Modification and characterization of phytases for animal feed production /

Phytases catalyze the hydrolysis phytic acid and are able to improve the nutritional quality of phytate rich diet. Monogastric animal such as poultry and fish have lack of significant activity to hydrolyze phytate that contributes to elimination of beneficial nutrient for growth and therefore, contr...

Full description

Saved in:
Bibliographic Details
Main Author: Nurhusna Binti Samsudin (Author)
Format: Thesis
Language:English
Published: Kuala Lumpur : Kulliyyah of Engineering, International Islamic University Malaysia, 2012
Subjects:
Online Access:Click here to view 1st 24 pages of the thesis. Members can view fulltext at the specified PCs in the library.
Tags: Add Tag
No Tags, Be the first to tag this record!
LEADER 042560000a22004330004500
008 130307s2012 my a f m 000 0 eng d
040 |a UIAM  |b eng  |e rda 
041 |a eng 
043 |a a-my--- 
050 0 0 |a TP248.65.E59 
100 0 |a Nurhusna Binti Samsudin,  |e author 
245 1 0 |a Modification and characterization of phytases for animal feed production /  |c by Nurhusna Binti Samsudin 
264 1 |a Kuala Lumpur :  |b Kulliyyah of Engineering, International Islamic University Malaysia,  |c 2012 
300 |a xvii, 142 leaves :  |b illustrations ;  |c 30cm. 
336 |2 rdacontent  |a text 
337 |2 rdamedia  |a unmediated 
337 |2 rdamedia  |a computer 
338 |2 rdacarrier  |a volume 
338 |2 rdacarrier  |a computer disc 
338 |2 rdacarrier  |a online resource 
347 |2 rdaft  |a text file  |b PDF 
500 |a Abstracts in English and Arabic. 
500 |a " A thesis submitted in fulfilment of the requirement for the degree of Master of Science in Biotechnology Engineering."--On title page. 
502 |a Thesis (MSBTE)--International Islamic University Malaysia, 2012. 
504 |a Includes bibliographical references (leaves 125-134) 
520 |a Phytases catalyze the hydrolysis phytic acid and are able to improve the nutritional quality of phytate rich diet. Monogastric animal such as poultry and fish have lack of significant activity to hydrolyze phytate that contributes to elimination of beneficial nutrient for growth and therefore, contribute to land pollution, eutrophication of ground water and aquatic environment. In addition, it leads to the negative effect on vitamin utilization that leads to the emaciation, retarded growth and reproductive failure to animals. Due to the importance of microbial sources for the commercial production of phytases, a waste water bacterium phytase is the subject of interest in this work. In silica experiment is used to identify and examine the active site of waste water bacterium 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 ligand binding strength. From the directive results of computational studies, point mutation was introduced by site directed mutagenesis using polymerase chain reaction (PCR). Mutagenesis is achieved by two step PCR megaprimer procedure. After mutants of PhyFAUIAl were generated, variants were expressed in Escherichia coli (DH5a) and characterized for improved catalytic properties. Detailed studies on kinetic stability and the thermostability of the mutational variants M2 l 6R, E2 l 9R and A 116T, and the respective multiple mutants M216R/E219R and M216R/E2 l 9R/F254E are presented. The selected substitutions at position M216R and A 116T improved the catalytic activity relative to the wild type enzyme. Thermostability study showed that variant M216R showed over 28% improvement in thermostability (90°C for 30 minutes) and 6.2°C increased in melting temperature (T111) over wild type en:z;yme. Structural predictions suggest that substitution of M216R might introduce additional hydrogen bonds with adjacent residues, improving the enzymes thermostability by stabilizing local interaction. 
596 |a 1 
650 0 |a Microbial enzymes  |x Biotechnology 
650 0 |a Phytases 
650 0 |a Enzymes in animal nutrition 
655 7 |a Theses, IIUM local 
690 |a Dissertations, Academic  |x Department of Biotechnology Engineering.  |z IIUM 
710 2 |a International Islamic University Malaysia.  |b Department of Biotechnology Engineering. 
856 |u http://studentrepo.iium.edu.my/handle/123456789/5002  |z Click here to view 1st 24 pages of the thesis. Members can view fulltext at the specified PCs in the library. 
900 |a sbh-aaz-naw 
999 |c 438288  |c 438288  |d 468999  |d 468999 
999 |c 438288  |c 438288  |d 468999  |d 468999 
952 |0 0  |6 T TP 000248.65 E59 N974M 2012  |7 0  |8 THESES  |9 758727  |a IIUM  |b IIUM  |c MULTIMEDIA  |g 0.00  |o t TP 248.65 E59 N974M 2012  |p 00011282805  |r 2018-10-01  |t 1  |v 0.00  |y THESIS 
952 |0 0  |6 TS CDF TP 248.65 E59 N974M 2012  |7 0  |8 THESES  |9 850524  |a IIUM  |b IIUM  |c MULTIMEDIA  |g 0.00  |o ts cdf TP 248.65 E59 N974M 2012  |p 00011105440  |r 2020-06-25  |t 1  |v 0.00  |y THESISDIG