococcus faecalis VB63F for reduction of allergenicity of bovine milk proteins

Author keywords

Casein; Milk allergy; Protein hydrolysis; Whey protein

Indexed keywords

ALLERGEN; BACTERIAL PROTEIN; CASEIN; MILK PROTEIN; PEPTIDE HYDROLASE; WHEY PROTEIN;

EID: 84966545993     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2016-11036     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 79959325309 scopus 로고    scopus 로고
    • Proteolytic activities and safety of use of enterococci strains isolated from traditional Azerbaijani dairy products
    • Ahmadova A., Dimov S., Ivanova I., Choiset Y., Chobert J.M., Kuliev A., Haertlé T. Proteolytic activities and safety of use of enterococci strains isolated from traditional Azerbaijani dairy products. Eur. Food Res. Technol. 2011, 233:131-140.
    • (2011) Eur. Food Res. Technol. , vol.233 , pp. 131-140
    • Ahmadova, A.1    Dimov, S.2    Ivanova, I.3    Choiset, Y.4    Chobert, J.M.5    Kuliev, A.6    Haertlé, T.7
  • 4
    • 84883010738 scopus 로고    scopus 로고
    • Milk processing as a tool to reduce cow's milk allergenicity: A mini-review
    • Bu G., Luo Y., Chen F., Liu K., Zhu T. Milk processing as a tool to reduce cow's milk allergenicity: A mini-review. Dairy Sci. Technol. 2013, 93:211-223.
    • (2013) Dairy Sci. Technol. , vol.93 , pp. 211-223
    • Bu, G.1    Luo, Y.2    Chen, F.3    Liu, K.4    Zhu, T.5
  • 5
    • 77955939723 scopus 로고    scopus 로고
    • Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins
    • Bu G., Luo Y., Zhang Y., Chen F. Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins. J. Sci. Food Agric. 2010, 90:2015-2020.
    • (2010) J. Sci. Food Agric. , vol.90 , pp. 2015-2020
    • Bu, G.1    Luo, Y.2    Zhang, Y.3    Chen, F.4
  • 8
    • 0029791731 scopus 로고    scopus 로고
    • Identification of casein as the major allergenic and antigenic protein of cow's milk
    • Docena G.H., Fernandez R., Chirdo F.G., Fossati C.A. Identification of casein as the major allergenic and antigenic protein of cow's milk. Allergy 1996, 51:412-416.
    • (1996) Allergy , vol.51 , pp. 412-416
    • Docena, G.H.1    Fernandez, R.2    Chirdo, F.G.3    Fossati, C.A.4
  • 9
    • 0035315807 scopus 로고    scopus 로고
    • Molecular screening of Enterococcus virulence determinants and potential for genetic exchange between food and medical isolates
    • Eaton T.J., Gasson M.J. Molecular screening of Enterococcus virulence determinants and potential for genetic exchange between food and medical isolates. Appl. Environ. Microbiol. 2001, 67:1628-1635.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1628-1635
    • Eaton, T.J.1    Gasson, M.J.2
  • 13
    • 84899058800 scopus 로고    scopus 로고
    • Oral immunotherapy for food allergy, ready for prime time? Heated egg and milk
    • Feldman M.F., Bird J.A. Oral immunotherapy for food allergy, ready for prime time? Heated egg and milk. Curr. Allergy Asthma Rep. 2014, 14:436. http://dx.doi.org/10.1007/s11882-014-0436-6.
    • (2014) Curr. Allergy Asthma Rep. , vol.14 , pp. 436
    • Feldman, M.F.1    Bird, J.A.2
  • 20
    • 33746733581 scopus 로고    scopus 로고
    • Screening for lactic acid bacteria with potential to reduce antigenic response of β-lactoglobulin in bovine skim milk and sweet whey
    • Kleber N., Weyrich U., Hinrichs J. Screening for lactic acid bacteria with potential to reduce antigenic response of β-lactoglobulin in bovine skim milk and sweet whey. Innov. Food Sci. Emerg. Technol. 2006, 7:233-238.
    • (2006) Innov. Food Sci. Emerg. Technol. , vol.7 , pp. 233-238
    • Kleber, N.1    Weyrich, U.2    Hinrichs, J.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 80051591771 scopus 로고    scopus 로고
    • Comparative analysis of β-casein proteolysis by PrtP proteinase from Lactobacillus paracasei ssp. paracasei BGHN14, PrtR proteinase from Lactobacillus rhamnosus BGT10 and PrtH from Lactobacillus helveticus BGRA43
