Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Immobilization of thermostable beta-glucosidase variants on acrylic supports for biocatalytic processes in hot water

In English

Författare

Summary, in English

Two variants of the thermostable beta-glucosidase TnBgl1A (wt and N221S/P342L) from Thermotoga neapolitana were immobilized on acrylic supports (Eupergit (R) C, Eupergit (R) C250L, and cryogel) and evaluated at conditions close to the boiling point of water. Thermo-gravimetric analysis showed the supports to be stable <250 degrees C. Both wt and N221S/P342L were covalently bound to oxirane-groups respectively via glutaraldehyde spacers, and for coupling reactions 26 Lys and 20 Ser/Thr were surface-located. Immobilized enzymes were active on all supports in the temperature range 80-95 degrees C, but the observed specific activity was low (<= 19 U mg(-1)) using the cryogel. More than 91% of the initial activity was maintained after ten times recycling, and the same was recovered after 3 months storage at 4 degrees C for Eupergit (R) supports by simply incubating the preparation with bovine serum albumin. No storage loss was detectable on cryogels. The glutaraldehyde spacer improved activity on cryogels, but not on Eupergie supports. Immobilization on Eupergit (R) C250L yielded the highest observed specific activity (254 U mg(-1) for N221S/P342L) in a procedure including blocking of free oxirane-groups by BSA. This biocatalyst was used for on-line hydrolysis of quercetin-glucosides in a yellow onion extract at 80 degrees C, proving the immobilized biocatalyst to be promising in on-line systems for extraction and hydrolysis using hot pressurized water. (C) 2012 Elsevier B.V. All rights reserved.

Publiceringsår

2012

Språk

Engelska

Sidor

28-38

Publikation/Tidskrift/Serie

Journal of Molecular Catalysis B: Enzymatic

Volym

80

Dokumenttyp

Artikel i tidskrift

Förlag

Elsevier

Ämne

  • Organic Chemistry
  • Industrial Biotechnology

Nyckelord

  • Immobilization
  • Glycoside hydrolase family 1
  • Eupergit (R) C
  • Eupergit
  • (R) C250L
  • Cryogel

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1873-3158