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Immobilized enzymes, 13. Immobilization of trypsin previously protected by a synthetic water‐soluble macromolecular inhibitor

1981; Wiley; Volume: 182; Issue: 6 Linguagem: Inglês

10.1002/macp.1981.021820601

0025-116X

Eric Brown, André Racois,

Chemical Synthesis and Analysis

Abstract A new water‐soluble acrylic polymer 5 , with spacer‐arms bearing benzamidine groups, was synthesized as a polymeric inhibitor to protect trypsin during immobilization of this enzyme on two different water‐insoluble carriers, i.e., VINAC‐S and ACAPROSUC. The latter is an acrylic polymer and bears sidechains ending with succinimido ester groups, whereas VINAC‐S is a polyvinylic matrix having aldehyde groups. The trypsin‐VINAC‐S conjugates prepared in the presence of the polymeric inhibitor 5 were twice as active towards N 2 ‐benzoyl‐L‐arginine ethyl ester, and four times as active towards haemoglobin, as the corresponding conjugates prepared in the absence of 5 . More than 80% of the overall initial esterolytic activity of trypsin was retained by the corresponding ACAPROSUC conjugate, when the immobilization reaction was carried out in the presence of 5 . The overall residual activity of the conjugate was 46% when operating in the absence of 5 . The above method of enzyme protection should prove very useful in immobilized enzyme methodology and technology.