    • Lozo J., Strahinic I., Dalgalarrondo M., Chobert J.M., Haertlé T., Topisirovic L. Comparative analysis of β-casein proteolysis by PrtP proteinase from Lactobacillus paracasei ssp. paracasei BGHN14, PrtR proteinase from Lactobacillus rhamnosus BGT10 and PrtH from Lactobacillus helveticus BGRA43. Int. Dairy J. 2011, 21:863-868.
    • (2011) Int. Dairy J. , vol.21 , pp. 863-868
    • Lozo, J.1    Strahinic, I.2    Dalgalarrondo, M.3    Chobert, J.M.4    Haertlé, T.5    Topisirovic, L.6
  • 25
  • 26
    • 84871804330 scopus 로고    scopus 로고
    • Biotechnological and safety characterization of Enterococcus lactis, a recently described species of dairy origin
    • Morandi S., Silvetti Y., Brasca M. Biotechnological and safety characterization of Enterococcus lactis, a recently described species of dairy origin. Antonie Van Leeuwenhoek 2013, 103:239-249.
    • (2013) Antonie Van Leeuwenhoek , vol.103 , pp. 239-249
    • Morandi, S.1    Silvetti, Y.2    Brasca, M.3
  • 27
    • 84886294840 scopus 로고    scopus 로고
    • Metabolomics as a tool for the comprehensive understanding of fermented and functional foods with lactic acid bacteria
    • Mozzi F., Ortiz M.E., Bleckwedel J., De Vuyst L., Pescuma M. Metabolomics as a tool for the comprehensive understanding of fermented and functional foods with lactic acid bacteria. Food Res. Int. 2013, 54:1152-1161.
    • (2013) Food Res. Int. , vol.54 , pp. 1152-1161
    • Mozzi, F.1    Ortiz, M.E.2    Bleckwedel, J.3    De Vuyst, L.4    Pescuma, M.5
  • 28
    • 8744308881 scopus 로고    scopus 로고
    • Cow's milk allergens identification by two-dimensional immunoblotting and mass spectrometry
    • Natale M., Bisson C., Monti G. Cow's milk allergens identification by two-dimensional immunoblotting and mass spectrometry. Mol. Nutr. Food Res. 2004, 48:363-369.
    • (2004) Mol. Nutr. Food Res. , vol.48 , pp. 363-369
    • Natale, M.1    Bisson, C.2    Monti, G.3
  • 29
    • 0034937341 scopus 로고    scopus 로고
    • Detection of extracellular bound proteinase in EPS-producing lactic acid bacteria cultures on skim milk agar
    • Pailin T., Kang D.H., Schmidt K., Fung D.Y.C. Detection of extracellular bound proteinase in EPS-producing lactic acid bacteria cultures on skim milk agar. Lett. Appl. Microbiol. 2001, 33:45-49.
    • (2001) Lett. Appl. Microbiol. , vol.33 , pp. 45-49
    • Pailin, T.1    Kang, D.H.2    Schmidt, K.3    Fung, D.Y.C.4
  • 31
    • 33646494005 scopus 로고    scopus 로고
    • Effect of combined high pressure and enzymatic treatment on the hydrolysis and immuno-reactivity of dairy whey proteins
    • Peñas E., Prestamo G., Baeza M.L., Martinez-Molero M.I., Gomez R. Effect of combined high pressure and enzymatic treatment on the hydrolysis and immuno-reactivity of dairy whey proteins. Int. Dairy J. 2006, 16:831-839.
    • (2006) Int. Dairy J. , vol.16 , pp. 831-839
    • Peñas, E.1    Prestamo, G.2    Baeza, M.L.3    Martinez-Molero, M.I.4    Gomez, R.5
  • 32
    • 84860178238 scopus 로고    scopus 로고
    • Diversity in growth and protein degradation by dairy relevant lactic acid bacteria species in reconstituted whey
    • Pescuma M., Hebert E.M., Bru E., Valdez G.F., Mozzi F. Diversity in growth and protein degradation by dairy relevant lactic acid bacteria species in reconstituted whey. J. Dairy Res. 2012, 79:201-208.
    • (2012) J. Dairy Res. , vol.79 , pp. 201-208
    • Pescuma, M.1    Hebert, E.M.2    Bru, E.3    Valdez, G.F.4    Mozzi, F.5
  • 33
    • 84908143975 scopus 로고    scopus 로고
    • Lactobacillus delbrueckii ssp. bulgaricus CRL454 cleaves allergenic peptides of β-lactoglobulin
    • Pescuma M., Hebert E.M., Haertlé T., Chobert J.M., Mozzi F., Valdez G.F. Lactobacillus delbrueckii ssp. bulgaricus CRL454 cleaves allergenic peptides of β-lactoglobulin. Food Chem. 2015, 170:407-414.
