Enzyme immobilisation using SBA-15 mesoporous molecular sieves with functionalised surfaces

Humphrey Hak Ping Yiu, Paul A Wright, Nigel P Botting

Research output: Contribution to journalArticlepeer-review

350 Citations (Scopus)


Functionalised hexagonal mesoporous SBA-15-type molecular sieves with pore sizes in the range 51-56 Angstrom have been prepared using non-ionic block copolymers and used for immobilisation of the enzyme trypsin. Thiol, chloride, amine, and carboxylic acid functional groups were attached by siloxypropane tethers to the siliceous surface of SBA-15 via two methods, post-synthesis grafting and in situ synthesis. Phenylsiloxane groups were also incorporated using these two methods. The resulting solids were rendered porous and used to immobilise trypsin, giving variable but in general higher retention of the enzyme molecules than was observed on unfunctionalised, purely siliceous SBA-15. The resulting supported enzyme catalysts were shown to be active and stable catalysts for the hydrolysis of N-alpha -benzoyl-DL-arginine-4-nitroanilide (BA-PNA). The solids prepared by supporting the enzyme on thiol-functionalised SBA-15 prepared by in situ synthesis were found to be the most promising. Trypsin supported on thiol-functionalised SBA-15 was shown to be recyclable, (C) 2001 Elsevier Science B.V. All rights reserved.

Original languageEnglish
Pages (from-to)81-92
Number of pages12
JournalJournal of Molecular Catalysis B: Enzymatic
Issue number1-3
Publication statusPublished - 28 Sept 2001


  • mesoporous molecular sieve
  • SBA-15
  • functionalisation
  • trypsin
  • enzyme immobilisation
  • MCM-41


Dive into the research topics of 'Enzyme immobilisation using SBA-15 mesoporous molecular sieves with functionalised surfaces'. Together they form a unique fingerprint.

Cite this