Abstract
The newly Tunisian soil-isolated bacterium, producing the alkaline proteinase termed SAPB that was already purified and characterized [1], was assigned as Bacillus pumilus CBS strain on the basis of biochemical properties and 16S rRNA gene sequencing. The maximum protease activity recorded after 24 h of incubation in an optimized medium at 37°C was 6,500 U/mL in shaking flask culture and 25,000 U/mL in fermentor. SAPB showed excellent stability and compatibility in laundry detergent retaining more than 98% of its initial activity after pre-incubation for 1 h at 40°C with Det, followed by OMO (97%), Dinol (94%), and Dixan (93%). Examination of various stained cloth pieces exhibited a remarkable efficiency in the removal of blood and chocolate stains. More interestingly, SAPB demonstrated powerful dehairing capabilities of hair removal from skin with minimal damage on the collagen and a nearly complete feather-degradation. Likewise, Bacillus pumilus CBS effectively degraded feather-meal (98.5%), chicken feather (92%), goat hair (80%), and bovine hair (68%) whereas sheep wool under went less degradation. Keratin-degradation resulted in sulfhdryl group formation (0.95∼3.91 μM).
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Jaouadi, B., S. Ellouz-Chaabouni, M. Rhimi, and S. Bejar (2008) Biochemical and molecular characterization of a detergent-stable serine alkaline protease from Bacillus pumilus CBS with high catalytic efficiency. Biochimie 90: 1291–1305.
Rao, M. B., A. M. Tanksale, M. S. Ghatge, and V. V. Deshpande (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol. Mol. Biol. Rev. 62: 597–635.
Kirk, O., T. V. Borchert, and C. C. Fuglsang (2002) Industrial enzyme applications. Curr. Opin. Biotechnol. 13: 345–351.
Gupta, R., Q. K. Beg, and P. Lorenz (2002) Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 59: 15–32.
Beg, Q. and R. Gupta (2003) Purification and characterization of an oxidation-stable, thiol-dependent serine alkaline protease from Bacillus mojavensis. Enz. Microb. Technol. 32: 294–304.
Maurer, K. H. (2004) Detergent proteases. Curr. Opin. Biotechnol. 15: 330–334.
Coulombe, P. A. and M. B. Omary (2002) ’Hard’ and ’soft’ principles defining the structure, function, and regulation of keratin intermediate filaments. Curr. Opin. Cell. Biol. 14: 110–122
Hess, J. F. and P. G. FitzGerald (2007) Treatment of keratin intermediate filaments with sulfur mustard analogs. Biochem. Biophys. Res. Commun. 359: 616–621.
Papadopoulos, M. C., A. R. El Boushy, A. E. Roodbeen, and E. H. Ketelaars (1986) Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal. Anim. Feed Sci. Technol. 14: 279–290.
Thanikaivelan, P., J. R. Rao, B. U. Nair, and T. Ramasami (2004) Progress and recent trends in biotechnological methods for leather processing. Trends Biotechnol. 22: 181–188.
Son, H. J., H. C. Park, H. S. Kim, and C. Y. Lee (2008) Nutritional regulation of keratinolytic activity in Bacillus pumilis. Biotechnol. Lett. 30: 461–465.
Pillai, P. and G. Archana (2008) Hide depilation and feather disintegration studies with keratinolytic serine protease from a novel Bacillus subtilis isolate. Appl. Microbiol. Biotechnol. 78: 643–650.
Cao, L., H. Tan, Y. Liu, X. Xue, and S. Zhou (2008) Characterization of a new keratinolytic Trichoderma atroviride strain F6 that completely degrades native chicken feather. Lett. Appl. Microbiol. 46: 389–394.
Lee, Y. J., J. H. Kim, H. K. Kim, and J. S. Lee (2004) Production and characterization of keratinase from Paracoccus sp. WJ-98. Biotechnol. Bioprocess Eng. 9: 17–22.
Gurtler, V. and V. A. Stanisich (1996) New approches to typing and identification of bacteria using the 16S–23S rDNA spacer region. Microbiology 142: 3–16.
Sambrook, J., E. Fritsch, and T. Maniatis (1989) Molecular cloning: A laboratory Manual. 2nd ed., pp. 23–38. Cold Spring Harbor Laboratory Press, NY, USA.
Kim, S. J., M. K. Cha, E. Oh, S. M. Kang, J. S. So, and Y. J. Kwon (2005) Use of protease produced by Bacillus sp. SJ-121 for improvement of dyeing quality in wool and silk. Biotechnol. Bioprocess Eng. 10: 186–191.
