Site directed mutagenesis to improve phyfauia1 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: Mohd. Salleh, Hamzah, Samsuddin , Nurhusna
Format: Conference or Workshop Item
Language:English
Published: 2011
Subjects:
Online Access:http://irep.iium.edu.my/29245/
http://irep.iium.edu.my/29245/1/hamzah_site_directed.pdf
id iium-29245
recordtype eprints
spelling iium-292452013-02-27T09:25:22Z http://irep.iium.edu.my/29245/ Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed Mohd. Salleh, Hamzah Samsuddin , Nurhusna TP248.13 Biotechnology TP368 Food processing and manufacture 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 o 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 modelling is used to identify and examine the active site of phytase. The factors influencing the ligand binding strength in the active site is 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 mutant shows improvement in activity of phytase. 2011 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/29245/1/hamzah_site_directed.pdf Mohd. Salleh, Hamzah and Samsuddin , Nurhusna (2011) Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed. In: International Conference on Biotechnology Engineering, ICBioE’11, 17-19 May, 2011 , Kuala Lumpur.
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic TP248.13 Biotechnology
TP368 Food processing and manufacture
spellingShingle TP248.13 Biotechnology
TP368 Food processing and manufacture
Mohd. Salleh, Hamzah
Samsuddin , Nurhusna
Site directed mutagenesis to improve phyfauia1 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 o 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 modelling is used to identify and examine the active site of phytase. The factors influencing the ligand binding strength in the active site is 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 mutant shows improvement in activity of phytase.
format Conference or Workshop Item
author Mohd. Salleh, Hamzah
Samsuddin , Nurhusna
author_facet Mohd. Salleh, Hamzah
Samsuddin , Nurhusna
author_sort Mohd. Salleh, Hamzah
title Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed
title_short Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed
title_full Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed
title_fullStr Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed
title_full_unstemmed Site directed mutagenesis to improve phyfauia1 phytase activity for animal feed
title_sort site directed mutagenesis to improve phyfauia1 phytase activity for animal feed
publishDate 2011
url http://irep.iium.edu.my/29245/
http://irep.iium.edu.my/29245/1/hamzah_site_directed.pdf
first_indexed 2023-09-18T20:42:55Z
last_indexed 2023-09-18T20:42:55Z
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