期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 51, 期 3-4, 页码 86-92出版社
ELSEVIER
DOI: 10.1016/j.molcatb.2007.10.018
关键词
invert sugar; immobilized invertase; exchanging anionic resin
This work presents as a main objective to study the immobilization process of yeast invertase by adsorption in the ion exchanging resin Duolite A-568 for invert sugar production. Initially, a kinetic study of the soluble form of the enzyme was carried out. At the sequence was studied the immobilization process of yeast invertase in the weakly exchanging anionic resin Duolite A-568. The influences of the pH, enzyme concentration and temperature in the enzyme immobilization were analyzed through a central composite design (CCD). The results indicated that the retention of the catalytic activity in immobilization was strongly dependent of these variables, being maximum in a pH value of 5.0, with an enzyme concentration of 12.5 g/L (1.875 g of protein per liter) and temperature of 30 degrees C. The simultaneous influence of pH and temperature on the free and immobilized invertase activity was also studied through a CCD. (C) 2007 Elsevier B.V. All rights reserved.
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