{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T10:17:49Z","timestamp":1760782669940,"version":"build-2065373602"},"reference-count":16,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2002,1,4]],"date-time":"2002-01-04T00:00:00Z","timestamp":1010102400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotech &amp;amp; Bioengineering"],"published-print":{"date-parts":[[2002,2,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>\u03b2\u2010Galactosidase (<jats:italic>Escherichia coli<\/jats:italic>) was immobilized through its thiol groups on thiolsulfinate\u2010agarose gel. After enzyme immobilization, different nano\u2010environments were generated by reacting the excess of gel\u2010bound thiolsulfinate moieties with 2\u2010mercaptoethanesulfonic acid (S\u2010gel), glutathione (G\u2010gel), cysteamine (C\u2010gel), and mercaptoethanol (M\u2010gel). Concerning thermal stability at 50\u00b0C, the G\u2010gel and the M\u2010gel derivatives were the most stable with residual activity values of 67% and 45%, respectively. The stability in several solvent systems was studied: ethyl acetate (1.6% vol\/vol), ethylene glycol (50% vol\/vol), and 2\u2010propanol (50% vol\/vol). In ethyl acetate, both the M\u2010gel and S\u2010gel were highly stabilized; the time required for activity to decay to 80% of the initial activity was increased 29\u2010fold for the M\u2010gel and 20\u2010fold for the S\u2010gel with respect to the soluble enzyme. The G\u2010gel was the least stable of all the derivatives. The different behaviors of the derivatives in thermal and solvent stability studies suggest that each nano\u2010environment contributes differently to the enzyme stability, depending on the denaturing conditions. Therefore, it may be possible to tailor the matrix surface to maximize enzyme stability in particular applications. \u00a9 2002 John Wiley &amp; Sons, Inc. 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