Abstract
Thermostable lipase from Humicola lanuginosa No. 3 was immobilized by entrapment in photo-crosslinkable resin prepolymers, urethane prepolymers or Ca-alginate. Adsorption to different types of resins or gels, and covalent binding methods were also employed. From all the methods examined, adsorption on Amberlite XAD-7 followed by crosslinking with glutaraldehyde was superior, as to several points. Firstly, the adsorption efficiency for lipase was relatively high, being about 70%. Secondly, the optimal temperature was about 10°C higher than that for free lipase. The resin immobilized lipase was not affected by pH changes, and finally it also exhibited excellent stability as to repeated batch hydrolysis of triglycerides, both in a shaking flask system and in a recycling column reactor for more than 2 and 3 weeks, respectively.
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