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Please use this identifier to cite or link to this item: http://purl.org/purl/4264

Title: Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10
Authors: Chandrasekaran, M
Archana, Kishore
Sreeja, Chellappan
Soorej, Basheer M
Jasmin, C
Sarita,G Bhat
Elyas, K K
Keywords: Engyodontium album
Serine protease
Detergent enzyme
Amino acid analysis
Issue Date: 26-Nov-2010
Publisher: Springer
Abstract: An alkaline protease from marine Engyodontium album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme.Km, Vmax, and Kcat of the enzyme were 4.727 9 10-2 mg/ml, 394.68 U, and 4.2175 9 10-2 s-1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65 C), withmaximumactivity at pH 11 and 60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, and Al3? inhibited enzyme activity, while 1 mMCo2? enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.
Description: J Ind Microbiol Biotechnol (2011) 38:743–752 DOI 10.1007/s10295-010-0914-3
URI: http://dyuthi.cusat.ac.in/purl/4264
Appears in Collections:Dr. M Chandrasekharan

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