000			02022nam a2200241 a 4500
001			vtls000058052
003			KUKTEM
005			20251114204507.0
008			111227t2010 my da f m 000 0 eng d
020			_aTHE0004142(Local)
039		9	_a201905132127 _bfarhana _y201112271521 _zFida
040			_aUMP
090			_aTP156.F5 H39 2010 rs Bc.
100	0		_aHazman Abd Mulok
245	1	0	_aWhey protein fractionation based on sp-sepharose cation exchange chromatography / _cHazman Abd Mulok
260			_aKuantan, Pahang : _bUMP, _c2010
300			_axiv, 50 p. : _bill. (some col.) ; _c30 cm. + _e1 CD-ROM
502			_aProject paper (Bachelor of Chemical Engineering) -- Universiti Malaysia Pahang - 2010
504			_aBibliography: p. 40-41
520			_aBovine whey protein consists of different type of proteins such as βlactoglobulin (β-lag), α-lactalbumin (α-lac), immunoglobulin, bovine serum albumin (BSA), lactoferrin, lactoperoxidase and glycomacropeptide. Single protein is more valuable compare to the mixture of proteins and it can be used for specific application. The main objective of this study is to fractionate whey protein components into several groups or single protein fraction using SP-sepharose TM Fast Flow (Amersham Biosciences) cation exchange chromatography column. The chromatographic process was run at different pH range from pH 4 to pH 8 using 24 ml column. All major whey proteins were recovered in the elution fraction at pH 4 and pH 4.5. No protein was bound at pH 7 and pH 8. The best whey fractionation from 2 ml whey feed was achieved at pH 4 with the yield for β-lag, BSA and α-lac are 83.33%, 66.44% and 10.51% respectively. Different protein fraction recovered during fractionation process at different pH using cation exchange chromatography process, can be used as a guideline to isolate particular protein of interest from bovine whey.
650		0	_aUltrafiltration
999			_aVIRTUA40 _c2999 _d3005
999			_aVTLSSORT0080*0200*0400*0900*1000*2450*2600*3000*5020*5040*5200*6500*9992