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Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli

Chitinase generally referred as endochitinases is randomly hydrolyzing chitin to produce N-acetyl-glucosamine. In addition, chitinase play an important role in chitin metabolism of microorganism for production of carbon and energy source. Chitinase can be found in bacteria, fungi, virus and higher p...

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Main Author: Nor Fadzillah Hanis, Abu Sulaiman
Format: Undergraduates Project Papers
Language:English
Published: 2009
Subjects:
QP Physiology
Online Access:http://umpir.ump.edu.my/id/eprint/1157/1/CD4014.pdf
http://umpir.ump.edu.my/id/eprint/1157/
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spelling my.ump.umpir.11572021-06-17T06:54:37Z http://umpir.ump.edu.my/id/eprint/1157/ Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli Nor Fadzillah Hanis, Abu Sulaiman QP Physiology Chitinase generally referred as endochitinases is randomly hydrolyzing chitin to produce N-acetyl-glucosamine. In addition, chitinase play an important role in chitin metabolism of microorganism for production of carbon and energy source. Chitinase can be found in bacteria, fungi, virus and higher plant. There are a lot of applications of chitinase either in pharmaceutical, biopestisides or food industry. For this research, chitinase was expressed in recombinant bacteria using Escherichia Coli as a host. The optimization was carried out by using response surface methodology. Focusing on two parameters which are inoculum size and agitation rate, the optimum condition was identified to enhance the process of chitinase production. The chitinase was expressed in different inoculum size at 0.5, 1.0, 1.5, 2.0, 2.5 and 3.0 mL. Then the experiment continued observed in different agitation rate at 50, 100, 150, 200, 250 and 300 rpm. After overall observation, the best range of inoculum size gave between 0.8 mL to 1.2 mL and the range of agitation rate was identified between 230 rpm to 270 rpm. The best range of culture conditions was used for further study using Respond Surface Methodology (RSM). The optimal set of culture conditions for high soluble recombinant chitinase was determined as an inoculum size of 0.98 mL and 244.7 rpm of agitation rate. From the experimental value, the optimal production of recombinant chitinase was achieved 0.376 U/mL. This shows the 1.57-fold increment compared to the initial experiment which produced 0.239 U/mL of chitinase activity. These conditions successfully enhance the production of chitinase by using recombinant protein in Escherichia coli. 2009-04 Undergraduates Project Papers NonPeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/1157/1/CD4014.pdf Nor Fadzillah Hanis, Abu Sulaiman (2009) Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli. Faculty of Chemical & Natural Resources Engineering , Universiti Malaysia Pahang .
institution Universiti Malaysia Pahang
building UMP Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Pahang
content_source UMP Institutional Repository
url_provider http://umpir.ump.edu.my/
language English
topic QP Physiology
spellingShingle QP Physiology
Nor Fadzillah Hanis, Abu Sulaiman
Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli
description Chitinase generally referred as endochitinases is randomly hydrolyzing chitin to produce N-acetyl-glucosamine. In addition, chitinase play an important role in chitin metabolism of microorganism for production of carbon and energy source. Chitinase can be found in bacteria, fungi, virus and higher plant. There are a lot of applications of chitinase either in pharmaceutical, biopestisides or food industry. For this research, chitinase was expressed in recombinant bacteria using Escherichia Coli as a host. The optimization was carried out by using response surface methodology. Focusing on two parameters which are inoculum size and agitation rate, the optimum condition was identified to enhance the process of chitinase production. The chitinase was expressed in different inoculum size at 0.5, 1.0, 1.5, 2.0, 2.5 and 3.0 mL. Then the experiment continued observed in different agitation rate at 50, 100, 150, 200, 250 and 300 rpm. After overall observation, the best range of inoculum size gave between 0.8 mL to 1.2 mL and the range of agitation rate was identified between 230 rpm to 270 rpm. The best range of culture conditions was used for further study using Respond Surface Methodology (RSM). The optimal set of culture conditions for high soluble recombinant chitinase was determined as an inoculum size of 0.98 mL and 244.7 rpm of agitation rate. From the experimental value, the optimal production of recombinant chitinase was achieved 0.376 U/mL. This shows the 1.57-fold increment compared to the initial experiment which produced 0.239 U/mL of chitinase activity. These conditions successfully enhance the production of chitinase by using recombinant protein in Escherichia coli.
format Undergraduates Project Papers
author Nor Fadzillah Hanis, Abu Sulaiman
author_facet Nor Fadzillah Hanis, Abu Sulaiman
author_sort Nor Fadzillah Hanis, Abu Sulaiman
title Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli
title_short Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli
title_full Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli
title_fullStr Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli
title_full_unstemmed Optimization of inoculum size & agitation rate on expression of recombinant chitinase in Escherichia coli
title_sort optimization of inoculum size & agitation rate on expression of recombinant chitinase in escherichia coli
publishDate 2009
url http://umpir.ump.edu.my/id/eprint/1157/1/CD4014.pdf
http://umpir.ump.edu.my/id/eprint/1157/
_version_ 1703960642767028224
score 13.211869

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