Abstract
A newly isolated Rhizopus oryzae was found to exhibit some unusual phenomenon of secreting alkaline protease which was purified and characterized. The molecular weight was determined to be 28,600 dalton in gel electrophoresis. The enzyme is stable in the pH range from 3 to 11 and most active at pH 8. The temperature optimum of this thermostable biocatalyst is at 60 °C. The enzyme is sensitive to metal chelators, most of the metal ions (excepting a few monovalent cations) and inhibitor like PMSF. This indicates that the protease of isolated Rhizopus oryzae falls under alkaline serine group.
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Godfrey, T.; Reichelt, J.: Industrial Enzymology, New York, Nature Press 1983
Banerjee, R.: Some studies on production, purification and characterization of extracellular protease from Rhizopus oryzae (RO, IIT KGP); Ph. D. thesis report of Indian Institute of Technology, Kharagpur, 1991
Singh, D. P.; Singh, R.; Vyas, S. R.: Effect of pH, temperature, nitrogen sources and glucose concentration on acid protease production by Aspergillus niger mutant. Indian. J. Microbiol. 15 (3) (1975) 109–113
Tsuchiya, K.; Kirmura, T.: Decrease of protease activity by the addition of glucose to the culture of Cephalosporium sp. J. Ferment. Technol. 62 (1) (1984) 35–39
Masaru, O.; Jordan, T.; Delancy, R.: Liquid culture of Rhizopus chinensis for the production of acid protease Rhizopus pepsin. Inst. J. Biochem. 14 (10) (1982) 921–924
Deng, C.; Ochi, T.: Milk clotting enzyme from fungus I. Screening test of a potent fungus for producing milk clotting enzyme. Rakunokagaku Shokuhin Kenkyu 35 (5) (1986) A199-A204
Chandrasekaran, S.; Dhar, S. C.: A low cost method for the production of alkaline protease using. Tapoica starch. J. Ferment. Technol. 61 (5) (1983) 511–514
Patil, M.; Shastri, N. V.: Extracellular protease by Alternaria alternate (Fr.) Keissl. J. Ferment. Technol. 59 (5) (1981) 403–406
Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248–254
Laemmli, U. K.: Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (London) 227 (1970) 680–685
Sakka, K.; Shimada, K.; Matsushima, K.: Purifikation and some properties of serine proteinase from a mutant of Aspergillus niger. J. Ferment. Technol. 63 (5) (1983) 480–483
Kimoto, K.; Yokoi, T.; Mura Kami, K.: Purification and characterization of chymotrypsin like proteinase from Euphausia superba. Agric. Biol. Chem. 49 (6) (1985) 1599–1603
Iizumi, T.; Nakamura, K.; Pukase, T.: Purification and characterization of thermostable lipase from a newly isolated Pseudomonas sp. KWI-56. Agric. Biol. Chem. 54 (5) (1990) 1253–1258
Durham, Don R.; Stewart, David B.; Stellwag, E. J.: Novel alkaline and heat stable serine proteases from alkalophillic Bacillus Species strain GX6638. J. Bacteriology 169 (6) (1981) 2762–2768
Hon, W.-N.; Chung, M.-J.: Studies on the enzyme of Rhizopus oryzae: Part I: Production of acid protease and enzymatic characteristics. Hanguk Nonghwa Hakhoe chi 22 (3) (1979) 135–141
Impoolsup, A.; Bhumiratana, A.; Flegel, T. W.: Isolation of alkaline and neutral protease from Aspergillus flavus var. columanaris a Soy-Sauce Koji mold. Appl. Environ. Microbiol. 42 (4) (1981) 619–628
Masaki, T.; Suzuki, H.; Soejima, M.: Purification and some properties of Achromobacter protease Ia from Achromobactor lyticus M 497-1. Agric. Biol. Chem. 50 (12) (1986) 3087–3091
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Banerjee, R., Bhattacharyya, B.C. Purification and characterization of protease from a newly isolated Rhizopus oryzae. Bioprocess Engineering 7, 369–374 (1992). https://doi.org/10.1007/BF00369493
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DOI: https://doi.org/10.1007/BF00369493