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Protein purification by using immobilied metal ions affinity zeolite adsorbent / Su Najwa Mohamed

By:

Su Najwa Mohamed

Material type: Text

TextPublication details: Kuantan, Pahang : UMP, 2010Description: xv, 76 p. : ill. (some col.) ; 30 cm. + 1 CD-ROMISBN:

THE0004536(Local)

Subject(s):

Protein -- Purification

Dissertation note: Project paper (Bachelor of Chemical Engineering) -- Universiti Malaysia Pahang - 2010 Abstract: The applications for purified proteins have grown considerably over recent years due to their biological and nutritional properties. The aim of this research are to develop zeolite as inorganic stationary substrate in immobilized metal ion affinity (IMA) for protein purification and to study the optimum condition to purify protein in order to maximize yield and purity of protein by applying the principle of adsorption process. The effect of contact time, different types of adsorbent and various pH values were studied in a batch experiment by using Bovine Serum Albumin (BSA) as protein sample. The sorption equilibrium was reached within 10 minutes. Fe3+ ion showed the best performance for BSA and has the suitable interaction with both HY and HBeta zeolite framework and the protein as compared to Pb2+, Ni2+ ions. The adsorption capacity for BSA was found to be the highest at pH 4.5 that is close to isoelectric point (pI) with Fe- HBeta used as adsorbent. The adsorbed amount increases as the pH increases and reduces as the pH exceeds the pI value. This result proves that adsorption capacity of Bovine Serum Albumin depends on the types of adsorbent used, which means the adsorption stoichiometries depends on physical characteristic of adsorbent that could increase and reduce the adsorption capacity of the protein as well as the pH of protein. The adsorption isotherm data of BSA is well fitted to the Langmuir isotherm model.

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Holdings ( 2 )
Title notes ( 3 )

Holdings
Item type	Current library	Call number	Copy number	Status	Date due	Barcode
Final Year Report	UMPLIB GAMBANG	TP248.65.P76 S86 2010 rs Bc. (Browse shelf(Opens below))	1	Not for loan		0000063066
Final Year Report	UMPLIB GAMBANG	CD 5808 \| TP248.65.P76 S86 2010 rs Bc. (Browse shelf(Opens below))	1	Not for loan		0000063067

Project paper (Bachelor of Chemical Engineering) -- Universiti Malaysia Pahang - 2010

Bibliography : p. [59]-62

The applications for purified proteins have grown considerably over recent years due to their biological and nutritional properties. The aim of this research are to develop zeolite as inorganic stationary substrate in immobilized metal ion affinity (IMA) for protein purification and to study the optimum condition to purify protein in order to maximize yield and purity of protein by applying the principle of adsorption process. The effect of contact time, different types of adsorbent and various pH values were studied in a batch experiment by using Bovine Serum Albumin (BSA) as protein sample. The sorption equilibrium was reached within 10 minutes. Fe3+ ion showed the best performance for BSA and has the suitable interaction with both HY and HBeta zeolite framework and the protein as compared to Pb2+, Ni2+ ions. The adsorption capacity for BSA was found to be the highest at pH 4.5 that is close to isoelectric point (pI) with Fe- HBeta used as adsorbent. The adsorbed amount increases as the pH increases and reduces as the pH exceeds the pI value. This result proves that adsorption capacity of Bovine Serum Albumin depends on the types of adsorbent used, which means the adsorption stoichiometries depends on physical characteristic of adsorbent that could increase and reduce the adsorption capacity of the protein as well as the pH of protein. The adsorption isotherm data of BSA is well fitted to the Langmuir isotherm model.