M
Maryam Yousefi
Researcher at Avicenna Research Institute
Publications - 62
Citations - 1384
Maryam Yousefi is an academic researcher from Avicenna Research Institute. The author has contributed to research in topics: Lipase & Chemistry. The author has an hindex of 18, co-authored 48 publications receiving 946 citations. Previous affiliations of Maryam Yousefi include Shahid Chamran University of Ahvaz & Shahid Beheshti University.
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Journal ArticleDOI
Immobilization of laccase on epoxy-functionalized silica and its application in biodegradation of phenolic compounds.
Mehdi Mohammadi,Mohammad Ali As’habi,Peyman Salehi,Maryam Yousefi,Mahboobeh Nazari,Jesper Brask +5 more
TL;DR: The immobilized enzyme was found to be stabilized compared to the free enzyme, and the performance of the biocatalyst was evaluated by the degradation of phenolic compounds including phenol, p-chlorophenol and catechol.
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Enzymatic production of biodiesel using lipases immobilized on silica nanoparticles as highly reusable biocatalysts: effect of water, t-butanol and blue silica gel contents
Mohadese Babaki,Maryam Yousefi,Zohreh Habibi,Mehdi Mohammadi,Parisa Yousefi,Javad Mohammadi,Jesper Brask +6 more
TL;DR: In this paper, the effect of water, t-butanol and blue silica gel as water adsorbent on the yield of biodiesel by methanolysis of canola oil was studied using self-made biocatalysts.
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Preparation of highly reusable biocatalysts by immobilization of lipases on epoxy-functionalized silica for production of biodiesel from canola oil
TL;DR: It was found that lipases immobilized on silica provided biocatalyst derivatives with lower cost compared with the cost of commercially available Novozym 435 and also presented a good reusability.
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Process optimization for biodiesel production from waste cooking oil using multi-enzyme systems through response surface methodology
TL;DR: In this paper, a multi-enzyme system was developed to produce biodiesel with waste cooking oil and methanol, and a quadratic polynomial equation was obtained for methanolysis reaction by multiple regression analysis.
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Covalent binding of hyper-activated Rhizomucor miehei lipase (RML) on hetero-functionalized siliceous supports
Maryam Garmroodi,Mehdi Mohammadi,Ali Ramazani,Maryam Ashjari,Javad Mohammadi,Behrouz Sabour,Maryam Yousefi +6 more
TL;DR: The results showed that immobilization of RML on octyl-functionalized supports produces specific activity almost 1.5-2 folds greater than the specific activity of the free enzyme, confirming the enhancement of covalent nature of the attachment.