Proteases of Bacillus subtilis

Puhan, Z. and Irvine, D. M. 1973. Proteolysis by proteases of Bacillus subtilis used to make Canadian Cheddar cheese. J. Dairy Sci. 56, 317-322. 

Bovine lung or mucous QAE Sephadex A50 Proteases of Bacillus subtilis Proteolytic enzymes from pig pancreas... 

Varela H, Ferrari MD, Belobradjic L et al. (1997) Skin unhairing proteases of Bacillus subtilis production and partial characterization. Biotechnol Lett 19 755-758 Verduyn C, Zomerdijk TPL, van Etijken JHP et al. (1984) Continuous measurement of ethanol production by aerobic yeast suspensions with an enzyme electrode. J Appl Microbiol Biotechnol 19(3) 181-185... 

Varela, H., Ferrai, M. D., Belobrajdic, L., Vazquez, A., Loperena, M. L. Skin unhairing proteases of Bacillus subtilis, production and partial characterization. Biotechnol Lett 1997, 19,755-758. 

Isolation of a-amylase and protease from Bacillus subtilis fermentation broth [20]... 

Murashima, K., Chen, C.-L., Kosugi, A. et al. (2002) Heterologous production of Clostridium cellulovorans engB, using protease-deficient Bacillus subtilis, and preparation of active recombinant cellulosomes. Journal of Bacteriology, 184 (1), 76-81. 

More recently, the chemo-enzymatic synthesis of inulin-containing hydrogels was reported [54]. The key point was the solubility of inulin [a mixture of oligomers and polymers containing 2-60 (or more) 5-2,1 linked D-fructose molecules having a glucose unit as the initial residue] in dimethylformamide (DMF), a fact that allowed its esterification by action of a protease from Bacillus subtilis. 

Tanaka, T. Kawata, M. Gloning and characterization of Bacillus subtilis iep, which has positive and negative effects on production of extracellular proteases. J. Bacteriol., 170, 3593-3600 (1988)... 

Carbohydrase and Protease, Mixed (Bacillus subtilis var. including Bacillus amyloliquefaciens) Produced as an off white to tan, amorphous powder or as a liquid by controlled fermentation using Bacillus subtilis var. Soluble in water (the solution is usually light yellow to dark brown), but practically insoluble in alcohol, in chloroform, and in ether. Major active principles (1) a-amylase, (2) /3-glucanase, (3) protease, and (4) pentosanase. Typical applications used in the preparation of starch syrups, alcohol, beer, dextrose, bakery products, and fishmeal in the tenderizing of meat and in the preparation of protein hydrolysates. 

Enzyme-catalyzed hydrolysis, exploiting the esterase activity of proteases such as trypsin and chymotrypsint ° l or carboxypeptidase has opened alternative routes to the deprotection of several peptide methyl, ethyl, and ferf-butyl esters. In fact, methyl, ethyl, and benzyl esters are successfully hydrolyzed from protected peptides using the alkaline protease from Bacillus subtilis or alcalase from Bacillus licheniformis which accepts... 

An enzyme which generally displays a high esterase/protease ratio, such as the alkaline protease from Bacillus subtilis DY, selectively removes methyl, ethyl, and benzyl esters from a variety of Trt-, Z-, and Boc-protected di- and tripeptides and a pentapeptide at pH 8 and 37 °C (Scheme 14).P9]... 

Deprotenized mbber (DPNR) — this is very useful when low water absorption is wanted, vulcanizates with low creep are needed, or more than ordinary reproducibility is required. Normally NR has between 0.25 and 0.5% nitrogen as protein DPNR has only about 0.07%. A drawback is that since protein matter in the mbber accelerates cure, DPNR requires more acceleraticm. DPNR is made by treating NR latex with bioenzyme, which hydrolyzes the proteins to water-soluble forms. A protease like Bacillus subtilis is used at about 0.3 phr. When the enzymolysis is completed the latex is diluted to 3% total soUds and coagulated by adding a mixture of phosphoric and sulfuric acid. The coagulated mbber is then pressed free of most of the water, cmmbed, dried, and baled. 

Figure 18-9. C-terminal deprotection of peptide esters by the alkaline protease from Bacillus subtilis DY and alcalase.

The transesterifications of divinyl adipate with glucose in DMF catalyzed by alkaline protease from Bacillus subtilis at various water contents were examined. The enzymatic reaction by the Bacillus protease was carried out in the presence of more than 2% water and maximum reaction rate was observed at a water content of 20%. It seems that the protease activity in DMF can be recovered by the addition of water (Figure 14 B). 

