Production of alfa amylase from Haloarcula hispanica 2TK2 strain that is a kind of archaebacteria

Enzymes are protein structured molecules which catalyze the biochemical reactions. In recent years; because of the developments in biotechnology area; the thermo stable and alkaline stable enzymes that are produced via different sources are widely used in food and detergent industries. Enzymes can be produced from animal sources, plant sources and microorganisms. Microorganisms are particularly preferred as potential enzyme source because they grow in number easily and also, controlling the enzyme production is easy. Because of the high activity of these enzymes, less by-product, more stable and cheaper; enzyme production by microorganism has been very important topic day by day. Halophilic archaea adapted to life at salt concentrations at or nearly saturation and haloarchaeal proteins have specific properties for adapting to highly salty environments, so that their proteins maintain stability and functionality in extreme habitants. Many haloarchaeal enzymes have been detected in halophiles; one of them is ?-amylase that is industrially very important.In this study, ?-amylase properties of Haloarcula hispanica 2TK2 strain isolated from Tuzkoy Salt Mine of Turkey were investigated. The ?-amylase activity studies were carried out at 25 - 80 °C temperature values, 1 - 6 M salt concentration values and pH 4 - 10.8 values. The optimum pH, temperature and NaCl concentration values for the relative activity were determined as 6.9, 52 °C and 5 M, respectively. It was also found that the relative activity increases while salt concentration of growth media increases, in all of the samples. Also, the presence of starch in growth media significantly increased the activity of secreted ?-amylase from the halophilic archaeon Haloarcula hispanica 2TK2. In addition, the tolerance of alfa amylase produced from Haloarcula hispanica 2TK2 is investigated in the presence of some surfactants such as triton X 100, tween 80 and propylene glycol. This study indicates that Haloarcula hispanica 2TK2 and ?-amylase from Haloarcula hispanica 2TK2 are fairly salt tolerant, have enzyme activity at a wide range of temperature and pH values and have activity in the presence of some sulfactants. In the presence of 50 % (v/v), Triton X 100, 50 % (v/v) Tween 80 ve 50 % (v/v) propylene glycol; the remainin enzyme activities determined as % 49,87, % 47,62 ve % 66,47, respectively. Thus, it may be considered as a potential candidate for future use in industrial processes which require the use of enzymes that protect their stability and functionality under extreme conditions such as high salt concentrations.Keywords: ?-amylase, Haloarcula hispanica 2TK2, spectrophotometric method, relative activity, salt tolerant