Immobilized enzymes - valuable tools for the indication of temperature events

STEFANIE WETZEL; PETER ALLERTZ; SÖREN KOSCHNICKE; MARIANA TASSO; KATRIN SALCHERT

BIOCATALYSIS AND BIOTRANSFORMATION

TAYLOR & FRANCIS LTD

Lugar: Londres; Año: 2013 p. 1 - 4

1024-2422

The enzymes trypsin and urease were covalently tethered to cellulose to utilize their ability toproduce colored products as a consequence of enzymatic activity. Therefore, cellulose hadto be chemically modified first in order to generate appropriate chemical functionalities.Different approaches including periodate supported oxidation followed by immobilization viareductive amination, insertion of a reactive polymer interface, and cross-linking inside thecellulose matrix were utilized for the immobilization. The success of immobilization wasassessed by the quantification of surface-bound protein amounts as well as by recording ofenzymatic activities under different conditions. Enzymatic activity of trypsin as well as ofurease was maintained best when a hydrophilic intermediate polymer layer was used forimmobilization. The basic applicability of immobilized enzymes as temperature indicatorswas demonstrated using cross-linked urease. In dependency on the immobilized enzymeamount a continuous color change induced by bromothymol blue along different time pointscould be detected.