References
- Layman, P. L. (1986) Industrial enzymes: battling to remain specialties. Chem. Engineer. News 64: 11-14.
- Kumar, C. G. and H. Takagi (1999) Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnol. Adv. 17: 561-594. https://doi.org/10.1016/S0734-9750(99)00027-0
- Kirk, O., T. V. Borchert, and C. C. Fuglsang (2002) Industrial enzyme applications. Curr. Opin. Biotechnol. 13: 345-351. https://doi.org/10.1016/S0958-1669(02)00328-2
- Samal, B. B., B. Karan, and Y. Stabinsky (1990) Stability of two novel serine proteinases in commercial laundry detergent formulations. Biotechnol. Bioeng. 28: 609-612.
- Phadatare, S. U., V. V. Deshpande, and M. C. Srinvasan (1993) High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): enzyme production and compatibility with commercial detergents. Enz. Microb. Technol. 15: 72-76. https://doi.org/10.1016/0141-0229(93)90119-M
- Tunlid, A., S. Rosen, B. Ek, and L. Rask (1994) Purification and characterization of an extracellular serine protease from the nematode-trapping fungus Arthrobotrys oligospora. Microbiol. 140: 1687-1695. https://doi.org/10.1099/13500872-140-7-1687
- Jacobs, M. F. (1995) Expression of the subtilisin carlsbergencoding gene in Bacillus licheniformis and Bacillus subtilis. Gene 152: 67-74.
- Ito, S., T. Kobayashi, K. Ara, K. Ozaki, S. Kawai, and Y. Hatada (1998) Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures. Extremophiles 2: 185-190 https://doi.org/10.1007/s007920050059
- Manachini, P. L. and M. G. Fortina (1998) Production in sea-water of thermostable alkaline proteases by a halotolerant strain of Bacillus licheniformis. Biotechnol. Lett. 20: 565-568. https://doi.org/10.1023/A:1005349728182
- Banerjee, U. C., R. K. Sani, W. Azmi, and R. Soni (1999) Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive. Process Biochem. 35: 213-219. https://doi.org/10.1016/S0032-9592(99)00053-9
- Yang, J. K., I. L. Shih, Y. M. Tzeng, and S. L. Wang (2000) Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes. Enz. Microb. Technol. 26: 406-413. https://doi.org/10.1016/S0141-0229(99)00164-7
- Joo, H. S., C. G. Kumar, G. C. Park, S. R. Paik, and C. S. Chang (2002) Optimization of the production of an extracellular alkaline protease from Bacillus horikoshii. Process Biochem. 38: 155-159. https://doi.org/10.1016/S0032-9592(02)00061-4
- Joo, H. S., C. G. Kumar, G. C. Park, S. R. Paik, and C. S. Chang (2003) Oxidant and SDS-stable alkaline protease from Bacillus clausii I-52: production and some properties. J. Appl. Microbiol. 95: 267-272. https://doi.org/10.1046/j.1365-2672.2003.01982.x
- Joo, H. S., C. G. Kumar, G. C. Park, S. R. Paik, and C. S. Chang (2004) Bleach-resistant alkaline protease produced by a Bacillus sp. isolated from the Korean polychaeta, Periserrula leucophryna. Process Biochem. 39: 1441-1447. https://doi.org/10.1016/S0032-9592(03)00260-7
- Maurer, K. H. (2004) Detergent proteases. Curr. Opin. Biotechnol. 15: 330-334. https://doi.org/10.1016/j.copbio.2004.06.005
- Joo, H. S. and C. S. Chang (2005a) Production of protease from a new alkalophilic Bacilus sp. I-312 grown on soybean meal: optimization and some properties. Process Biochem. 40: 1263-1270 https://doi.org/10.1016/j.procbio.2004.05.010
- Gessesse, A. (1997) The use of nug meal as low-cost substrate for the production of alkaline protease by the alkaliphilic Bacillus sp. AR-009 and some properties of the enzyme. Bioresour. Technol. 62: 59-61. https://doi.org/10.1016/S0960-8524(97)00059-X
- 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.
