Abstract
The enantioselectivity of a lipase from Geobacillus thermocatenulatus (BTL2) has been altered by a site-directed immobilization on tailor-made disulfide supports. The enzyme was genetically modified introducing a unique cysteine into different positions of the protein surface. These new enzyme variants (ϕ-BTL2) maintained the catalytic properties of the native enzyme. The ϕ-BTL2 was immobilized by different orientation on disulfide support at pH 7 via disulfide-exchange and additionally rigidification was introduced by the immobilization on disulfide-aldehyde support through the interaction of the reactive amino groups on the protein near to the position of the introduced cysteine with aldehydes on the support.
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