Site directed mutagenesis to improve E. Coli phytase activity for animal feed

Phytate is largely unavailable to monogastric animal such as swine, poultry and fish, as they lack of sufficient endogenous enzymatic activity to hydrolyze phytate. The result is the elimination of precious nutrients that would be beneficial to their growth; furthermore, they will excrete most of th...

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Main Authors:	Samsudin, Nurhusna, Gad, Abd El-Aziem Farouk, Mohd. Salleh, Hamzah
Format:	Article
Language:	English
Published:	INSI Publications 2012
Subjects:	QH426 Genetics TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/23408/ http://irep.iium.edu.my/23408/ http://irep.iium.edu.my/23408/1/123-127_AJBAS.pdf

id	iium-23408
recordtype	eprints
spelling	iium-234082012-06-15T02:04:17Z http://irep.iium.edu.my/23408/ Site directed mutagenesis to improve E. Coli phytase activity for animal feed Samsudin, Nurhusna Gad, Abd El-Aziem Farouk Mohd. Salleh, Hamzah QH426 Genetics TP248.13 Biotechnology Phytate is largely unavailable to monogastric animal such as swine, poultry and fish, as they lack of sufficient endogenous enzymatic activity to hydrolyze phytate. The result is the elimination of precious nutrients that would be beneficial to their growth; furthermore, they will excrete most of the indigestive phytate which can contribute to phosphorus being over applied to the land. Phosphorus has a beneficial impact on vegetative growth on land as well as marine vegetation, causing an increased growth of weeds. This enhanced vegetation consumes large amounts of oxygen, resulting in the loss of aquatic life and ultimately contributes to water pollution and eutrophication of ground water and aquatic environment. Phytase, a type of histidine acid phosphatase hydrolyzes phytin phosphorus and when present in an animal's digestive tract, benefits the animal while reducing total phosphorus levels in manure. Computer modeling has been used to identify and examine the active site of phytase. The factors influencing the ligand binding strength in the active site were analyzed and computational site directed mutagenesis experiments were carried out to evaluate the effects of mutations on the binding strength before and after mutation. From the directive results of computational studies, point mutation was introduced by site directed mutagenesis using polymerase chain reaction (PCR). The activity was measured by kinetic characterization with phytate as a substrate. Decrease in KM notable in all functional mutants indicates that all mutant shows increment in substrate binding. Two functional mutants showed improvement in phytase activity and thermostability. INSI Publications 2012-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/23408/1/123-127_AJBAS.pdf Samsudin, Nurhusna and Gad, Abd El-Aziem Farouk and Mohd. Salleh, Hamzah (2012) Site directed mutagenesis to improve E. Coli phytase activity for animal feed. Australian Journal of Basic and Applied Sciences, 6 (1). pp. 123-127. ISSN 1991-8178 http://www.insipub.com/ajbas/2012/January/123-127.pdf
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	QH426 Genetics TP248.13 Biotechnology
spellingShingle	QH426 Genetics TP248.13 Biotechnology Samsudin, Nurhusna Gad, Abd El-Aziem Farouk Mohd. Salleh, Hamzah Site directed mutagenesis to improve E. Coli phytase activity for animal feed
description	Phytate is largely unavailable to monogastric animal such as swine, poultry and fish, as they lack of sufficient endogenous enzymatic activity to hydrolyze phytate. The result is the elimination of precious nutrients that would be beneficial to their growth; furthermore, they will excrete most of the indigestive phytate which can contribute to phosphorus being over applied to the land. Phosphorus has a beneficial impact on vegetative growth on land as well as marine vegetation, causing an increased growth of weeds. This enhanced vegetation consumes large amounts of oxygen, resulting in the loss of aquatic life and ultimately contributes to water pollution and eutrophication of ground water and aquatic environment. Phytase, a type of histidine acid phosphatase hydrolyzes phytin phosphorus and when present in an animal's digestive tract, benefits the animal while reducing total phosphorus levels in manure. Computer modeling has been used to identify and examine the active site of phytase. The factors influencing the ligand binding strength in the active site were analyzed and computational site directed mutagenesis experiments were carried out to evaluate the effects of mutations on the binding strength before and after mutation. From the directive results of computational studies, point mutation was introduced by site directed mutagenesis using polymerase chain reaction (PCR). The activity was measured by kinetic characterization with phytate as a substrate. Decrease in KM notable in all functional mutants indicates that all mutant shows increment in substrate binding. Two functional mutants showed improvement in phytase activity and thermostability.
format	Article
author	Samsudin, Nurhusna Gad, Abd El-Aziem Farouk Mohd. Salleh, Hamzah
author_facet	Samsudin, Nurhusna Gad, Abd El-Aziem Farouk Mohd. Salleh, Hamzah
author_sort	Samsudin, Nurhusna
title	Site directed mutagenesis to improve E. Coli phytase activity for animal feed
title_short	Site directed mutagenesis to improve E. Coli phytase activity for animal feed
title_full	Site directed mutagenesis to improve E. Coli phytase activity for animal feed
title_fullStr	Site directed mutagenesis to improve E. Coli phytase activity for animal feed
title_full_unstemmed	Site directed mutagenesis to improve E. Coli phytase activity for animal feed
title_sort	site directed mutagenesis to improve e. coli phytase activity for animal feed
publisher	INSI Publications
publishDate	2012
url	http://irep.iium.edu.my/23408/ http://irep.iium.edu.my/23408/ http://irep.iium.edu.my/23408/1/123-127_AJBAS.pdf
first_indexed	2023-09-18T20:35:25Z
last_indexed	2023-09-18T20:35:25Z
_version_	1777409013265203200

Site directed mutagenesis to improve E. Coli phytase activity for animal feed

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