Tjalsma H, Koetje EJ, Kiewiet R et al. (2004) Engineering of quotum-sensing systems for improved production of alkaline protease by Bacillus subtilis. J Appl Microbiol 96(3) 569-578 Torres S, Castro G (2004) Non-aqueous biocatalysis in homogeneous solvent systems. Food Tech-nol Biotechnol 42(4) 271-277... 

Bruckner, R., Shoseyov, O., and Doi, R.H. (1990) Multiple active forms of a novel serine protease from Bacillus subtilis. Mol Gen. Genet., 221 (3),... 

The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease. Microbiology, 142 (12), 3437-3444. 

Subtilisin (EC 3.4.21.4) an extracellular, single chain, alkaline serine protease from Bacillus subtilis and related species. S. are known from four different species of Bacillus S. Carlsberg (274 amino acid residues, M, 27,277), S. BPN (275 amino acid residues, M, 27,537), S. Novo (identical with S.BPN ) and S. amylosacchariticus (275 amino acid residues, M, 27671). The observed sequence differences between different S. represent conservative substitutions and are limited to the surface amino acids. Like the pancreatic proteinases, S. has catalytic Ser22i, His64 and Asnjj residues, but it is structurally very different from the other serine proteases, e. g. the active center of S. is -Thr-Ser-Met-, whereas that of the pancreatic enzymes is -Asp-Ser-Gly- pancreatic enzymes contain 4- disulfide bridges, whereas S. contains none S. contains 31 % a-helical structure and 3 spatially separated domains, whereas the pancreatic enzymes have 10-20% a-helical structure and a high content of p-structures in both types, the active center is a substrate cleft. S. also have a broader substrate specificity than the pancreatic enzymes. This is a notable example of the convergent evolution of catalytic activity in two structurally completely different classes of proteins. S. is used in the structural elucidation... 

The first commercial enzyme-containing washing powder, Burnus, was marketed in 1913. This trypsin-containing powder was not a success because it was unstable. In 1959, the Swiss Ferment Company marketed a washing powder containing a protease enzyme from one of the species of Bacillus subtilis. This was a major advance in enzyme technology since the bacteria... 

Cai,Y., Yao S-P., Wu Q. Lin X.F. (2004). Michael addition of imidazole with acrylates catalysed by alkaline protease from Bacillus subtilis in organic media. Biotechnology letters, vol.26, n°6, pp.525-528, (March 2004), ISSN 0141-5492... 

Siqueira FG, Filho EFF (2010) Plant cell wall as a substrate for the production of enzymes with industrial applications. Mini-Rev Org Chem 7 54-60 Suh HJ, Lee HK (2001) Characterization of a keratinolytic serine protease from Bacillus subtilis KS-1. J Protein Chem 20 165-169 Sukuruman RK, Singhania RR, Pandey A (2005) Microbial cellulases production, applications and challenges. J Sci Ind Res 64 832-844 Sun H, Zhao P, Ge X, Xia Y, Hao Z, Liu J, Peng M (2010) R ent advances in microbial raw starch degrading enzymes. Appl Biochem Biotechnol 160(4) 988-1003... 

Mukhtar, H., Ul-Haq, 1. Production of alkaline protease by Bacillus subtilis and its application as a depilating agent in leather processing. PakJBot 2008,40,1673-1679. 

Prabhavathy, G., Pandian, M. R., Senthilkumar, B. Identification of industrially important alkaline protease producing Bacillus subtilis by 16s rRNA sequence analysis and its applications. Int J Res Pharma Biomed Sci 2013,4, 332-338. 

Sathiya, G. Production of protease from Bacillus subtilis and its application in leather making process. Int J Res Biotechnol Biochem 2013, 3, 7-10. 

Many related so-called thermolysin-like proteinases (TLPs) from various Grampositive strains have been described [47], including neutral proteases from Bacillus subtilis, and some of these variants are applied in peptide synthesis. Several metal-loenzymes acting as carboxy- or aminopeptidase have also been characterized, but these variants have not been extensively used in peptide synthesis. A bovine carboxy-peptidase A [39] and orange carboxypeptidase C [68] have been applied for dipeptide synthesis in water-organic solvent mixtures, both under thermodynamic and xmder kinetic control. 

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