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

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. K (m), V (max), and K (cat) of the enzyme were 4.727 x 10⁻² mg/ml, 394.68 U, and 4.2175 x 10⁻² s⁻¹, respectively. Enzyme was noted to be active over a broad range of pH (6-12) and temperature (15-65 °C), with maximum activity 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 mM Co²⁺ 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.

Modulation of FAD-dependent monooxygenase activity from aromatic compounds-degrading Stenotrophomonas maltophilia strain KB2.

“…Different results were obtained by Lattard et al (2002) and Myasoedova et al (2007), who did not observe an effect of nonionic detergents on monooxygenase activity. The increase in activity in the presence of surfactants may be attributed to increased substrate accessibility of the enzyme (Chellappan et al, 2010). In the presence of oleic, stearic and sulphanilic acids the monooxygenase activity decreased significantly.…”

Purification and Characterization of Extracellular, Polyextremophilic α-amylase Obtained from Halophilic Engyodontium album

“…Except few preliminary screenings no reports of purification and detailed characterization of α-amy- lases from halophilic fungi exists. E. album has not been much reported for its potential of extracellular enzymes except few reports of proteases (22,23).…”

Engyodontochones, Antibiotic Polyketides from the Marine Fungus Engyodontium album Strain LF069

“…The keratinolytic capacity of E. album is the basis for the production of the extracellular broad spectrum serine protease, proteinase K, which is produced for commercial purposes. [7] Engyodontiumalbum was also found in several extreme environments. Thisincludes stratospheric air, [8] deep-sea, [9] and Antarctic macroalgae.…”

“…Biological activities of compounds[1][2][3][4][5]7,and 8 (IC 50 values are given in mM). The broadest range and the strongest effects were observed for 1-4,e xhibiting inhibition of all test strains;t hat is, S. epidermidis, S. aureus (MRSA), P. acnes, C. albicans,a nd T. rubrum.…”