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Volumn 168, Issue 5, 2012, Pages 1035-1050

Optimisation of batch culture conditions for cell-envelope-associated proteinase production from lactobacillus delbrueckii subsp. Lactis ATCC® 7830™

Author keywords

Cell envelope proteinases; Fermentation; Lactobacilli delbrueckii subsp. lactis 313; Optimisation; Process variables

Indexed keywords

AGITATION SPEED; BATCH CULTURE; BATCH GROWTH; CELL-ENVELOPE PROTEINASES; ECONOMIC OPTIMUM; GROWTH MEDIUM; INCUBATION TEMPERATURES; INITIAL PH; INOCULUM SIZE; LACTOBACILLI DELBRUECKII SUBSP. LACTIS 313; LACTOBACILLUS DELBRUECKII; OPTIMAL CONDITIONS; OPTIMISATIONS; PROCESS VARIABLES; PRODUCTION MEDIUM; WHOLE CELL;

EID: 84871928666     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-012-9839-9     Document Type: Article
Times cited : (20)

References (53)
  • 1
    • 77953990216 scopus 로고    scopus 로고
    • Functional and probiotic attributes of an indigenous isolate of Lactobacillus plantarum
    • Kaushik, J. K., Kumar, A., Duary, R. K., Mohanty, A. K., Grover, S., Batish, V. K., et al. (2009). Functional and probiotic attributes of an indigenous isolate of Lactobacillus plantarum. PLoS One, 4, e8099.
    • (2009) PLoS One , vol.4
    • Kaushik, J.K.1    Kumar, A.2    Duary, R.K.3    Mohanty, A.K.4    Grover, S.5    Batish, V.K.6
  • 2
    • 0037213311 scopus 로고    scopus 로고
    • An overview on fermentation, downstream processing and properties of microbial alkaline proteases
    • Gupta, R., Beg, Q. K., Khan, S., & Chauhan, B. (2002). An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Applied Microbiology and Biotechnology, 60, 381-395.
    • (2002) Applied Microbiology and Biotechnology , vol.60 , pp. 381-395
    • Gupta, R.1    Beg, Q.K.2    Khan, S.3    Chauhan, B.4
  • 5
    • 0029810854 scopus 로고    scopus 로고
    • The proteolytic system of Lactobacillus sanfrancisco CB1: Purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase
    • Gobbetti, M., Smacchi, E., & Corsetti, A. (1996). The proteolytic system of Lactobacillus sanfrancisco CB1: purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase. Applied and Environmental Microbiology, 62, 3220-3226.
    • (1996) Applied and Environmental Microbiology , vol.62 , pp. 3220-3226
    • Gobbetti, M.1    Smacchi, E.2    Corsetti, A.3
  • 6
    • 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, T. M. B., Savoy de Giori, G., & Hebert, E. M. (2009). Release of the cell-envelope-associated proteinase of Lactobacillus delbrueckii subspecies lactis CRL 581 is dependent upon pH and temperature. Journal of Agricultural and Food Chemistry, 57, 8607-8611.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 8607-8611
    • Espeche, T.M.B.1    Savoy De Giori, G.2    Hebert, E.M.3
  • 7
    • 33947308748 scopus 로고    scopus 로고
    • Alkaline protease production by submerged fermentation in stirred tank reactor using Bacillus licheniformis NCIM-2042: Effect of aeration and agitation regimes
    • Potumarthi, R., Ch, S., & Jetty, A. (2007). Alkaline protease production by submerged fermentation in stirred tank reactor using Bacillus licheniformis NCIM-2042: effect of aeration and agitation regimes. Biochemical Engineering Journal, 34, 185-192.
    • (2007) Biochemical Engineering Journal , vol.34 , pp. 185-192
    • Potumarthi, R.1    Ch, S.2    Jetty, A.3
  • 8
    • 2942598307 scopus 로고    scopus 로고
    • Optimisation of batch culture conditions for cyclodextrin glucanotransferase production from Bacillus circulans DF 9R
    • Rosso, A. M., Ferrarotti, S. A., Krymkiewicz, N., & Nudel, B. C. (2002). Optimisation of batch culture conditions for cyclodextrin glucanotransferase production from Bacillus circulans DF 9R. Microbial Cell Factories, 1, 3.
    • (2002) Microbial Cell Factories , vol.1 , pp. 3
    • Rosso, M.A.1    Ferrarotti, A.S.2    Krymkiewicz, N.3    Nudel, C.B.4
  • 9
    • 38149049119 scopus 로고    scopus 로고
    • Growth medium selection and its economic impact on plasmid DNA production
    • Danquah, M. K., & Forde, G. M. (2007). Growth medium selection and its economic impact on plasmid DNA production. Journal of Bioscience and Bioengineering, 104, 490-497.
