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Activity and stability of cross-linked tyrosinase aggregates in aqueous and nonaqueous media

Paper ID Volume ID Publish Year Pages File Format Full-Text
24101 43497 2011 7 PDF Available
Title
Activity and stability of cross-linked tyrosinase aggregates in aqueous and nonaqueous media
Abstract

Cross-linked tyrosinase aggregates were prepared by precipitating the enzyme with ammonium sulfate and subsequent cross-linking with glutaraldehyde. Both activity and stability of these cross-linked enzyme aggregates (CLEAs) in aqueous solution, organic solvents, and ionic liquids have been investigated. Immobilization effectively improved the stability of the enzyme in aqueous solution against various deactivating conditions such as pH, temperature, denaturants, inhibitors, and organic solvents. The stability of the CLEAs in various organic solvents such as tert-butanol (t1/2 = 326.7 h at 40 °C) was significantly enhanced relative to that in aqueous solution (t1/2 = 5.5 h). The effect of thermodynamic water activity (aw) on the CLEA activity in organic media was examined, demonstrating that the enzyme incorporated into CLEAs required an extensive hydration (with an aw approaching 1.0) for optimizing its activity. The impact of ionic liquids on the CLEA activity in aqueous solution was also assessed.

Keywords
Cross-linked enzyme aggregates (CLEAs); Tyrosinase; Thermodynamic water activity; Organic solvents; Ionic liquids (ILs)
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Activity and stability of cross-linked tyrosinase aggregates in aqueous and nonaqueous media
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 152, Issues 1–2, 10 March 2011, Pages 30–36
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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