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Crosslinking of enzymes for improved stability and performance
Stabilization of enzymes without diminishing and diluting their activity is crucial for their use as industrial catalysts. One practically proven approach involves crystallization of the enzyme (size 1–200 μm) followed by subsequent crosslinking. In many cases, the resulting crosslinked enzyme cryst...
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Published in: | Current opinion in biotechnology 1999-08, Vol.10 (4), p.331-335 |
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Main Author: | |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Stabilization of enzymes without diminishing and diluting their activity is crucial for their use as industrial catalysts. One practically proven approach involves crystallization of the enzyme (size 1–200 μm) followed by subsequent crosslinking. In many cases, the resulting crosslinked enzyme crystals exhibit increased storage stability as well as stability in applications. The technology is complementary to protein engineering methods that aim at boosting the inherent stability of the enzyme. |
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ISSN: | 0958-1669 1879-0429 |
DOI: | 10.1016/S0958-1669(99)80060-3 |