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Mahmoud Karimi

Mahmoud Karimi

Academic rank: Assistant Professor
ORCID: https://orcid.org/0000-0003-2097-7858
Education: PhD.
ScopusId: 55892910300
HIndex:
Faculty: Agriculture and Environment
Address: Arak University
Phone:

Research

Title
Hybrid response surface methodology-genetic algorithm optimization of ultrasound-assisted transesterification of waste oil catalysed by immobilized lipase on mesoporous silica/iron oxide magnetic core-shell nanoparticles
Type
JournalPaper
Keywords
magnetic nanoparticles; immobilized lipase; biodiesel; transesterification; waste cooking oil; response surface methodology; genetic algorithm
Year
2013
Journal Environmental Technology
DOI
Researchers Mahmoud Karimi ، Alireza Keyhani ، Asadolah Akram ، Masoud Rahman ، Bryan Jenkins ، Pieter Stroeve

Abstract

The production of biodiesel by transesterification of waste cooking oil (WCO) to partially substitute petroleum diesel is one of the measures for solving the twin problems of environment pollution and energy demand. An environmentally benign process for the enzymatic transesterification using immobilized lipase has attracted considerable attention for biodiesel production. Here, a superparamagnetic, high surface area substrate for lipase immobilization is evaluated. These immobilization substrates are composed of mesoporous silica/superparamagnetic iron oxide core-shell nanoparticles. The effects of methanol ratio to WCO, lipase concentration, water content and reaction time on the synthesis of biodiesel were analysed by utilizing the response surface methodology (RSM). A quadratic response surface equation for calculating fatty acid methyl ester (FAME) content as the objective function was established based on experimental data obtained in accordance with the central composite design. The RSM-based model was then used as the fitness function for genetic algorithm (GA) to optimize its input space. Hybrid RSM-GA predicted the maximum FAME content (91%) at the optimum level of medium variables: methanol ratio to WCO, 4.34; lipase content, 43.6%; water content, 10.22%; and reaction time, 6 h. Moreover, the immobilized lipase could be used for four times without considerable loss of the activity.