Crosslinking of enzymes for improved stability and performance
Current Opinion in Biotechnology, ISSN: 0958-1669, Vol: 10, Issue: 4, Page: 331-335
1999
- 160Citations
- 73Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations160
- Citation Indexes160
- 160
- CrossRef124
- Captures73
- Readers73
- 73
Article Description
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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0958166999800603; http://dx.doi.org/10.1016/s0958-1669(99)80060-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033179495&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10449320; http://linkinghub.elsevier.com/retrieve/pii/S0958166999800603; http://api.elsevier.com/content/article/PII:S0958166999800603?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0958166999800603?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0958166999800603; http://dx.doi.org/10.1016/s0958-1669%2899%2980060-3; https://dx.doi.org/10.1016/s0958-1669%2899%2980060-3
Elsevier BV
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