Proteinase microbial

Microbial proteinases can be classified by mechanism of action. Hartley (1960) divided them into four groups serine proteinases, thio proteinases, metalloproteinases, and acid proteinases. Morihara (1974) classified enzymes within these groups according to substrate specificity. Enzymes which split peptide substrates at the carboxyl side of specific amino acids are called carboxyendopeptidases, and those which split peptide substrates at the amino side of specific amino acids are called aminoendopeptidases. Acid proteinases, such as rennin and pepsin, split either side of specific aromatic or hydrophobic amino acid residues. The action of proteolytic enzymes on milk proteins has been reviewed by Visser (1981). 

Morihara, K. 1974. Comparative specificity of microbial proteinases. Adv. Enzymol. 41, 179-244. 

Heitz, T., P. Geoffroy, A. Stintzi, B. Fritig, and M. Legrandf cDNA cloning and gene expression analysis of the microbial proteinase inhibitor of tobacco J. Biol. Chem. 268 (1993) 16987-16992. 

Molla A, Yamamoto T, Akaike T, Miyoshi S, Maeda H. Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases. J Biol Chem 1989 264 10589-10594. 

Use of Highly Porous Bead Cellulose with Attached Bacitracin for Affinity Chromatography of a Microbial Proteinase J, TurkovA, M.J. Benes, M. Kiihn, V.M. Stepanov, and L.A. Lyublinskaya... 

USE OF HIGHLY POROUS BEAD CELLULOSE WITH ATTACHED BACITRACIN FOR AFFINITY CHROMATOGRAPHY OF A MICROBIAL PROTEINASE... 

Processes involving proteolysis play a role in the production of many foods. Proteolysis can occur as a result of proteinases in the food itself, e. g., autolytic reactions in meat, or due to microbial proteinases, e. g., the addition of pure cultures of selected microorganisms during the production of cheese. 

The partially-purified extract oxidised a range of phenolic substrates, and also contained proteinases and amino acid decarboxylases. Preincubation of a toluene-treated soil enzyme preparation for 12h at 37°C did not affect diphenol oxidase activities, ie. the oxidases appeared to be resistant to attack by the coextracted soil proteinases. Addition of hyaluronidase before preincubation also was without effect. Preincubation with the microbial proteinase, Pronase for I8h at 37°C decreased diphenol oxidase activities by 307o, and by 100% when both Pronase and hyaluronidase were added. The results suggested that the polysaccharides associated with the extracted soil oxidases protected the enzymes from proteolysis and may play a role in stabilizing exocellular enzymes in soils. 

Soil differed in their relative activities towards ZPL and BAA the enzymes involved were extracted from a soil with different efficiencies. Extracted ZPL-hydrolysing enzymes retained complete activity when freeze-dried, or dried at 30°C (90 min), or when incubated under bacteriostatic conditions for 10 days at 25°C. Incubation of the extracts for 1 day at 30°C with or without the addition of microbial proteinases, thermolysin or subtilisin decreased activities towards ZPL by about 10% only. The extracted enzyme, in regard to its specificity of hydrolysis of Z-dipeptides and its response to inhibitors, exhibited some of the properties of carboxypeptidase. 

Outtrup, H., Boyce, C. O. L. Microbial proteinases and biotechnology. In Microbial Enzymes and Biotechnology, 2 edition, Fogarty, W. M., Kelly, C. T. (Eds.), Elsevier Applied Science London, England, 1990, pp. 221-25 >. 

Kalisz, H. M., Microbial Proteinases, Advances in Biochemical Engineering/Biotechnology, 36, 1 (1988). 

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