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Amylase immobilization on calcined-kaolin and sodium alginate beads / Nor Sa'adah Bt Mohamed

By:

Nor Sa'adah Mohamed

Material type: Text

TextPublication details: Kuantan : UMP, 2009Description: 45 p. : ill . ; 30 cm. + 1 computer discISBN:

THE0002249(Local)

Subject(s):

Amylases

Dissertation note: Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang - 2009 Abstract: The objective of this research was to study the techniques for α-amylase immobilization on two different support materials. α-Amylase from Bacillus sp was immobilized by two different techniques which were physical adsorption onto calcined-kaolin and entrapment in sodium alginate beads. The advantages of attaching enzymes to a solid support and a few of the major reasons are single batch of enzyme can be used either multiple or repetitive and at the same time it can save cost. The immobilized α-amylase exhibited better thermostability than the free one. It is believed that kaolin and alginates has tremendous potential to be utilized as solid support material. It was estimated that the percentage of protein loading was 59% for adsorption onto calcined-kaolin, whereas for entrapment in sodium alginate, 74% of protein was immobilized. The immobilized α-amylase was tested for its capacity of converting starch into glucose, as well as its optimum pH and temperature. The optimum pH and temperature for both immobilized α-amylase were found to be pH 8 and 70°C, respectively.

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Holdings ( 2 )
Title notes ( 2 )

Holdings
Item type	Current library	Call number	Copy number	Status	Date due	Barcode
Final Year Report	UMPLIB GAMBANG	QP609.A45 N67 2009 rs Thesis (Browse shelf(Opens below))	1	Not for loan		0000042953
Final Year Report	UMPLIB GAMBANG	CD 4008 \| QP609.A45 N67 2009 rs Thesis (Browse shelf(Opens below))	1	Not for loan		0000042954

Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang - 2009

The objective of this research was to study the techniques for α-amylase immobilization on two different support materials. α-Amylase from Bacillus sp was immobilized by two different techniques which were physical adsorption onto calcined-kaolin and entrapment in sodium alginate beads. The advantages of attaching enzymes to a solid support and a few of the major reasons are single batch of enzyme can be used either multiple or repetitive and at the same time it can save cost. The immobilized α-amylase exhibited better thermostability than the free one. It is believed that kaolin and alginates has tremendous potential to be utilized as solid support material. It was estimated that the percentage of protein loading was 59% for adsorption onto calcined-kaolin, whereas for entrapment in sodium alginate, 74% of protein was immobilized. The immobilized α-amylase was tested for its capacity of converting starch into glucose, as well as its optimum pH and temperature. The optimum pH and temperature for both immobilized α-amylase were found to be pH 8 and 70°C, respectively.