Convenience of immobilizedBacillus licheniformis α-amylase as time—temperature-integrator (TTI)

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Abstract
For the immobilization of Bacillus licheniformis α‐amylase to porous glass beads, the performances of three possible linking agents, glutaric dialdehyde, benzoquinone and S‐trichlorotriazine were assessed in respect of the protein yield, the enzymic activity and the thermostability of the immobilized enzyme. These three properties are to be evaluated in view of the possible use of the enzyme preparations as time–temperature‐integrators (TTIs) for assessing the severity of heat pasteurization or sterilization processes of food or pharmaceuticals. All three linkers improved the enzymes's resistance to irreversible heat inactivation to a similar extent and in each case biphasic inactivation kinetics were observed, whereas the dissolved B. licheniformis α‐amylase showed a simple first order decay. The immobilization yield, measured as protein per carrier weight, did not differ markedly for the three linkers, although the enzymic activity of the glutaric dialdehyde‐linked enzyme was lower than that of the benzoquinone‐ and S‐trichlorotriazine‐linked preparations.