Native and Biotechnologically Engineered Plant Proteases with Industrial Applications
Food and Bioprocess Technology, ISSN: 1935-5130, Vol: 4, Issue: 6, Page: 1066-1088
2011
- 124Citations
- 272Captures
- 6Mentions
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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.
Review Description
Proteases occupy the most relevant position among industrial enzymes. Plant proteases have been used in medicine, detergent manufacturing, and food science for many years, but their production is diminishing in favor of those of microbial origin because lower production costs. Papain, bromelain, and ficin are the most frequently employed plant proteases, although new proteases with new and more appealing physicochemical properties for industry are still emerging. DNA technology and genetic engineering shall play, without a doubt, an important role for the production of these proteases at the industrial level. The present review focuses on the applications of traditional plant proteases as well as new proteases discovered during the last 20 years, some of which have already been genetically engineered either to increase production or to strengthen some of their physicochemical properties. The review also refers to the protease classification, action pattern, and main characteristics. © 2010 Springer Science + Business Media, LLC.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79958262740&origin=inward; http://dx.doi.org/10.1007/s11947-010-0431-4; http://link.springer.com/10.1007/s11947-010-0431-4; http://www.springerlink.com/index/10.1007/s11947-010-0431-4; http://www.springerlink.com/index/pdf/10.1007/s11947-010-0431-4; https://dx.doi.org/10.1007/s11947-010-0431-4; https://link.springer.com/article/10.1007/s11947-010-0431-4
Springer Science and Business Media LLC
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