메뉴 건너뛰기




Volumn 95, Issue , 2013, Pages 323-330

Bioanalytical evaluation of Lactobacillus delbrueckii subsp. lactis 313 cell-envelope proteinase extraction

Author keywords

Cell wall binding; Cell envelope proteinases; Enzyme extraction; Lactobacillus delbrueckii subsp. lactis 313; Proteolytic system

Indexed keywords

CHLORINE COMPOUNDS; CYTOLOGY; ENZYMES; EXTRACTION; LITHIUM COMPOUNDS;

EID: 84876706194     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ces.2013.03.049     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 84865772839 scopus 로고    scopus 로고
    • Carbohydrate utilization affects Lactobacillus delbrueckii subsp. lactis 313 cell-envelope-associated proteinase production
    • Agyei D., Danquah M. Carbohydrate utilization affects Lactobacillus delbrueckii subsp. lactis 313 cell-envelope-associated proteinase production. Biotechnol. Bioprocess Eng. 2012, 17:787-794.
    • (2012) Biotechnol. Bioprocess Eng. , vol.17 , pp. 787-794
    • Agyei, D.1    Danquah, M.2
  • 2
    • 79952698383 scopus 로고    scopus 로고
    • Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides
    • Agyei D., Danquah M.K. Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides. Biotechnol. Adv. 2011, 29:272-277.
    • (2011) Biotechnol. Adv. , vol.29 , pp. 272-277
    • Agyei, D.1    Danquah, M.K.2
  • 3
    • 84859871453 scopus 로고    scopus 로고
    • In-depth characterisation of Lactobacillus delbrueckii subsp. lactis 313 for growth and cell-envelope-associated proteinase production
    • Agyei D., Danquah M.K. In-depth characterisation of Lactobacillus delbrueckii subsp. lactis 313 for growth and cell-envelope-associated proteinase production. Biochem. Eng. J. 2012, 64:61-68.
    • (2012) Biochem. Eng. J. , vol.64 , pp. 61-68
    • Agyei, D.1    Danquah, M.K.2
  • 5
    • 0024400001 scopus 로고
    • Isolation and characterization of aminopeptidase-deficient Lactobacillus bulgaricus mutants
    • Atlan D., Laloi P., Portalier R. Isolation and characterization of aminopeptidase-deficient Lactobacillus bulgaricus mutants. Appl. Environ. Microbiol. 1989, 55:1717-1723.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 1717-1723
    • Atlan, D.1    Laloi, P.2    Portalier, R.3
  • 6
    • 0025334090 scopus 로고
    • X-prolyl-dipeptidyl aminopeptidase of Lactobacillus delbrueckii subsp. bulgaricus: characterization of the enzyme and isolation of deficient mutants
    • Atlan D., Laloi P., Portalier R. X-prolyl-dipeptidyl aminopeptidase of Lactobacillus delbrueckii subsp. bulgaricus: characterization of the enzyme and isolation of deficient mutants. Appl. Environ. Microbiol. 1990, 56:2174-2179.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2174-2179
    • Atlan, D.1    Laloi, P.2    Portalier, R.3
  • 7
    • 34547878370 scopus 로고    scopus 로고
    • Isolation, taxonomic identification and hydrogen peroxide production by Lactobacillus delbrueckii subsp. lactis T31, isolated from Mongolian yoghurt: inhibitory activity on food-borne pathogens
    • Batdorj B., Trinetta V., Dalgalarrondo M., Prévost H., Dousset X., Ivanova I., Haertlé T., Chobert J.M. Isolation, taxonomic identification and hydrogen peroxide production by Lactobacillus delbrueckii subsp. lactis T31, isolated from Mongolian yoghurt: inhibitory activity on food-borne pathogens. J. Appl. Microbiol. 2007, 103:584-593.
    • (2007) J. Appl. Microbiol. , vol.103 , pp. 584-593
    • Batdorj, B.1    Trinetta, V.2    Dalgalarrondo, M.3    Prévost, H.4    Dousset, X.5    Ivanova, I.6    Haertlé, T.7    Chobert, J.M.8
  • 8
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion B.J., Daggett V. The molecular basis for the chemical denaturation of proteins by urea. Proc. Natl. Acad. Sci. 2003, 100:5142-5147.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 9
    • 0021931943 scopus 로고
    • Isolation and partial characterization of the surface protein of Lactobacillus acidophilus strains
    • Bhowmik T., Johnson M.C., Ray B. Isolation and partial characterization of the surface protein of Lactobacillus acidophilus strains. Int. J. Food Microbiol. 1985, 2:311-321.
    • (1985) Int. J. Food Microbiol. , vol.2 , pp. 311-321
    • Bhowmik, T.1    Johnson, M.C.2    Ray, B.3
  • 10
    • 0027169421 scopus 로고
