scispace - formally typeset
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.

Papers
More filters
Journal ArticleDOI

Immobilization of laccase on epoxy-functionalized silica and its application in biodegradation of phenolic compounds.

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.
Journal ArticleDOI

Enzymatic production of biodiesel using lipases immobilized on silica nanoparticles as highly reusable biocatalysts: effect of water, t-butanol and blue silica gel contents

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

Covalent binding of hyper-activated Rhizomucor miehei lipase (RML) on hetero-functionalized siliceous supports

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.