    • (2015) Food Chem. , vol.170 , pp. 407-414
    • Pescuma, M.1    Hebert, E.M.2    Haertlé, T.3    Chobert, J.M.4    Mozzi, F.5    Valdez, G.F.6
  • 34
  • 36
    • 0035038936 scopus 로고    scopus 로고
    • Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF
    • Qin X., Singh K.V., Weinstock G.M., Murray B.E. Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF. J. Bacteriol. 2001, 183:3372-3382.
    • (2001) J. Bacteriol. , vol.183 , pp. 3372-3382
    • Qin, X.1    Singh, K.V.2    Weinstock, G.M.3    Murray, B.E.4
  • 39
    • 26644438794 scopus 로고    scopus 로고
    • Rapid identification of dairy lactic acid bacteria by M13-generated, RAPD-PCR fingerprint databases
    • Rossetti L., Giraffa G. Rapid identification of dairy lactic acid bacteria by M13-generated, RAPD-PCR fingerprint databases. J. Microbiol. Methods 2005, 63:135-144.
    • (2005) J. Microbiol. Methods , vol.63 , pp. 135-144
    • Rossetti, L.1    Giraffa, G.2
  • 41
    • 77950863806 scopus 로고    scopus 로고
    • Evaluation of metabolic activities of enterococci isolated from Pecorino Abruzzese cheese
    • Serio A., Chaves-López C., Paparella A., Suzzi G. Evaluation of metabolic activities of enterococci isolated from Pecorino Abruzzese cheese. Int. Dairy J. 2010, 20:459-464.
    • (2010) Int. Dairy J. , vol.20 , pp. 459-464
    • Serio, A.1    Chaves-López, C.2    Paparella, A.3    Suzzi, G.4
  • 42
    • 0034973596 scopus 로고    scopus 로고
    • Role of Enterococcus faecalis surface protein esp in the pathogenesis of ascending urinary tract infection
    • Shankar N., Lockatell C.V., Baghayan A.S., Drachenberg C., Gilmore M.S., Johnson D.E. Role of Enterococcus faecalis surface protein esp in the pathogenesis of ascending urinary tract infection. Infect. Immun. 2001, 69:4366-4372.
    • (2001) Infect. Immun. , vol.69 , pp. 4366-4372
    • Shankar, N.1    Lockatell, C.V.2    Baghayan, A.S.3    Drachenberg, C.4    Gilmore, M.S.5    Johnson, D.E.6
  • 43
    • 0032950027 scopus 로고    scopus 로고
    • Cow's milk protein-specific IgE concentrations in two age groups of milk-allergic children and in children achieving clinical tolerance
    • Sicherer S.H., Sampson H.A. Cow's milk protein-specific IgE concentrations in two age groups of milk-allergic children and in children achieving clinical tolerance. Clin. Exp. Allergy 1999, 29:507-512.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 507-512
    • Sicherer, S.H.1    Sampson, H.A.2
  • 46
    • 5444253691 scopus 로고    scopus 로고
    • Development of a multiplex PCR for the detection of asa1gelEcylAesp, and hyl genes in Enterococci and survey for virulence determinants among European hospital isolates of Enterococcus faecium.
    • Vankerckhoven V., van Autgaerden T., Vael C., Lammens C., Chapelle S., Rossi R., Jabes D., Goznes H. Development of a multiplex PCR for the detection of asa1gelEcylAesp, and hyl genes in Enterococci and survey for virulence determinants among European hospital isolates of Enterococcus faecium. J. Clin. Microbiol. 2004, 42:4473-4479.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 4473-4479
    • Vankerckhoven, V.1    van Autgaerden, T.2    Vael, C.3    Lammens, C.4    Chapelle, S.5    Rossi, R.6    Jabes, D.7    Goznes, H.8
  • 47
    • 0034795756 scopus 로고    scopus 로고
    • Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy
    • Vila L., Beyer K., Jarvinen K.M., Chatchatee P., Bardina L., Sampson H.A. Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy. Clin. Exp. Allergy 2001, 31:1599-1606.
    • (2001) Clin. Exp. Allergy , vol.31 , pp. 1599-1606
    • Vila, L.1    Beyer, K.2    Jarvinen, K.M.3    Chatchatee, P.4    Bardina, L.5    Sampson, H.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.