    • Two cell-wall-associated aminopeptidases from Lactobacillus helveticus and the purification and characterization of APII from strain ITGL1
    • Blanc B., Laloi P., Atlan D., Gilbert C., Portalier R. Two cell-wall-associated aminopeptidases from Lactobacillus helveticus and the purification and characterization of APII from strain ITGL1. J. Gen. Microbiol. 1993, 139:1441-1448.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1441-1448
    • Blanc, B.1    Laloi, P.2    Atlan, D.3    Gilbert, C.4    Portalier, R.5
  • 12
    • 0016682862 scopus 로고
    • Improved culture flask for obligate anaerobes
    • Daniels L., Zeikus J.G. Improved culture flask for obligate anaerobes. Appl. Environ. Microbiol. 1975, 29:710-711.
    • (1975) Appl. Environ. Microbiol. , vol.29 , pp. 710-711
    • Daniels, L.1    Zeikus, J.G.2
  • 13
    • 84876713006 scopus 로고    scopus 로고
    • Pharmaceutical applications of bioactive peptides
    • Danquah M.K., Agyei D. Pharmaceutical applications of bioactive peptides. OA Biotechnol. 2012, 1:5.
    • (2012) OA Biotechnol. , vol.1 , pp. 5
    • Danquah, M.K.1    Agyei, D.2
  • 14
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure
    • Desvaux M., Dumas E., Chafsey I., Hébraud M. Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure. FEMS Microbiol. Lett. 2006, 256:1-15.
    • (2006) FEMS Microbiol. Lett. , vol.256 , pp. 1-15
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Hébraud, M.4
  • 15
    • 0000165735 scopus 로고
    • Lactobacillus spp. from Washington state wines: isolation and characterization
    • Edwards C., Powers J., Jensen K., Weller K., Peterson J. Lactobacillus spp. from Washington state wines: isolation and characterization. J. Food Sci. 1993, 58:453-458.
    • (1993) J. Food Sci. , vol.58 , pp. 453-458
    • Edwards, C.1    Powers, J.2    Jensen, K.3    Weller, K.4    Peterson, J.5
  • 17
    • 70349333801 scopus 로고    scopus 로고
    • Release of the cell-envelope-associated proteinase of Lactobacillus delbrueckii subspecies lactis CRL 581 is dependent upon pH and temperature
    • Espeche Turbay M.a.B., Savoy de Giori G., Hebert E.M Release of the cell-envelope-associated proteinase of Lactobacillus delbrueckii subspecies lactis CRL 581 is dependent upon pH and temperature. J. Agric. Food Chem. 2009, 57:8607-8611.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 8607-8611
    • Espeche Turbay, M.1    Savoy de Giori, G.2    Hebert, E.M.3
  • 18
    • 0025087747 scopus 로고
    • Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactococcus lactis subsp. cremoris are related to secondary binding specificity
    • Exterkate F.A. Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactococcus lactis subsp. cremoris are related to secondary binding specificity. Appl. Microbiol. Biotechnol. 1990, 33:401-406.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 401-406
    • Exterkate, F.A.1
  • 19
    • 0034020319 scopus 로고    scopus 로고
    • 2+-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11
    • 2+-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11. Appl. Environ. Microbiol. 2000, 66:2021-2028.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2021-2028
    • Exterkate, F.A.1
  • 20
    • 0032962740 scopus 로고    scopus 로고
    • Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase
    • Exterkate F.A., Alting A.C. Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase. Appl. Environ. Microbiol. 1999, 65:1390-1396.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1390-1396
    • Exterkate, F.A.1    Alting, A.C.2
  • 22
    • 0037979052 scopus 로고    scopus 로고
    • Determination of the domain of the Lactobacillus delbrueckii subsp. bulgaricus cell surface proteinase PrtB involved in attachment to the cell wall after heterologous expression of the PrtB gene in Lactococcus lactis
    • Germond J.-E., Delley M., Gilbert C., Atlan D. Determination of the domain of the Lactobacillus delbrueckii subsp. bulgaricus cell surface proteinase PrtB involved in attachment to the cell wall after heterologous expression of the PrtB gene in Lactococcus lactis. Appl. Environ. Microbiol. 2003, 69:3377-3384.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3377-3384
    • Germond, J.-E.1    Delley, M.2    Gilbert, C.3    Atlan, D.4
  • 23
    • 0037230789 scopus 로고    scopus 로고