- Horikoshii, K. (1999) Alkalophiles: some applications of their products for biotechnology. Microbiol. Mol. Biol. Rev. 63: 735-750
- Kumar, C. G., M. P. Tiwari, and K. D. Jany (1999) Novel alkaline serine proteases from alkalophilic Bacillus sp.: purification and characterization. Process Biochem. 34: 441-449. https://doi.org/10.1016/S0032-9592(98)00110-1
- Saeki, K., K. Ozaki, T. Kobayashi, and S. Ito (2007) Detergent alkaline proteases: enzymatic properties, genes, and crystal structures. J. Biosci. Bioeng. 103: 501-508. https://doi.org/10.1263/jbb.103.501
- Johnvesly, B. and G. R. Naik (2001) Studies on production of thermostable alkaline protease from thermophilic and alkaliphilic Bacillus sp. JB-99 in a chemically defined medium. Process Biochem. 37: 139-144. https://doi.org/10.1016/S0032-9592(01)00191-1
- Uyar, F. and Z. Baysal (2004) Production and optimization of process parameters for alkaline protease production by a newly isolated Bacillus sp. under solid state fermentation. Process Biochem. 39: 1893-1898. https://doi.org/10.1016/j.procbio.2003.09.016
- Haddar, A., N. Fakhfakh-Zouari, N. Hmidet, F. Frikha, M. Nasri, and A. S. Kamoun (2010) Low-cost fermentation medium for alkaline protease production by Bacillus mojavensis A21 using hulled grain of wheat and sardinella peptone. J. Biosci. Bioengineer. 110: 288-294. https://doi.org/10.1016/j.jbiosc.2010.03.015
- Hameed, A., T. Keshavarz, and C. S. Evans (1999) Effect of dissolved oxygen tension and pH on the production of extracellular protease from a new isolate of Bacillus subtilis K2, for use in leather processing. J. Chem. Technol. Biotechnol. 74: 5-8. https://doi.org/10.1002/(SICI)1097-4660(199901)74:1<5::AID-JCTB979>3.0.CO;2-T
- Christiansen, T. and J. Nielsen (2002) Production of extracellular protease and glucose uptake in Bacillus clausii in steady-state transient continuous cultures. J. Biotechnol. 97: 265-273. https://doi.org/10.1016/S0168-1656(02)00109-8
- Calik, P., E. Celik, E. T. Ilkin, C. Oktar, and E. Ozdemir (2003) Protein-based complex medium design for recombinant serine alkaline protease production. Enz. Microb. Technol. 33: 975-986. https://doi.org/10.1016/j.enzmictec.2003.07.002
- Ramnani, P. and R. Gupta (2004) Optimization of medium composition for keratinase production by Bacillus licheniformis RG1 using statistical methods involving response surface methodology. Biotechnol. Appl. Biochem. 40: 191-196 https://doi.org/10.1042/BA20030228
- Rai, S. K. and A. K. Mukherjee (2010) Statistical optimization of production, purification and industrial application of a laundry detergent and organic solvent-stable subtilisin-like serine protease (Alzwiprase) from Bacillus subtilis DM-04. Biochem. Eng. J. 48: 173-180. https://doi.org/10.1016/j.bej.2009.09.007
- Gupta, R., Q. K. Beg, S. Khan, and B. Chauhan (2002) An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl. Microbiol. Biotechnol. 60: 381-395. https://doi.org/10.1007/s00253-002-1142-1
- Bryan, P. N. (2000) Protein engineering of subtilisin. Biochim. Biophys. Acta. 1543: 203-222. https://doi.org/10.1016/S0167-4838(00)00235-1
- Estell, D. D., T. P. Graycar, and J. A. Wells (1985) Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J. Biol. Chem. 260: 6518-6521.
- Ness, J. E., M. Welch, L. Giver, M. Bueno, J. R. Cherry, T. V, Borchert, W. P. C. Stemmer, and J. Minshull (1999) DNA shuffling of subgenomic sequences of subtilisin. Nat. Biotechnol. 17: 893-896. https://doi.org/10.1038/12884
- Davis, B. G., K. Khumtaveeporn, R. R. Bott, and J. B. Jones (1999) Altering the specificity of subtilisin Bacillus lentus through the introduction of positive charge at single amino acid sites. Bioorg. Med. Chem. 7: 2303-2311. https://doi.org/10.1016/S0968-0896(99)00168-6
- Bhosale, S. H., M. B. Rao, V. V. Deshpande, and M. C. Srinivasan (1995) Thermostability of high activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20). Enz. Microb. Technol. 17: 136-139. https://doi.org/10.1016/0141-0229(94)00045-S
- Becker, T., G. Park, and A. L. Gaertner (1997) Formulating of detergent enzymes. Surfactant Sci. Ser. 69: 299-325.
- Kumar, C. G., R. K., Malik, and M. P. Tiwari (1998) Novel enzyme-based detergents: an Indian perspective. Curr. Sci. 75: 1312-1318.