    • (2007) Journal of Bioscience and Bioengineering , vol.104 , pp. 490-497
    • Danquah, M.K.1    Forde, G.M.2
  • 10
    • 45749128307 scopus 로고    scopus 로고
    • Characterization of the pattern of αs1-and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. Lactis CRL 581
    • Hebert, E., Mamone, G., Picariello, G., Raya, R., Savoy, G., Ferranti, P., et al. (2008) Characterization of the pattern of αs1-and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581. Applied and Environmental Microbiology, 74, 3682-3689.
    • (2008) Applied and Environmental Microbiology , vol.74 , pp. 3682-3689
    • Hebert, E.1    Mamone, G.2    Picariello, G.3    Raya, R.4    Savoy, G.5    Ferranti, P.6
  • 12
    • 0742332792 scopus 로고
    • Lactobacilli-their enzymes and role in ripening and spoilage of cheese: A review
    • Khalid, N. M., & Marth, E. H. (1990). Lactobacilli-their enzymes and role in ripening and spoilage of cheese: a review. Journal of Dairy Science, 73, 2669-2684.
    • (1990) Journal of Dairy Science , vol.73 , pp. 2669-2684
    • Khalid, M.N.1    Marth, H.E.2
  • 13
    • 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. (1991). Cell-wall-associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: differential extraction, purification and properties of the enzyme. Applied Microbiology and Biotechnology, 36, 196-204.
    • (1991) Applied Microbiology and Biotechnology , vol.36 , pp. 196-204
    • Laloi, P.1    Atlan, D.2    Blanc, B.3    Gilbert, C.4    Portalier, R.5
  • 14
    • 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. (1994). Purification and characterization of the mature, membrane-associated cell-envelope proteinase of Lactobacillus helveticus L89. Applied Microbiology and Biotechnology, 40, 828-834.
    • (1994) Applied Microbiology and Biotechnology , vol.40 , pp. 828-834
    • Martín-Hernández, M.C.1    Alting, A.C.2    Exterkate, F.A.3
  • 15
    • 78651179880 scopus 로고
    • Survival of lactobacillus leichmannii in relation to vitamin B12 assays
    • Valu, J. A. (1965). Survival of Lactobacillus leichmannii in relation to vitamin B12 assays. Applied and Environmental Microbiology, 13, 486-490.
    • (1965) Applied and Environmental Microbiology , vol.13 , pp. 486-490
    • Valu, J.A.1
  • 17
    • 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., et al. (2007). Isolation, taxonomic identification and hydrogen peroxide production by Lactobacillus delbrueckii subsp. lactis T31, isolated from Mongolian yoghurt: inhibitory activity on food-borne pathogens. Journal of Applied Microbiology, 103, 584-593.
    • (2007) Journal of Applied Microbiology , vol.103 , pp. 584-593
    • Batdorj, B.1    Trinetta, V.2    Dalgalarrondo, M.3    Prévost, H.4    Dousset, X.5    Ivanova, I.6
  • 19
    • 79952698383 scopus 로고    scopus 로고
    • Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides
    • Agyei, D., & Danquah, M. K. (2011). Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides. Biotechnology Advances, 29, 272-277.
    • (2011) Biotechnology Advances , vol.29 , pp. 272-277
    • Agyei, D.1    Danquah, M.K.2
  • 21
    • 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. (1990). Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactococcus lactis subsp. cremoris are related to secondary binding specificity. Applied Microbiology and Biotechnology, 33, 401-406.
    • (1990) Applied Microbiology and Biotechnology , vol.33 , pp. 401-406
    • Exterkate, F.A.1
  • 22
    • 65449153243 scopus 로고    scopus 로고
    • Optimization of physical factors affecting the production of thermo-stable organic solvent-tolerant protease from a newly isolated halo tolerant Bacillus subtilis strain Rand
    • Abusham, R. A., Rahman, R. N., Salleh, A. B., & Basri, M. (2009). Optimization of physical factors affecting the production of thermo-stable organic solvent-tolerant protease from a newly isolated halo tolerant Bacillus subtilis strain Rand. Microbial Cell Factories, 8, 20.
    • (2009) Microbial Cell Factories , vol.8 , pp. 20
    • Abusham, R.A.1    Rahman, R.N.2    Salleh, A.B.3    Basri, M.4
  • 24
    • 23944474776 scopus 로고    scopus 로고
    • Effect of inoculum size on the combined temperature, pH and aw limits for growth of Listeria monocytogenes
    • Koutsoumanis, K. P., & Sofos, J. N. (2005). Effect of inoculum size on the combined temperature, pH and aw limits for growth of Listeria monocytogenes. International Journal of Food Microbiology, 104, 83-91.