    • Evolution of the bacterial species Lactobacillus delbrueckii: a partial genomic study with reflections on prokaryotic species concept
    • Germond J.-E., Lapierre L., Delley M., Mollet B., Felis G.E., Dellaglio F. Evolution of the bacterial species Lactobacillus delbrueckii: a partial genomic study with reflections on prokaryotic species concept. Mol. Biol. Evol. 2003, 20:93-104.
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 93-104
    • Germond, J.-E.1    Lapierre, L.2    Delley, M.3    Mollet, B.4    Felis, G.E.5    Dellaglio, F.6
  • 24
    • 0029941580 scopus 로고    scopus 로고
    • A new cell surface proteinase: sequencing and analysis of the PrtB gene from Lactobacillus delbruekii subsp. bulgaricus
    • Gilbert C., Atlan D., Blanc B., Portailer R., Germond J., Lapierre L., Mollet B. A new cell surface proteinase: sequencing and analysis of the PrtB gene from Lactobacillus delbruekii subsp. bulgaricus. J. Bacteriol. 1996, 178:3059-3065.
    • (1996) J. Bacteriol. , vol.178 , pp. 3059-3065
    • Gilbert, C.1    Atlan, D.2    Blanc, B.3    Portailer, R.4    Germond, J.5    Lapierre, L.6    Mollet, B.7
  • 25
    • 1842414318 scopus 로고    scopus 로고
    • Characterization of a cell membrane-associated proteinase from Lactobacillus helveticus CRL 581
    • Hébert E.M., Raya R., de Giori G.S. Characterization of a cell membrane-associated proteinase from Lactobacillus helveticus CRL 581. Curr. Microbiol. 1997, 35:161-164.
    • (1997) Curr. Microbiol. , vol.35 , pp. 161-164
    • Hébert, E.M.1    Raya, R.2    de Giori, G.S.3
  • 26
    • 0032752644 scopus 로고    scopus 로고
    • A lithium chloride-extracted, broad-spectrum-adhesive 42-kilodalton protein of Staphylococcus epidermidis is ornithine carbamoyltransferase
    • Hussain M., Peters G., Chhatwal G.S., Herrmann M. A lithium chloride-extracted, broad-spectrum-adhesive 42-kilodalton protein of Staphylococcus epidermidis is ornithine carbamoyltransferase. Infect. Immun. 1999, 67:6688-6690.
    • (1999) Infect. Immun. , vol.67 , pp. 6688-6690
    • Hussain, M.1    Peters, G.2    Chhatwal, G.S.3    Herrmann, M.4
  • 27
    • 77954285516 scopus 로고    scopus 로고
    • Differentiation of three Lactobacillus rhamnosus strains (E/N, Oxy and Pen) by SDS-PAGE and two-dimensional electrophoresis of surface-associated proteins
    • Jarocki P., Podlesny M., Wasko A., Siuda A., Targonski Z. Differentiation of three Lactobacillus rhamnosus strains (E/N, Oxy and Pen) by SDS-PAGE and two-dimensional electrophoresis of surface-associated proteins. J. Microbiol. Biotechnol. 2010, 20:558-562.
    • (2010) J. Microbiol. Biotechnol. , vol.20 , pp. 558-562
    • Jarocki, P.1    Podlesny, M.2    Wasko, A.3    Siuda, A.4    Targonski, Z.5
  • 28
    • 64549156088 scopus 로고    scopus 로고
    • Milk-derived bioactive peptides: from science to applications
    • Korhonen H. Milk-derived bioactive peptides: from science to applications. J. Funct. Foods 2009, 1:177-187.
    • (2009) J. Funct. Foods , vol.1 , pp. 177-187
    • Korhonen, H.1
  • 29
    • 0033942365 scopus 로고    scopus 로고
    • Studies on lactate dehydrogenase of Lactobacillus plantarum spp. involved in lactic acid biosynthesis using permeabilized cells
    • Krishnan S., Gowda R., Karanth, N.G.L. Studies on lactate dehydrogenase of Lactobacillus plantarum spp. involved in lactic acid biosynthesis using permeabilized cells. Process Biochem. 2000, 35:1191-1198.
    • (2000) Process Biochem. , vol.35 , pp. 1191-1198
    • Krishnan, S.1    Gowda, R.2    Karanth, N.G.L.3
  • 31
    • 0024404583 scopus 로고
    • Mechanism of proteinase release from Lactococcus lactis subsp. cremoris Wg2
    • Laan H., Konings W.N. Mechanism of proteinase release from Lactococcus lactis subsp. cremoris Wg2. Appl. Environ. Microbiol. 1989, 55:3101-3106.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 3101-3106
    • Laan, H.1    Konings, W.N.2
  • 32
    • 0025999146 scopus 로고
    • Cell-wall-associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: differential extraction, purification and properties of the enzyme
    • Laloi P., Atlan D., Blanc B., Gilbert C., Portalier R. Cell-wall-associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: differential extraction, purification and properties of the enzyme. Appl. Microbiol. Biotechnol. 1991, 36:196-204.
    • (1991) Appl. Microbiol. Biotechnol. , vol.36 , pp. 196-204
