اخبار و اعلانات

 آمار

تعداد نشریات24
تعداد شماره‌ها859
تعداد مقالات7,631
تعداد مشاهده مقاله13,515,212
تعداد دریافت فایل اصل مقاله11,637,790
Shahbazi, Mahnaz, Karbalaei-Heidari, Hamid Reza. (1391). A novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties. , 1(2), 45-56. doi: 10.22099/mbrc.2012.576
Mahnaz Shahbazi; Hamid Reza Karbalaei-Heidari. "A novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties". , 1, 2, 1391, 45-56. doi: 10.22099/mbrc.2012.576
Shahbazi, Mahnaz, Karbalaei-Heidari, Hamid Reza. (1391). 'A novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties', , 1(2), pp. 45-56. doi: 10.22099/mbrc.2012.576
Shahbazi, Mahnaz, Karbalaei-Heidari, Hamid Reza. A novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties. , 1391; 1(2): 45-56. doi: 10.22099/mbrc.2012.576

A novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties

Molecular Biology Research Communications
مقاله 2، دوره 1، شماره 2، اسفند 2012، صفحه 45-56    اصل مقاله (188.76 K)
نوع مقاله: Original article
شناسه دیجیتال (DOI): 10.22099/mbrc.2012.576
نویسندگان
Mahnaz Shahbazi؛ Hamid Reza Karbalaei-Heidari*
Molecular Biotechnology Lab, Department of Biology, Faculty of Sciences, Shiraz University, Shiraz 71454, Iran
چکیده
Kinetics of bacterial growth and protease production were monitored on a novel isolated moderately halophilic bacterium, Salinivibrio sp. strain MS-7, and maximum growth and protease activity was achieved after 48 hours at 30°C and 180 rpm. To determine the effect of various carbon sources on protease production, glucose, lactose, sucrose and maltose were investigated and  maximum production of the enzyme was obtained in a basal medium (pH 8.0) containing maltose as a carbon source (494 U/ml). The protease was isolated from a stationary phase culture, purified 3.6-fold with 56% yield by a simple procedure and characterized biochemically. The enzyme revealed a monomeric structure with a relative molecular mass of 21 KDa by running on SDS-PAGE. Maximum caseinolytic activity of the enzyme was observed at 50°C, pH 8.0 and 0–0.5 M NaCl with a high tolerance to salt concentrations of up to 3 M. The effect of various metal ions and inhibitors on caseinolytic activity of the purified protease revealed that it probably belongs to the subclass of serine metalloproteases. These findings suggest that the protease secreted by Salinivibrio sp. strain MS-7 can be introduced as a candidate for biotechnological applications based on its haloalkaline properties.
کلیدواژه‌ها
Salinivibrio sp. strain MS-7؛ Biochemical properties؛ Low molecular weight protease؛ Moderately halophilic bacterium؛ Production optimization
مراجع
  1. Mala M, Srividya S. Partial purification and properties of a laundry detergent compatible alkaline protease from a newly isolated Bacillus species Y. Indian J Microbiol 2010;50: 309-317.
  2. Gupta R, Beg QK, Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol 2002;59:15-32.
  3. Rao MB, Tanksale AM, Ghatge MS, Deshpande VV. Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Biol Rev 1998;62:597-635.
  4. Hough DW, Danson MJ. Extremozymes. Curr Opin Chem Biol 1999;3:39-46.
  5. Margesin R, Schinner F. Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 2001;5:73-83.
  6. Van Den Burg B. Extremophiles as a source for novel enzymes. Curr Opin Microbiol 2003;6:213-218.
  7. Mellado E, Sánchez-Porro C, Martín S, Ventosa A. Extracellular hydrolytic enzymes produced by moderately halophilic bacteria, Halophilic microorganisms. Springer, Berlin, 2004, pp. 285–295.
  8. Sanchez-Porro C, Martin S, Mellado E, Ventosa A. Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes. J Appl Microbiol 2003;94:295-300.
  9. Mellado E, Moore ER, Nieto JJ, Ventosa A. Analysis of 16S rRNA gene sequences of Vibrio costicola strains: description of Salinivibrio costicola gen. nov., comb. nov. Int J Syst Bacteriol 1996;46:817-821.
  10. Huang CY, Garcia JL, Patel BK, Cayol JL, Baresi L, Mah RA. Salinivibrio costicola subsp. vallismortis subsp. nov., a halotolerant facultative anaerobe from Death Valley, and emended description of Salinivibrio costicola. Int J Syst Evol Microbiol 2000;50:615-622.
  11. Romano I, Gambacorta A, Lama L, Nicolaus B, Giordano A. Salinivibrio costicola subsp. alcaliphilus subsp. nov., a haloalkaliphilic aerobe from Campania Region (Italy). Syst Appl Microbiol 2005;28:34-42.