- Joo, H. S., Y. M. Koo, J. W. Choi, and C. S. Chang (2005) Stabilization method of an alkaline protease from inactivation by heat, SDS and hydrogen peroxide. Enz. Microb. Technol. 36: 766-772. https://doi.org/10.1016/j.enzmictec.2005.01.002
- Joo, H. S. and C. S. Chang (2005b) Oxidant and SDS-stable alkaline protease from a halo-tolerant Bacillus clausii I-52: enhanced production and simple purification. J. Appl. Microbiol. 98: 491-497. https://doi.org/10.1111/j.1365-2672.2004.02464.x
- Joo, H. S. and C. S. Chang (2006) Production of an oxidant and SDS-stable alkaline protease from an alkaophilic Bacillus clausii I-52 by submerged fermentation: feasibility as a laundry detergent additive. Enz. Microb. Technol. 38: 176-183. https://doi.org/10.1016/j.enzmictec.2005.05.008
- Joo, H. S. and J. W. Choi (2011) Cloning and expression of a alkaline protease from Bacillus clausii I-52. J. Agri. Life Sci. 45: 201-212.
- Joo, H. S., D. C. Park, and J. W. Choi (2012) Increased production of an alkaline protease from Bacillus clausii I-52 by chromosomal integration. J. Agri. Life Sci. 46: 163-176.
- Gonzalez, G., C. Gonzalez, and P. Merino (1992) Thermotabilization of Cucurbita ficifolia protease in the presence of additives. Biotechnol. Lett. 14: 919-924. https://doi.org/10.1007/BF01020629
- Han, X. Q. and S. Damodran (1997) Stability of protease Q against autolysis and in sodium dodecyl sulfate and urea solutions. Biochem. Biophys. Res. Comm. 240: 839-843. https://doi.org/10.1006/bbrc.1997.7698
- Otzen, D. E. (2002) Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature. Biophys. J. 83: 2219-2230. https://doi.org/10.1016/S0006-3495(02)73982-9
- Siezen, R. J. and J. A. M. Leunissen (1997) Subtilases: the superfamily of subtilisin like serine proteases. Protein Sci. 6: 501-523.
- Kembhavi, A. A., A. Kulkarni, and A. Pant (1993) Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64. Appl. Biochem. Biotechnol. 38: 83-92. https://doi.org/10.1007/BF02916414
-
Lee, S. and D. J. Jang (2001) Progressive rearrangement of subtilisin carlsberg into orderly and inflexible conformation with
$Ca^{2+}$ binding. Biophys. J. 81: 2972-2978. https://doi.org/10.1016/S0006-3495(01)75937-1 - Ghorbel, B., A. Sellami-Kamoun, and M. Nasri (2003) Stability studies of protease from Bacillus cereus BG1. Enz. Microbial Technol. 32: 513-518. https://doi.org/10.1016/S0141-0229(03)00004-8
- Hajji, M., S. Kanoun, M. Nasri, and N. Gharsallah (2007) Purification and characterization of an alkaline serine-protease produced by a new isolated Aspergillus clavatus ES1. Process Biochem. 42: 791-797. https://doi.org/10.1016/j.procbio.2007.01.011
- Stoner, M. R., D. A. Dale, P. J. Gualfetti, T. Becker, M. C. Manning, and J. F. Carpenter (2004) Protease autolysis in heavyduty liquid detergent formulations: effect of thermodynamic stabilizers and protease inhibitors. Enz. Microb. Technol. 34: 114-125. https://doi.org/10.1016/j.enzmictec.2003.09.008
- Kravetz, L. and K. F. Guin (1985) Effect of surfactant structure on stability of enzymes formulated into laundry liquids. J. Am. Oil Chem. Soc. 62: 943-949. https://doi.org/10.1007/BF02541765
- Lalonde, J., E. J. Witte, and M. L. Oconnell (1995) Protease stabilization by highly concentrated anionic surfactant mixtures. J. Am. Oil Chem. Soc. 52: 53-59.
- Kotomin, A. A., M. B. Petelskii, A. A. Abramzon, A. E. Punin, and O. D. Yakimchuk (2001) Optimization of the component concentrations in solutions of synthetic detergents. Russ. J. Appl. Chem. 74: 2038-2042.
- Kumar, D., S. N. Thakur, R. Verma, and T. C. Bhalla (2008) Microbial proteases and application as laundry detergent additive. Res. J. Microbiol. 3: 661-672. https://doi.org/10.3923/jm.2008.661.672
- Sekhon, B. S. and M. K. Sangha (2004) Detergents-zeolites and enzymes excel cleaning power. Resonance 9: 35-45. https://doi.org/10.1007/BF02837576
- Russell, G. L. and L. M. Britton (2002) Use of certain alcohol ethoxyates to maintain protease stability in the presence of anionic surfactants. J. Surfact. Detergent 5: 5-10. https://doi.org/10.1007/s11743-002-0198-9