Abstract
Abstract Thermomyces lanuginosus lipase, in both its free form as well as immobilized in sol-gel matrices produced using the precursor tetraethoxysilane (TEOS) and dried using the xerogel technique, was used in transesterification reactions between 2-phenylethyl alcohol and vinyl acetate. The free lipase was first characterized in terms of its transesterification activity at 37°C, with a value of 1,233 U/g obtained and lower temperatures providing higher activity. The influence of humidity on the enzyme immobilized with TEOS was evaluated using a 22 factorial design (varying the conditions of humidity and temperature). The results indicate that higher humidity (30%) and lower temperature (40°C) provided the best transesterification activity, and that these two factors and their interaction had a significant influence on activity (at the 95% confidence level). Under these conditions, the biocatalyst presented a surface area of 502 m2/g, a pore volume of 0.643 cm3/g, and an average pore diameter of 51.2 A. ...
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