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PRELIMINARY DATA REGARDING THE KINETIC PROPERTIES OF AN ALPHA-AMYLASE FROM ROBINIA PSEUDACACIA L. GERMINATED SEEDS

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Author(s): Vlad Artenie | Marius Mihasan

Journal: Analele Ştiinţifice Ale Universităţii Alexandru Ioan Cuza din Iași,Sectiunea II A : Genetica si Biologie Moleculara
ISSN 1582-3571

Volume: 6;
Issue: 1;
Date: 2005;
Original page

ABSTRACT
We have accomplished a partial purification of a alpha amylase from germinated seeds of Robinia pseudacacia L. by affinity precipitation. The key element is the sodium alginate, a polymer that proved affinity for this enzyme, and also has the propriety to reversibly precipitate with Ca2+. The enzyme binds to the alginate and the complex is precipitated with Ca2+. The amylase activity is recovered by dissolving the precipitate in 1M maltose and precipitating the alginate alone by addition of Ca2+. The  enzyme has a molecular weight estimated between 50 and 65 kDa, an optimum pH between 5 and 6; it is inhibited by ammonium sulfate and activated by CaCl2.

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