Sina Aghili

Abstracts

2 Determination of Effect Factor for Effective Parameter on Saccharification of Lignocellulosic Material by Concentrated Acid

Authors: Sina Aghili, Ali Arasteh Nodeh

Abstract:

Tamarisk usage as a new group of lignocelluloses material to produce fermentable sugars in bio-ethanol process was studied. The overall aim of this work was to establish the optimum condition for acid hydrolysis of this new material and a mathematical model predicting glucose release as a function of operation variable. Sulfuric acid concentration in the range of 20 to 60%(w/w), process temperature between 60 to 95oC, hydrolysis time from 120 to 240 min and solid content 5,10,15%(w/w) were used as hydrolysis conditions. HPLC was used to analysis of the product. This analysis indicated that glucose was the main fermentable sugar and was increased with time, temperature and solid content and acid concentration was a parabola influence in glucose production.The process was modeled by a quadratic equation. Curve study and model were found that 42% acid concentration, 15 % solid content and 90oC were in optimum condition.

Keywords: Wood, Hydrolysis, saccharification, fermentable sugar

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1 Immobilization of Enzymes and Proteins on Epoxy-Activated Supports

Authors: Afshin Farahbakhsh, Ehsan Khorshidian, Sina Aghili

Abstract:

Enzymes are promising biocatalysts for many organic reactions. They have excellent features like high activity, specificity and selectivity, and can catalyze under mild and environment friendly conditions. Epoxy-activated supports are almost-ideal ones to perform very easy immobilization of proteins and enzymes at both laboratory and industrial scale. The activated epoxy supports (chitosan/alginate, Eupergit C) may be very suitable to achieve the multipoint covalent attachment of proteins and enzymes, therefore, to stabilize their three-dimensional structure. The enzyme is firstly covalently immobilized under conditions pH 7.0 and 10.0. The remaining groups of the support are blocked to stop additional interaction between the enzyme and support by mercaptoethanol or Triton X-100. The results show support allowed obtaining biocatalysts with high immobilized protein amount and hydrolytic activity. The immobilization of lipases on epoxy support may be considered as attractive tool for obtaining highly active biocatalysts to be used in both aqueous and anhydrous aqueous media.

Keywords: immobilization of enzymes, epoxy supports, enzyme multipoint covalent attachment, microbial lipases

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