    • (2005) International Journal of Food Microbiology , vol.104 , pp. 83-91
    • Koutsoumanis, K.P.1    Sofos, J.N.2
  • 25
    • 0029076810 scopus 로고
    • Medium-dependent regulation of proteinase gene expression in Lactococcus lactis: Control of transcription initiation by specific dipeptides
    • Marugg, J., Meijer, W., van Kranenburg, R., Laverman, P., Bruinenberg, P., & de Vos, W. (1995). Medium-dependent regulation of proteinase gene expression in Lactococcus lactis: control of transcription initiation by specific dipeptides. Journal of Bacteriology, 177, 2982-2989.
    • (1995) Journal of Bacteriology , vol.177 , pp. 2982-2989
    • Marugg, J.1    Meijer, W.2    Van Kranenburg, R.3    Laverman, P.4    Bruinenberg, P.5    De Vos, W.6
  • 26
    • 0023838854 scopus 로고
    • The effect of incubation temperature and inoculum size on growth of salmonellae in minced beef
    • Mackey, B. M., & Kerridge, A. L. (1988). The effect of incubation temperature and inoculum size on growth of salmonellae in minced beef. International Journal of Food Microbiology, 6, 57-65.
    • (1988) International Journal of Food Microbiology , vol.6 , pp. 57-65
    • Mackey, B.M.1    Kerridge, A.L.2
  • 27
    • 80054794338 scopus 로고    scopus 로고
    • Growth and kinetics of Lactobacillus plantarum in the fermentation of edible Irish brown seaweeds
    • Gupta, S. Abu-Ghannam, N. & Scannell, A. G. M. (2011). Growth and kinetics of Lactobacillus plantarum in the fermentation of edible Irish brown seaweeds. Food Bioproducts Process, 89, 345-355.
    • (2011) Food Bioproducts Process , vol.89 , pp. 345-355
    • Gupta, S.1    Abu-Ghannam, N.2    Scannell, A.G.M.3
  • 28
    • 0032787958 scopus 로고    scopus 로고
    • Amelioration of lactic acid production from cheese whey using micro-aeration
    • Tango, M. S. A., & Ghaly, A. E. (1999). Amelioration of lactic acid production from cheese whey using micro-aeration. Biomass Bioenergetics, 17, 221-238.
    • (1999) Biomass Bioenergetics , vol.17 , pp. 221-238
    • Tango, M.S.A.1    Ghaly, A.E.2
  • 29
    • 0021260276 scopus 로고
    • Comparison of aerobic and anaerobic growth of Lactobacillus plantarum in a glucose medium
    • Murphy, M. G., & Condon, S. (1984). Comparison of aerobic and anaerobic growth of Lactobacillus plantarum in a glucose medium. Archives of Microbiology, 138, 49-53.
    • (1984) Archives of Microbiology , vol.138 , pp. 49-53
    • Murphy, M.G.1    Condon, S.2
  • 30
    • 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. (2012). In-depth characterisation of Lactobacillus delbrueckii subsp. lactis 313 for growth and cell-envelope- associated proteinase production. Biochemical Engineering Journal, 64, 61-68.
    • (2012) Biochemical Engineering Journal , vol.64 , pp. 61-68
    • Agyei, D.1    Danquah, M.K.2
  • 31
    • 85054258666 scopus 로고    scopus 로고
    • Lactic acid bacteria: Classification and physiology
    • S. Salminen, A. von Wright, & A. Ouwehand (Eds.), New York: Marcel Dekker
    • Axelsson, L. (2004). Lactic acid bacteria: Classification and physiology. In S. Salminen, A. von Wright, & A. Ouwehand (Eds.), Lactic acid bacteria. Microbiological and functional aspects (pp. 1-66). New York: Marcel Dekker.
    • (2004) Lactic Acid Bacteria, Microbiological and Functional Aspects , pp. 1-66
    • Axelsson, L.1
  • 32
    • 0020607444 scopus 로고
    • Carbohydrate metabolism in lactic acid bacteria
    • Kandler, O. (1983). Carbohydrate metabolism in lactic acid bacteria. Anton Leeuw, 49, 209-224.