Lin, Y. C. (1969) Action of proteolytic enzymes on N,N-dimethyl proteins. Basis for a microassay for proteolytic enzymes. J. Biol. Chem. 244: 789–793.
Letourneau, F., V. Soussotte, P. Bressollier, P. Branland, and B. Verneuil (1998) Keratinolytic activity of Streptomyces sp. S.K1-02: a new isolated strain. Lett. Appl. Microbiol. 26: 77–80.
Sellami-Kamoun, A., A. Haddar, N. E. Ali, B. Ghorbel- Frikha, S. Kanoun, and M. Nasri (2008) Stability of thermostable alkaline protease from Bacillus licheniformis RP1 in commercial solid laundry detergent formulations. Microbiol. Res. 163: 299–306.
Banik, R. M. and M. Prakash (2004) Laundry detergent compatibility of the alkaline protease from Bacillus cereus. Microbiol. Res. 159: 135–140.
Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82: 70–77.
Hadj-Ali, N. E., R. Agrebi, B. Ghorbel-Frikha, A. Sellami-Kamoun, S. Kanoun, and M. Nasri (2007) Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated Bacillus licheniformis NH1. Enz. Microb. Technol. 40: 515–523.
Venugopal, M. and A. V. Saramma (2006) Characterization of alkaline protease from Vibrio fluvialis strain VM10 isolated from a mangrove sediment sample and its application as a laundry detergent additive. Proc. Biochem. 41: 1239–1243.
Singh, J., N. Batra, and R. C. Sobti (2001) Serine alkaline protease from a newly isolated Bacillus sp. SSR1. Proc. Biochem. 36: 781–785.
Anwar, A. and M. Saleemuddin (1997) Alkaline-pHacting digestive enzymes of Polyphagous brevis and its characterization as a laundry detergent additive. Proc. Biochem. 35: 213–216.
Banerjee, U., R. Sani, W. Azmi, and R. K. Sani (1999) Thermostable alkaline protease from Bacillus brevis and its characterisation as a laundry detergent additive. Proc. Biochem. 35: 213–219.
Bressollier, P., F. Letourneau, M. Urdaci, and B. Verneuil (1999) Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus. Appl. Environ. Microbiol. 65: 2570–2576.
El-Refai, H. A., M. A. AbdelNaby, A. Gaballa, M. H. El-Araby, and A. F. Abdel Fattah (2005) Improvement of the newly isolated Bacillus pumilus FH9 keratinolytic activity. Proc. Biochem. 40: 2325–2332.
Williams, C. M., C. S. Richter, J. M. Mackenzie, and J. C. Shih (1990) Isolation, Identification, and Characterization of a Feather-Degrading Bacterium. Appl. Environ. Microbial. 56: 1509–1515.
Dayanandan, A., J. Kanagaraj, L. Sounderraj, R. Govindaraju, and G. S. Rajkumar (2003) Application of an alkaline protease in leather processing: an ecofriendly approach. J. Clean. Prod. 11: 533–536.
Grazziotin, A., F. A. Pimentel, S. Sangali, E. V. de Jong, and A. Brandelli (2007) Production of feather protein hydrolysate by keratinolytic bacterium Vibrio sp. kr2. Biores. Technol. 98: 3172–3175.
Kumar, A. G., S. Swarnalatha, S. Gayathri, N. Nagesh, and G. Sekaran (2008) Characterization of an alkaline active-thiol forming extracellular serine keratinase by the newly isolated Bacillus pumilus. J. Appl. Microbiol. 104: 411–419.
Wang, H. Y., D. M. Liu, Y. Liu, C. F. Cheng, Q. Y. Ma, Q. Huang, and Y. Z. Zhang (2007) Screening and mutagenesis of a novel Bacillus pumilus strain producing alkaline protease for dehairing. Lett. Appl. Microbiol. 44: 1–6.
Huang, Q., Y. Peng, X. Li, H. Wang, and Y. Zhang (2003) Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus. Curr. Microbiol. 46: 169–173.
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Jaouadi, B., Ellouz-Chaabouni, S., Ali, M.B. et al. Excellent laundry detergent compatibility and high dehairing ability of the Bacillus pumilus CBS alkaline proteinase (SAPB). Biotechnol Bioproc E 14, 503–512 (2009). https://doi.org/10.1007/s12257-008-0244-8
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DOI: https://doi.org/10.1007/s12257-008-0244-8