NDLI: Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10

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Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10

Content Provider	CUSAT-Thesis
Author	Chandrasekaran, M. Archana, Kishore Sreeja, Chellappan Soorej, Basheer M. Jasmin, C. Sarita, G. Bhat Elyas, K. K.
Abstract	An alkaline protease from marine Engyodontiumalbum was characterized for its physicochemicalproperties towards evaluation of its suitability for potentialindustrial applications. Molecular mass of the enzyme bymatrix-assisted laser desorption ionization-mass spectrometry(MALDI-MS) analysis was calculated as 28.6 kDa.Isoelectric focusing yielded pI of 3–4. Enzyme inhibition byphenylmethylsulfonyl fluoride (PMSF) and aprotininconfirmed 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. Enzymewas noted to be active over a broad range of pH (6–12) andtemperature (15–65 C), withmaximumactivity at pH 11 and60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) impartedthermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, andAl3? inhibited enzyme activity, while 1 mMCo2? enhancedenzyme activity. Reducing agents enhanced enzyme activityat lower concentrations. The enzyme showed considerablestorage stability, and retained its activity in the presence ofhydrocarbons, natural oils, surfactants, and most of theorganic solvents tested. Results indicate that the marineprotease holds potential for use in the detergent industry andfor varied applications.
File Format	PDF
Language	English
Publisher	Springer
Access Restriction	Open
Subject Keyword	Engyodontium album Serine protease Detergent enzyme Characterization Amino acid analysis MALDI-MS
Content Type	Text
Resource Type	Article

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