RESUMO
The process of enzymatic hydrolysis of the mycelial waste from the manufacture of tetracycline with using Streptomyces aureofaciens was studied. For the enzymatic hydrolysis, neutral and alkaline proteinases were used. It was shown that alkaline proteinase (protosubtilin G10X) provided the most efficient hydrolysis. Optimal conditions for the hydrolysis were determined: a temperature of 42 degrees C, hydrolysis time of 4 to 6 hours and enzyme concentrations of 1.25 to 2.20 mg/ml at a mycecial waste concentration of 12.5 mg/ml. The time course of changes in amino acid and amine nitrogen levels during enzymatic hydrolysis was investigated. It was demonstrated that the hydrolysis efficiency depended on the mode of enzyme addition. The highest efficiency was observed with fractional feeding of the enzyme.
Assuntos
Proteínas de Bactérias/metabolismo , Indústria Farmacêutica , Microbiologia Industrial , Resíduos Industriais , Hidrolisados de Proteína/isolamento & purificação , Streptomyces aureofaciens/metabolismo , Tetraciclina/biossíntese , Endopeptidases/farmacologia , Hidrólise , U.R.S.S.RESUMO
A possibility of invertase immobilization in the polyvinyl alcohol coating formed directly on the electrode surface from water solution of polyvinyl alcohol and boric acid was being investigated. Conditions for obtaining the polymeric coating at the constant potential and at the constant current were compared. In order to obtain the polymeric coatings with a marked enzyme activity optimal conditions were found.
Assuntos
Enzimas Imobilizadas , Glicosídeo Hidrolases , Álcool de Polivinil , Eletroquímica , Eletrodos , beta-FrutofuranosidaseRESUMO
Trypsin immobilization in an inorganic polymer, i.e. silica gel, was investigated. Properties of the immobilized enzyme were examined. It was found that the enzyme retained its activity, depending on the gel genesis and dehydration of the carrier. The effect of stabilizing supplements on the enzyme activity was studied. The enzyme immobilization was accompanied by an increase in its thermostability.