메뉴 건너뛰기




Volumn 28, Issue 8, 2012, Pages 2651-2659

Hydrolytic activity of Virgibacillus sp. SK37, a starter culture of fish sauce fermentation, and its cell-bound proteinases

Author keywords

Cell bound proteinase; Fish sauce fermentation; Moderately halophilic bacterium; Virgibacillus sp.

Indexed keywords

AMINO GROUP; CELL SURFACES; CELL-BOUND PROTEINASE; FERMENTATION PROCESS; FISH MUSCLES; FISH SAUCE; FREEFORMS; HALOPHILIC BACTERIA; HYDROLYTIC ACTIVITIES; POTENTIAL STRAIN; PROTEIN HYDROLYSIS; PROTEOLYTIC ACTIVITIES; SOY PROTEIN ISOLATES; STARTER CULTURES; SYNTHETIC PEPTIDE; VIRGIBACILLUS SP;

EID: 84864061180     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-012-1075-5     Document Type: Article
Times cited : (13)

References (27)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J (1979) Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27: 1256-1262.
    • (1979) J Agric Food Chem , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • S. P. Colowick and N. O. Kaplan (Eds.), New York: Academic Press
    • Barrett AJ, Kirschke H (1981) Cathepsin B, cathepsin H, and cathepsin L. In: Colowick SP, Kaplan NO (eds) Methods in enzymology, vol 80. Academic Press, New York, pp 535-561.
    • (1981) Methods in Enzymology , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 3
    • 0028989722 scopus 로고
    • The 2 Å crystal structure of subtilisin E with PMSF inhibitor
    • Chu N-M, Chao Y, Bi R-C (1995) The 2 Å crystal structure of subtilisin E with PMSF inhibitor. Protein Eng 8: 211-215.
    • (1995) Protein Eng , vol.8 , pp. 211-215
    • Chu, N.-M.1    Chao, Y.2    Bi, R.-C.3
  • 4
    • 70349333801 scopus 로고    scopus 로고
    • Release of the cell-envelope-associated proteinase of Lactobacillus delbrueckii subspecies lactis CRL 581 is dependent upon pH and temperatue
    • Espeche Turbay MB, Savoy de Giori G, Hebert EM (2009) Release of the cell-envelope-associated proteinase of Lactobacillus delbrueckii subspecies lactis CRL 581 is dependent upon pH and temperatue. J Agric Food Chem 57: 8607-8611.
    • (2009) J Agric Food Chem , vol.57 , pp. 8607-8611
    • Espeche Turbay, M.B.1    Savoy de Giori, G.2    Hebert, E.M.3
  • 5
    • 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 66: 2021-2028.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2021-2028
    • Exterkate, F.A.1
  • 7
    • 0033759602 scopus 로고    scopus 로고
    • Streptococcus thermophilus cell wall-anchored proteinase: release, purification, and biochemical and genetic characterization
    • Fernandez-Espla MD, Garault P, Monnet V, Rul F (2000) Streptococcus thermophilus cell wall-anchored proteinase: release, purification, and biochemical and genetic characterization. Appl Environ Microbiol 66: 4772-4778.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4772-4778
    • Fernandez-Espla, M.D.1    Garault, P.2    Monnet, V.3    Rul, F.4
  • 8
    • 0042984801 scopus 로고
    • Membrane-bound proteinases of Halobacterium halobium
    • Fricke B, Parchmann O, Aurich H (1993) Membrane-bound proteinases of Halobacterium halobium. J Basic Microbiol 1: 9-18.
    • (1993) J Basic Microbiol , vol.1 , pp. 9-18
    • Fricke, B.1    Parchmann, O.2    Aurich, H.3
  • 9
    • 0028790890 scopus 로고
    • Unusual chromatographic behavior and one-step purification of a novel membrane proteinase from Bacillus cereus
    • Fricke B, Buchmann T, Friebe S (1995) Unusual chromatographic behavior and one-step purification of a novel membrane proteinase from Bacillus cereus. J Chromatogr 715: 247-258.
    • (1995) J Chromatogr , vol.715 , pp. 247-258
    • Fricke, B.1    Buchmann, T.2    Friebe, S.3
  • 10
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinase or proteinaceous proteinase inhibitors
    • García-Carreño FL, Dimes LE, Haard NF (1993) Substrate-gel electrophoresis for composition and molecular weight of proteinase or proteinaceous proteinase inhibitors. Anal Biochem 214: 65-69.
    • (1993) Anal Biochem , vol.214 , pp. 65-69
    • García-Carreño, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 11
    • 0029941580 scopus 로고    scopus 로고
    • A new cell surface proteinase: sequencing and analysis of the prtB gene from Lactobacillus delbrueckii subsp. bulgaricus
    • Gilbert C, Atlan D, Blanc B, Portailer R, Germond JE, Lapierre L, Mollet B (1996) A new cell surface proteinase: sequencing and analysis of the prtB gene from Lactobacillus delbrueckii subsp. bulgaricus. J Bacteriol 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.E.5    Lapierre, L.6    Mollet, B.7
  • 12
    • 34250842936 scopus 로고    scopus 로고
    • Subtilisin
    • 2nd edn., A. J. Barrett, N. D. Rawlings, and J. F. Woessner (Eds.), Amsterdam: Elsevier Academic Press
    • Graycer TP, Ballinger MD, Wells JA (2004) Subtilisin. In: Barrett AJ, Rawlings ND, Woessner JF (eds) Handbook of proteolytic enzymes, 2nd edn. Elsevier Academic Press, Amsterdam, pp 1786-1792.
    • (2004) Handbook of Proteolytic Enzymes , pp. 1786-1792
    • Graycer, T.P.1    Ballinger, M.D.2    Wells, J.A.3
  • 13
    • 0024404583 scopus 로고
    • Mechanism of proteinase release from Lactococcus lactis subsp. cremoris Wg2
    • Laan H, Konings WN (1989) Mechanism of proteinase release from Lactococcus lactis subsp. cremoris Wg2. Appl Environ Microbiol 55: 3101-3106.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 3101-3106
