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Rotating bed reactor packed with heterofunctional structured silica-supported lipase or Novozym 435. Developing an effective system for the organic solvent and aqueous phase reactions
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  • Katarzyna Szymańska,
  • Daria Kowalczykiewicz,
  • Danuta Gillner,
  • Andrzej Jarzębski
Katarzyna Szymańska
Politechnika Śląska Wydział Chemiczny
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Daria Kowalczykiewicz
Politechnika Slaska Wydzial Chemiczny
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Danuta Gillner
Politechnika Śląska Wydział Chemiczny
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Andrzej Jarzębski
Politechnika Śląska Wydział Chemiczny
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Peer review status:POSTED

31 Jul 2020Submitted to Biotechnology and Bioengineering
31 Jul 2020Assigned to Editor
31 Jul 2020Submission Checks Completed

Abstract

Production of specialty chemicals increasingly makes use of enzyme catalysts, and Novozym 435 (N435) is among most often applied. However, its polymeric skeleton is unstable in many solvents. In this context, we report results of a systematic study of the biocatalysts, fabricated using highly porous siliceous pellets/enzyme (MH), grafted with octyl (-O), amino (-A) and octyl and amino (-OA) groups, deployed in a rotating bed reactor and tested in hydrolysis and esterification reactions. N435 appeared the most active in both reactions, when activity was related to the catalyst’s mass, mainly owing to very large enzyme load. But its structure degraded in many typical solvents, whereas no such effect was detected in MH-O- and MH-OA-catalysts. MH-O showed the highest specific activity, however, a significant enzyme leaching was observed in a hydrolytic reaction, in contrast to MH-OA. In esterification reaction the MH-O-bound lipase was not only most active but also quite stable.