    • (1983) Anton Leeuw , vol.49 , pp. 209-224
    • Kandler, O.1
  • 34
    • 0029859396 scopus 로고    scopus 로고
    • Aerobic growth of and activities of NADH oxidase and NADH peroxidase in lactic acid bacteria
    • Sakamoto, M., & Komagata, K. (1996). Aerobic growth of and activities of NADH oxidase and NADH peroxidase in lactic acid bacteria. Journal of Fermentation and Bioengineering, 82, 210-216.
    • (1996) Journal of Fermentation and Bioengineering , vol.82 , pp. 210-216
    • Sakamoto, M.1    Komagata, K.2
  • 35
    • 80052324824 scopus 로고    scopus 로고
    • Effects of agitation speed, temperature, carbon and nitrogen sources on the growth of recombinant Lactococcus lactis NZ9000 carrying domain 1 of aerolysin gene
    • Ibrahim, S. B., Rahman, N. A. A., Mohamad, R., & Rahim, R. A. (2010). Effects of agitation speed, temperature, carbon and nitrogen sources on the growth of recombinant Lactococcus lactis NZ9000 carrying domain 1 of aerolysin gene. African Journal of Biotechnology, 9, 5392-5398.
    • (2010) African Journal of Biotechnology , vol.9 , pp. 5392-5398
    • Ibrahim, S.B.1    Rahman, N.A.A.2    Mohamad, R.3    Rahim, R.A.4
  • 36
    • 84869026022 scopus 로고    scopus 로고
    • Effect of culture conditions on the production of an extracellular protease by Bacillus sp. Isolated from soil sample of Lavizan Jungle Park
    • 2011 (in press)
    • Sepahy, A.A., and L. Jabalameli. (2011). Effect of culture conditions on the production of an extracellular protease by Bacillus sp. isolated from soil sample of Lavizan Jungle Park. Enzyme Res., 2011 (in press).
    • (2011) Enzyme Res
    • Sepahy, A.A.1    Jabalameli, L.2
  • 37
    • 77951876018 scopus 로고    scopus 로고
    • Enhanced productivity of serine alkaline protease by Bacillus sp. Using soybean as substrate
    • Saurabh, S., Jasmine, I., Pritesh, G., & Kumar, S. R. (2007). Enhanced productivity of serine alkaline protease by Bacillus sp. using soybean as substrate. Malaysian Journal of Microbiology, 3, 1-6.
    • (2007) Malaysian Journal of Microbiology , vol.3 , pp. 1-6
    • Saurabh, S.1    Jasmine, I.2    Pritesh, G.3    Kumar, S.R.4
  • 39
    • 18044383152 scopus 로고    scopus 로고
    • Temperature effect on bacterial growth rate: Quantitative microbiology approach including cardinal values and variability estimates to perform growth simulations on/in food
    • Membré, J.-M., Leporq, B., Vialette, M., Mettler, E., Perrier, L., Thuault, D., et al. (2005). Temperature effect on bacterial growth rate: quantitative microbiology approach including cardinal values and variability estimates to perform growth simulations on/in food. International Journal of Food Microbiology, 100, 179-186.
    • (2005) International Journal of Food Microbiology , vol.100 , pp. 179-186
    • Membré, J.-M.1    Leporq, B.2    Vialette, M.3    Mettler, E.4    Perrier, L.5    Thuault, D.6
  • 40
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: From a bioindustrial viewpoint
    • Kumar, C. G., & Takagi, H. (1999). Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnology Advances, 17, 561-594.
    • (1999) Biotechnology Advances , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 41
    • 0037412129 scopus 로고    scopus 로고
    • Effects of temperature, inoculum size and starch hydrolyzate concentration on butanediol production by Bacillus licheniformis
    • Perego, P., Converti, A., & Del Borghi, M. (2003). Effects of temperature, inoculum size and starch hydrolyzate concentration on butanediol production by Bacillus licheniformis. Bioresource Technology, 89, 125-131.
    • (2003) Bioresource Technology , vol.89 , pp. 125-131
    • Perego, P.1    Converti, A.2    Del Borghi, M.3
  • 43
    • 0029853815 scopus 로고    scopus 로고
    • The extracellular acid protease gene of Yarrowia lipolytica: Sequence and pH-regulated transcription
    • Young, T. W., Wadeson, A., Glover, D. J., Quincey, R. V., Butlin, M. J., & Kamei, E. A. (1996). The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription. Microbiology, 142, 2913-2921.
    • (1996) Microbiology , vol.142 , pp. 2913-2921
    • Young, T.W.1    Wadeson, A.2    Glover, D.J.3    Quincey, R.V.4    Butlin, M.J.5    Kamei, E.A.6
  • 44
    • 85040766040 scopus 로고    scopus 로고
    • A review on microbial alkaline proteases
    • Ellaiah, P., Srinivasulu, B., & Adinarayana, K. (2002). A review on microbial alkaline proteases. Anglais, 61, 15.
