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1

Catalytical activity of penicyllin acylase in native and stabilized derivatives

100%
Bryjak J., Noworyta A.
Biotechnologia
|
1993
|
issue 4
175-185
EN
Three different enzyme preparations were investigated:native enzyme, enzyme stabilized by adding poly(ethyleneimine) and enzyme attached to acrylic carrier.The preparations were compared with regard to their storage, temparature and pH-stabilities as well as the effect of temperature and pH-value on enzyme activity.It was found that for all preparations hydrolisis was kinetically limited.Five kinetic equation constans were calculated. The enzyme stabilized by poly(ethyleneimine) was selected as the best preparation to be applied in industry.
2

Selection of reaction system for dipeptides enzymatic synthesis

100%
Trusek-Holownia A., Noworyta A.
Biotechnologia
|
2000
|
issue 1
156-170
EN
Synthesis of dipeptides in water, in the solution of water/organic cosolvent and in the binary aqueous-organic system was studied. A set of equlibrium equations was determined and used to predict a product yield. Reagents activities served as variable. Verification of equation's validity was performed in the synthesis of ZAlaPheOMe dipeptide catalysed by thermolysin. The reaction was carried out in water, metanol-water solution and in binary system ethyl acetate - water. It was shown that the synthesis in the binary system was the most effective. It was concluded that the efficiency of ethyl acetate - water system resulted from: 1) improvement of the reagents solubility; 2) product extraction into the organic phase. An insignificant difference in enzyme stability when thermolysin was immersed in water or in the ethyl acetate - water system was observed. Process kinetics in the binary system will be the aim of the next studies.
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