In order to use lysozyme as an antimicrobial agent in the brewing process, the hen protein lysozyme (LYZ) is in two different covalent immobilization micro size magnetic particle (toluene sulfonyl activation and carboxylated, TSA and CA, respectively). A cell suspension of Oenococcus oeni, a oenological strain to participate in brewing process, be used as LYZ substrate. At the same time, a research dynamics study the stability of a LYZ free and fixed in the McIlvane buffer in the pH value is 3.2, the lowest pH value in wine. Activities and dynamics parameter measuring free LYZ pH value is 3.2, below reported in the best pH value (4.5); However residual activity in the pH value 3.2 is enough interests for further fixed and applications in the wine. All the dynamics parameters two biological catalyst (LYZ - CA and LYZ - TSA) after fixed change, this may be due to the active site structure modification caused by covalent attachment support. At 25 ° C is free the half-life of calculation LYZ 39 h, but it increases to 280 and 134 h and LYZ - CA LYZ - TSA of respectively. The results show that the stability of the immobilized enzyme and improve, can use LYZ in wine application in its fixed form. In addition, LYZ - TSA seems to be the best biological catalyst for further application in wine.

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