Optimization of medium formulation on production of recombinant chitinase in escherichia coli

Chitinase is enzyme that hydrolyzing chitin to produce N-acetyl- glucosamine. Chitinase can be found in bacteria, fungi, higher plant, insect and some vertebrates. There are a lots of applications of chitinase as the demands of the enzyme is rising high in the market due to usage in pharmaceutical,...

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Main Author:	Mohd Faris, Mohd Yunus
Format:	Undergraduates Project Papers
Language:	English
Published:	2010
Subjects:	QC Physics
Online Access:	http://umpir.ump.edu.my/id/eprint/3272/ http://umpir.ump.edu.my/id/eprint/3272/ http://umpir.ump.edu.my/id/eprint/3272/1/CD5856_MOHD_FARIS_MOHD_YUNUS.pdf

id	ump-3272
recordtype	eprints
spelling	ump-32722015-03-03T08:00:16Z http://umpir.ump.edu.my/id/eprint/3272/ Optimization of medium formulation on production of recombinant chitinase in escherichia coli Mohd Faris, Mohd Yunus QC Physics Chitinase is enzyme that hydrolyzing chitin to produce N-acetyl- glucosamine. Chitinase can be found in bacteria, fungi, higher plant, insect and some vertebrates. There are a lots of applications of chitinase as the demands of the enzyme is rising high in the market due to usage in pharmaceutical, biopesticides or food industry. For this study, chitinase enzyme was expressed in recombinant bacteria using Escherichia coli as a host. The effect of various medium on expression of chitinase in Escherichia coli was conducted in this research. Five medium were studied. LB, TB, SB, SOB and 2x YT were screened. LB medium gave the best result of highest chitinase enzyme activity. Each component of LB medium was study to determine the optimize amount of composition to produce the highest enzyme activity. The best range of every composition obtained from the conventional method was 3.0 g/l to 7.0 g/l for sodium chloride, 1.5 g/l to 4.5 g/l for yeast extract and 10 g/l to 14 g/l for tryptone. The optimization was done using response surface methodology (RSM) conducted by software named Design Expert. The optimal medium composition for high soluble recombinant chitinase was determined as 3.63 g/l of sodium chloride, 4.50 g/l of yeast extract and 13.11 g/l of tryptone. From the experimental, the enzyme activity after optimization was achieved 2.291 U/ml compared to predicted response of 2.409 U/ml. This result shows increment of the activity for 82% than before the optimization which is 0.411 U/ml. It shows that the optimization of the medium formulation to improve the expression and production of chitinase was successfully conducted by using RSM. 2010-04 Undergraduates Project Papers NonPeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/3272/1/CD5856_MOHD_FARIS_MOHD_YUNUS.pdf Mohd Faris, Mohd Yunus (2010) Optimization of medium formulation on production of recombinant chitinase in escherichia coli. Faculty of Chemical & Natural Resources Engineering , Universiti Malaysia Pahang . http://iportal.ump.edu.my/lib/item?id=chamo:58608&theme=UMP2
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Malaysia Pahang
building	UMP Institutional Repository
collection	Online Access
language	English
topic	QC Physics
spellingShingle	QC Physics Mohd Faris, Mohd Yunus Optimization of medium formulation on production of recombinant chitinase in escherichia coli
description	Chitinase is enzyme that hydrolyzing chitin to produce N-acetyl- glucosamine. Chitinase can be found in bacteria, fungi, higher plant, insect and some vertebrates. There are a lots of applications of chitinase as the demands of the enzyme is rising high in the market due to usage in pharmaceutical, biopesticides or food industry. For this study, chitinase enzyme was expressed in recombinant bacteria using Escherichia coli as a host. The effect of various medium on expression of chitinase in Escherichia coli was conducted in this research. Five medium were studied. LB, TB, SB, SOB and 2x YT were screened. LB medium gave the best result of highest chitinase enzyme activity. Each component of LB medium was study to determine the optimize amount of composition to produce the highest enzyme activity. The best range of every composition obtained from the conventional method was 3.0 g/l to 7.0 g/l for sodium chloride, 1.5 g/l to 4.5 g/l for yeast extract and 10 g/l to 14 g/l for tryptone. The optimization was done using response surface methodology (RSM) conducted by software named Design Expert. The optimal medium composition for high soluble recombinant chitinase was determined as 3.63 g/l of sodium chloride, 4.50 g/l of yeast extract and 13.11 g/l of tryptone. From the experimental, the enzyme activity after optimization was achieved 2.291 U/ml compared to predicted response of 2.409 U/ml. This result shows increment of the activity for 82% than before the optimization which is 0.411 U/ml. It shows that the optimization of the medium formulation to improve the expression and production of chitinase was successfully conducted by using RSM.
format	Undergraduates Project Papers
author	Mohd Faris, Mohd Yunus
author_facet	Mohd Faris, Mohd Yunus
author_sort	Mohd Faris, Mohd Yunus
title	Optimization of medium formulation on production of recombinant chitinase in escherichia coli
title_short	Optimization of medium formulation on production of recombinant chitinase in escherichia coli
title_full	Optimization of medium formulation on production of recombinant chitinase in escherichia coli
title_fullStr	Optimization of medium formulation on production of recombinant chitinase in escherichia coli
title_full_unstemmed	Optimization of medium formulation on production of recombinant chitinase in escherichia coli
title_sort	optimization of medium formulation on production of recombinant chitinase in escherichia coli
publishDate	2010
url	http://umpir.ump.edu.my/id/eprint/3272/ http://umpir.ump.edu.my/id/eprint/3272/ http://umpir.ump.edu.my/id/eprint/3272/1/CD5856_MOHD_FARIS_MOHD_YUNUS.pdf
first_indexed	2023-09-18T21:57:26Z
last_indexed	2023-09-18T21:57:26Z
_version_	1777414172738322432

Optimization of medium formulation on production of recombinant chitinase in escherichia coli

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