شانزدهمین کنفرانس سراسری و چهارمین کنفرانس بین المللی زیست شناسی ایران , 2010-09-14

Title : ( Isolation and purification of lysozyme from hen egg wight )

Authors: Ahmad Asoodeh , ,

Citation: BibTeX | EndNote

Abstract

Hen’s egg white has four proteins (ovalbumin, ovotransferin, ovomucoid, lysozyme) that they have several utilities. Ten percent of the weight of it, is protein. Lysozyme has 129 amino acids with the weight of 14.4kD. This enzyme has pH optimum of 9.2 for its activation and the range of the pI is from 10.5 to 11. It has 4 disulfide bonds. 0.3 percent of its weight is sugar. It is antibacterial protein and has biological applications. We can find it in different resources like: animals, plants, a few bacteria and the Hen’s egg white, that’s the most important of them and the most studies, have been done on this enzyme. In this study, we applied the easy way for purifying of Lysozyme. We use SP-sepharose chromatography and extract the enzyme in one-step. The advantages of this method: 1-availability of its redoing, 2- high efficacy 3-we can do it in high or low criteria, 4- its purification is in one step, which have a high commercial importance

Keywords

, Hen Egg White Lysozyme, Purification, Chromatography
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@inproceedings{paperid:1017971,
author = {Asoodeh, Ahmad and , },
title = {Isolation and purification of lysozyme from hen egg wight},
booktitle = {شانزدهمین کنفرانس سراسری و چهارمین کنفرانس بین المللی زیست شناسی ایران},
year = {2010},
location = {مشهد, IRAN},
keywords = {Hen Egg White Lysozyme; Purification; Chromatography},
}

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%0 Conference Proceedings
%T Isolation and purification of lysozyme from hen egg wight
%A Asoodeh, Ahmad
%A ,
%J شانزدهمین کنفرانس سراسری و چهارمین کنفرانس بین المللی زیست شناسی ایران
%D 2010

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