Production and immobilization of a novel thermoalkalophilic extracellular amylase from bacilli isolate
Özet
A Thermoalkalophilic amylase was produced from an environmental bacterial isolate. The enzyme was then immobilized through its amino groups onto the epoxy rings of magnetic poly glycidyl methacrylate [m-poly (GMA)] beads. The free enzyme was active within a large pH range, between 7 and 12 and displayed the optimum activity at 95 degrees C and pH 10. The immobilization appeared to increase the stability of the enzyme as its bound form showed optimum activity at 105 degrees C and pH 11.0. Kinetic studies demonstrated that immobilized enzyme had higher K-m and lower V-max values. The activity of the free and bound enzyme was determined, at 37 degrees C and pH 10.0 and pH 11.0, respectively, in the presence of various organic solvents and detergents (5%, v/v). Results obtained indicated that detergents, sodium dodecyl sulfate (SDS) and TritonX-100, caused six fold increase and that various organic solvents also increased the activity of the amylase. (C) 2012 Elsevier B.V. All rights reserved.
Kaynak
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULESCilt
50Sayı
4Koleksiyonlar
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