000			01989nam a2200229 a 4500
001			vtls000045085
003			KUKTEM
005			20251114204355.0
008			100204t2009 my a f m 000 0 eng d
020			_aTHE0002249(Local)
039		9	_a201905241118 _bshamsul _c201111250825 _dFida _c201108030915 _dFida _c201107132112 _dVLOAD _y201002041703 _zkam
040			_aUMP
090			_aQP609.A45 N67 2009 rs Thesis
100	0		_aNor Sa'adah Mohamed
245	1	0	_aAmylase immobilization on calcined-kaolin and sodium alginate beads / _cNor Sa'adah Bt Mohamed
260			_aKuantan : _bUMP, _c2009
300			_a45 p. : _bill . ; _c30 cm. + _e1 computer disc
502			_aProject paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang - 2009
520	3		_aThe 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.
650		0	_aAmylases
999			_aVIRTUA40 _c914 _d920
999			_aVTLSSORT0080*0200*0400*0900*1000*2450*2600*3000*5020*5200*6500*9992