ABSTRACT
The biotransformation of acrylonitrile was investigated using thermophilic nitrilase produced from a new isolate Streptomyces sp. MTCC 7546 in both the free and immobilized state. Under optimal conditions,the enzyme converts nitriles to acids without the formation of amides.The whole cells of the isolate were immobilized in agar-agar and the beads so formed were evaluated for 25 cycles at 50 degrees C. The enzyme showed a little loss of activity during reuse. Seventy-one per cent of 0.5 M acrylonitrile was converted to acid at 6 h of incubation at a very low density of immobilized cells, while 100% conversion was observed at 3 h by free cells.
Subject(s)
Acrylonitrile/metabolism , Aminohydrolases/metabolism , Streptomyces/metabolism , Agar , Biotransformation , Cells, Immobilized/metabolism , Streptomyces/isolation & purificationABSTRACT
The efficiency of xylanase of Bacillus brevis BISR-062 as a prebleaching agent was evaluated on three nonwoody pulps at two different pH values (7.0 and 8.5). Crude xylanase was found to have an optimum temperature and pH of 65-70 degrees C and 7.0, respectively. The stability of the enzyme was determined at two pH values (7.0 and 8.0), and it lost approx 50% of its activity at both values within 2 h at 50 degrees C. However, the enzyme was found to be effective as a prebleaching agent only with rice straw pulp. A maximum brightness gain of 6 points was obtained with this pulp at pH 7.0. The strength properties of the rice straw pulp at pH 7.0 also improved as the result of enzyme treatment.