  12. Amoozegar MA, Schumann P, Hajighasemi M, Fatemi AZ, Karbalaei-Heidari HR. Salinivibrio proteolyticus sp. nov., a moderately halophilic and proteolytic species from a hypersaline lake in Iran. Int J Syst Evol Microbiol 2008;58:1159-1163.
  13. Chamroensaksri N, Tanasupawat S, Akaracharanya A, Visessanguan W, Kudo T, Itoh T. Salinivibrio siamensis sp. nov., from fermented fish (pla-ra) in Thailand. Int J Syst Evol Microbiol 2009;59:880-885.
  14. Romano I, Orlando P, Gambacorta A, Nicolaus B, Dipasquale L, Pascual J, Giordano A, Lama L. Salinivibrio sharmensis sp. nov., a novel haloalkaliphilic bacterium from a saline lake in Ras Mohammed Park (Egypt). Extremophiles 2011;15:213-220.
  15. Lama L, Romano I, Calandrelli V, Nicolaus B, Gambacorta A. Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus. Res Microbiol 2005;156:478-484.
  16. Karbalaei-Heidari HR, Ziaee A-A, Schaller J, Amoozegar MA. Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004. Enzyme Microb Technol 2007;40: 266-272.
  17. .Karbalaei-Heidari HR, Ziaee AA, Amoozegar MA. Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents. Extremophiles 2007;11:237-243.
  18. Smibert RM, Krieg NR.  1994. Phenotypic characterization, p. 615.  In P. Gerhardt, R. Murray, W. Wood, and N. Krieg (ed.), Methods for general and molecular bacteriology.  ASM Press, Washington, DC.
  19. Ventosa A, Quesada E, Rodrı´guez-Valera F, Ruiz-Berraquero F, Ramos-Cormenzana A. (1982). Numerical taxonomy of moderately halophilic Gram-negative rods. J Gen Microbiol 128, 1959–1968.
  20. Tamura K, Dudley. J, Neim M. MEGA 4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 2007;24:1596–1599.
  21. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254.
  22. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
  23. Chu WH. Optimization of extracellular alkaline protease production from species of Bacillus. J Ind Microbiol Biotechnol 2007;34:241-245.
  24. Joo HS, Kumar CG, Park GC, Paik SR, Chang CS. Oxidant and SDS-stable alkaline protease from Bacillus clausii I-52: production and some properties. J Appl Microbiol 2003;95:267-272.
  25. Sanchez-Porro C, Mellado E, Bertoldo C, Antranikian G, Ventosa A. Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76. Extremophiles 2003;7:221-228.
  26. Patel R, Dodia M, Singh SP. Extracellular alkaline protease from a newly isolated haloalkaliphilic Bacillus sp.: Production and optimization. Process Biochem 2005;40: 3569-3575.
  27. Karbalaei-Heidari HR, Amoozegar MA, Hajighasemi M, Ziaee AA, Ventosa A. Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis. J Ind Microbiol Biotechnol 2009;36:21-27.
  28. Ningthoujam DS, Kshetri P, Sanasam S, Nimaichand S. Screening, identification of best producers and optimization of extracellular proteases from moderately halophilic alkalithermotolerant indigenous actinomycetes. World Appl Sci J 2009;7:907-916.
  29. Akel H, Al-Quadan F, Yousef TK. Characterization of a purified thermostable protease from hyperthermophilic Bacillus strain HUTBS71. Eur J Sci Res 2009;31:280-288.
  30. Dutta JR, Dutta PK, Baberjee R. Kinetic study of a low molecular weight protease from newly isolated Pseudomonas sp. using artificial neural network. Indian J Biotechnol 2005;4:127-133.
  31. Ningthoujam DS, Kshetri P. A thermostable alkaline protease from a moderately halo-alkalithermotolerant Bacillus Subtilis strain SH1. Aus J Basic and Appl Sci 2010;4:5126-5134.
  32. Deng A, Wu J, Zhang Y, Zhang G, Wen T. Purification and characterization of a surfactant-stable high-alkaline protease from Bacillus sp. B001. Bioresour Technol 2010; 101:7111-7117.
  33. Jellouli K, Ghorbel-Bellaaj O, Ayed HB, Manni L, Agrebi R, Nasri M. Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a detergent additive and for shrimp waste deproteinization. Process Biochem 2011;46: 1248-1256.
  34. Setyorini E, Takenaka S, Murakami S, Aoki K. Purification and characterization of two novel halotolerant extracellular proteases from Bacillus subtilis strain FP-133. Biosci Biotechnol Biochem 2006;70:433-440.
آمار
تعداد مشاهده مقاله: 12,919
تعداد دریافت فایل اصل مقاله: 9,513


سامانه مدیریت نشریات علمی. قدرت گرفته از سیناوب