    • Laloi, P.1    Atlan, D.2    Blanc, B.3    Gilbert, C.4    Portalier, R.5
  • 33
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee J.C., Timasheff S.N. The stabilization of proteins by sucrose. J. Biol. Chem. 1981, 256:7193-7201.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 34
    • 0028269929 scopus 로고
    • Purification and characterization of the mature, membrane-associated cell-envelope proteinase of Lactobacillus helveticus L89
    • Martín-Hernández M.C., Alting A.C., Exterkate F.A. Purification and characterization of the mature, membrane-associated cell-envelope proteinase of Lactobacillus helveticus L89. Appl. Microbiol. Biotechnol. 1994, 40:828-834.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 828-834
    • Martín-Hernández, M.C.1    Alting, A.C.2    Exterkate, F.A.3
  • 35
    • 0032783298 scopus 로고    scopus 로고
    • Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32
    • Pederson J.A., Mileski G.J., Weimer B.C., Steele J.L. Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32. J. Bacteriol. 1999, 181:4592-4597.
    • (1999) J. Bacteriol. , vol.181 , pp. 4592-4597
    • Pederson, J.A.1    Mileski, G.J.2    Weimer, B.C.3    Steele, J.L.4
  • 37
    • 0036253495 scopus 로고    scopus 로고
    • Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin
    • Rojas M., Ascencio F., Conway P.L. Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin. Appl. Environ. Microbiol. 2002, 68:2330-2336.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2330-2336
    • Rojas, M.1    Ascencio, F.2    Conway, P.L.3
  • 39
    • 56749163205 scopus 로고    scopus 로고
    • Identification of surface-associated proteins in the probiotic bacterium Lactobacillus rhamnosus GG
    • Sánchez B., Bressollier P., Chaignepain S., Schmitter J.-M., Urdaci M.C. Identification of surface-associated proteins in the probiotic bacterium Lactobacillus rhamnosus GG. Int. Dairy J. 2009, 19:85-88.
    • (2009) Int. Dairy J. , vol.19 , pp. 85-88
    • Sánchez, B.1    Bressollier, P.2    Chaignepain, S.3    Schmitter, J.-M.4    Urdaci, M.C.5
  • 40
    • 0344550528 scopus 로고    scopus 로고
    • The cell wall of lactic acid bacteria: surface constituents and macromolecular conformations
    • Schär-Zammaretti P., Ubbink J. The cell wall of lactic acid bacteria: surface constituents and macromolecular conformations. Biophys. J. 2003, 85:4076-4092.
    • (2003) Biophys. J. , vol.85 , pp. 4076-4092
    • Schär-Zammaretti, P.1    Ubbink, J.2
  • 41
    • 0032871626 scopus 로고    scopus 로고
    • Multi-domain, cell-envelope proteinases of lactic acid bacteria
    • Siezen R.J. Multi-domain, cell-envelope proteinases of lactic acid bacteria. Antonie van Leeuwenhoek 1999, 76:139-155.
    • (1999) Antonie van Leeuwenhoek , vol.76 , pp. 139-155
    • Siezen, R.J.1
  • 42
    • 84864384779 scopus 로고    scopus 로고
    • Studying the Effects of Heat and Cold Shock on Cell wall Microstructure and Survival of Some LAB in Milk World
    • Tabatabaie F., Mortazavi A. Studying the Effects of Heat and Cold Shock on Cell wall Microstructure and Survival of Some LAB in Milk World. Appl. Sc. J. 2008, 4:191-194.
    • (2008) Appl. Sc. J. , vol.4 , pp. 191-194
    • Tabatabaie, F.1    Mortazavi, A.2
  • 44
    • 0032899032 scopus 로고    scopus 로고
    • Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: characterization and Specificity for β-casein
    • Tsakalidou E., Anastasiou R., Vandenberghe I., van Beeumen J., Kalantzopoulos G. Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: characterization and Specificity for β-casein. Appl. Environ. Microbiol. 1999, 65:2035-2040.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2035-2040
    • Tsakalidou, E.1    Anastasiou, R.2    Vandenberghe, I.3    van Beeumen, J.4    Kalantzopoulos, G.5
  • 45
    • 0031010519 scopus 로고    scopus 로고
    • Identification and characterization of a basic cell surface-located protein from Lactobacillus fermentum BR11
    • Turner M., Timms P., Hafner L., Giffard P. Identification and characterization of a basic cell surface-located protein from Lactobacillus fermentum BR11. J. Bacteriol. 1997, 179:3310-3316.
    • (1997) J. Bacteriol. , vol.179 , pp. 3310-3316
    • Turner, M.1    Timms, P.2    Hafner, L.3    Giffard, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.