01989nam a2200229 a 4500 vtls000045085 KUKTEM 20251114204355.0 100204t2009 my a f m 000 0 eng d THE0002249(Local) 201905241118 shamsul 201111250825 Fida 201108030915 Fida 201107132112 VLOAD 201002041703 kam UMP QP609.A45 N67 2009 rs Thesis Nor Sa'adah Mohamed Amylase immobilization on calcined-kaolin and sodium alginate beads / Nor Sa'adah Bt Mohamed Kuantan : UMP, 2009 45 p. : ill . ; 30 cm. + 1 computer disc 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. Amylases 0 0 0 1 10000 10000 2019-09-04 0 QP609.A45 N67 2009 rs Thesis 0000042953 2019-09-04 00:00:00 1 2019-09-04 PSM 0 0 0 1 10000 10000 2019-09-04 0 CD 4008 | QP609.A45 N67 2009 rs Thesis 0000042954 2019-09-04 00:00:00 1 2019-09-04 PSM VIRTUA40 914 920 VTLSSORT0080*0200*0400*0900*1000*2450*2600*3000*5020*5200*6500*9992