    • (2002) Anglais , vol.61 , pp. 15
    • Ellaiah, P.1    Srinivasulu, B.2    Adinarayana, K.3
  • 45
    • 64249140141 scopus 로고    scopus 로고
    • Tannase production by Bacillus licheniformis KBR6: Optimization of submerged culture conditions by Taguchi DOE methodology
    • Das Mohapatra, P. K., Maity, C., Rao, R. S., Pati, B. R., & Mondal, K. C. (2009). Tannase production by Bacillus licheniformis KBR6: optimization of submerged culture conditions by Taguchi DOE methodology. Food Research International, 42, 430-435.
    • (2009) Food Research International , vol.42 , pp. 430-435
    • Das Mohapatra, P.K.1    Maity, C.2    Rao, R.S.3    Pati, B.R.4    Mondal, K.C.5
  • 47
    • 0036693775 scopus 로고    scopus 로고
    • Global control of sugar metabolism: A Gram-positive solution
    • Titgemeyer, F., & Hillen, W. (2002). Global control of sugar metabolism: a Gram-positive solution. Anton Leeuwenhoek, 82, 59-71.
    • (2002) Anton Leeuwenhoek , vol.82 , pp. 59-71
    • Titgemeyer, F.1    Hillen, W.2
  • 48
    • 0032975561 scopus 로고    scopus 로고
    • Indication that the Nitrogen source influences both amount and size of exopolysaccharides produced by Streptococcus thermophilus LY03 and modelling of the bacterial growth and exopolysaccharide production in a complex medium
    • Degeest, B., & De Vuyst, L. (1999). Indication that the Nitrogen source influences both amount and size of exopolysaccharides produced by Streptococcus thermophilus LY03 and modelling of the bacterial growth and exopolysaccharide production in a complex medium. Applied and Environmental Microbiology, 65, 2863-2870.
    • (1999) Applied and Environmental Microbiology , vol.65 , pp. 2863-2870
    • Degeest, B.1    De Vuyst, L.2
  • 49
    • 1842739255 scopus 로고    scopus 로고
    • Influence of nutrients on growth and bacteriocin production by Leuconostoc mesenteroides L124 and Lactobacillus curvatus L442
    • Mataragas, M., Drosinos, E. H., Tsakalidou, E., & Metaxopoulos, J. (2004). Influence of nutrients on growth and bacteriocin production by Leuconostoc mesenteroides L124 and Lactobacillus curvatus L442. Anton Leeuwenhoek, 85, 191-198.
    • (2004) Anton Leeuwenhoek , vol.85 , pp. 191-198
    • Mataragas, M.1    Drosinos, E.H.2    Tsakalidou, E.3    Metaxopoulos, J.4
  • 50
    • 84864019493 scopus 로고    scopus 로고
    • Influence of carbon and nitrogen sources on the α-amylase production by a newly isolated thermophilic Streptomyces sp. MSC702 (MTCC 10772)
    • Singh, R., Kapoor, V., & Kumar, V. (2011). Influence of carbon and nitrogen sources on the α-amylase production by a newly isolated thermophilic Streptomyces sp. MSC702 (MTCC 10772). Asian Journal Biotechnology, 3, 540-553.
    • (2011) Asian Journal Biotechnology , vol.3 , pp. 540-553
    • Singh, R.1    Kapoor, V.2    Kumar, V.3
  • 51
    • 0034467795 scopus 로고    scopus 로고
    • Nutritional requirements and nitrogen-dependent regulation of proteinase activity of Lactobacillus helveticus CRL 1062
    • Hebert, E. M., Raya, R. R., & De Giori, G. S. (2000). Nutritional requirements and nitrogen-dependent regulation of proteinase activity of Lactobacillus helveticus CRL 1062. Applied and Environmental Microbiology, 66, 5316-5321.
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 5316-5321
    • Hebert, E.M.1    Raya, R.R.2    De Giori, G.S.3
  • 52
    • 0142040920 scopus 로고    scopus 로고
    • Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10
    • Pastar, I., Tonic, I., Golic, N., Kojic, M., van Kranenburg, R., Kleerebezem, M., et al. (2003). Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10. Applied and Environmental Microbiology, 69, 5802-5811.
    • (2003) Applied and Environmental Microbiology , vol.69 , pp. 5802-5811
    • Pastar, I.1    Tonic, I.2    Golic, N.3    Kojic, M.4    Van Kranenburg, R.5    Kleerebezem, M.6
  • 53


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