    • Laan, H.1    Konings, W.N.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 78650156262 scopus 로고    scopus 로고
    • Identification of novel halotolerant bacillopeptidase F-like proteinases from a moderately halophilic bacterium, Virgibacillus sp. SK37
    • Phrommao E, Rodtong S, Yongsawatdigul J (2010) Identification of novel halotolerant bacillopeptidase F-like proteinases from a moderately halophilic bacterium, Virgibacillus sp. SK37. J Appl Microbiol 110: 191-201.
    • (2010) J Appl Microbiol , vol.110 , pp. 191-201
    • Phrommao, E.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 17
    • 0027514727 scopus 로고
    • Characterization of a cell envelope-associated proteinase activity from Streptococcus thermophilus H-strains
    • Shahbal S, Hemme D, Renault P (1993) Characterization of a cell envelope-associated proteinase activity from Streptococcus thermophilus H-strains. Appl Environ Microbiol 59: 177-182.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 177-182
    • Shahbal, S.1    Hemme, D.2    Renault, P.3
  • 18
    • 0032871626 scopus 로고    scopus 로고
    • Multi-domain, cell-envelope proteinases of lactic acid bacteria
    • Siezen RJ (1999) Multi-domain, cell-envelope proteinases of lactic acid bacteria. Antonie van Leeuwenhoek 76: 139-155.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 139-155
    • Siezen, R.J.1
  • 19
    • 34250832681 scopus 로고    scopus 로고
    • NaCl-activated extracellular proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation
    • Sinsuwan S, Rodtong S, Yongsawatdigul J (2007) NaCl-activated extracellular proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation. J Food Sci 72: 264-269.
    • (2007) J Food Sci , vol.72 , pp. 264-269
    • Sinsuwan, S.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 20
    • 38049089790 scopus 로고    scopus 로고
    • Production and characterization of NaCl-activated proteinases from Virgibacillus sp. SK33 isolated from fish sauce fermentation
    • Sinsuwan S, Rodtong S, Yongsawatdigul J (2008a) Production and characterization of NaCl-activated proteinases from Virgibacillus sp. SK33 isolated from fish sauce fermentation. Process Biochem 43: 185-192.
    • (2008) Process Biochem , vol.43 , pp. 185-192
    • Sinsuwan, S.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 21
    • 50449099862 scopus 로고    scopus 로고
    • 2+-activated cell-bound proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation
    • 2+-activated cell-bound proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation. LWT Food Sci Technol 41: 2166-2174.
    • (2008) LWT Food Sci Technol , vol.41 , pp. 2166-2174
    • Sinsuwan, S.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 22
    • 75249107560 scopus 로고    scopus 로고
    • Purification and characterization of a salt-activated and organic solvent-stable heterotrimer proteinase from Virgibacillus sp. SK33 isolated from Thai fish sauce
    • Sinsuwan S, Rodtong S, Yongsawatdigul J (2010a) Purification and characterization of a salt-activated and organic solvent-stable heterotrimer proteinase from Virgibacillus sp. SK33 isolated from Thai fish sauce. J Agric Food Chem 58: 248-256.
    • (2010) J Agric Food Chem , vol.58 , pp. 248-256
    • Sinsuwan, S.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 23
    • 70350564801 scopus 로고    scopus 로고
    • A NaCl-stable serine proteinase from Virgibacillus sp. SK33 isolated from Thai fish sauce
    • Sinsuwan S, Rodtong S, Yongsawatdigul J (2010b) A NaCl-stable serine proteinase from Virgibacillus sp. SK33 isolated from Thai fish sauce. Food Chem 119: 573-579.
    • (2010) Food Chem , vol.119 , pp. 573-579
    • Sinsuwan, S.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 24
    • 79955032408 scopus 로고    scopus 로고
    • Evidence of cell-associated proteinases from Virgibacillus sp. SK33 isolated from fish sauce fermentation
    • Sinsuwan S, Rodtong S, Yongsawatdigul J (2011) Evidence of cell-associated proteinases from Virgibacillus sp. SK33 isolated from fish sauce fermentation. J Food Sci 76: 413-419.
    • (2011) J Food Sci , vol.76 , pp. 413-419
    • Sinsuwan, S.1    Rodtong, S.2    Yongsawatdigul, J.3
  • 25
    • 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 (1999) Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: characterization and specificity for β-casein. Appl Environ Microbiol 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
  • 26
    • 0034045641 scopus 로고    scopus 로고
    • Detection of proteolytic activity by fluorescent zymogram in-gel assays
    • Yasothornsrikul S, Hook VY (2000) Detection of proteolytic activity by fluorescent zymogram in-gel assays. Biotechniques 28: 1166-1173.
    • (2000) Biotechniques , vol.28 , pp. 1166-1173
    • Yasothornsrikul, S.1    Hook, V.Y.2
  • 27
    • 36348961909 scopus 로고    scopus 로고
    • Acceleration of Thai fish sauce fermentation using proteinases and bacterial starter cultures
    • Yongsawatdigul J, Rodtong S, Raksakulthai N (2007) Acceleration of Thai fish sauce fermentation using proteinases and bacterial starter cultures. J Food Sci 72: 382-390.
    • (2007) J Food Sci , vol.72 , pp. 382-390
    • Yongsawatdigul, J.1    Rodtong, S.2    Raksakulthai, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.