03156ntm a2200277 a 4500 vtls000084693 KUKTEM 20251117113251.0 141224t2014 my a f m 000 0 eng d THE0003877(Local) 201905161516 shah 201712061027 huda 201412241442 fawwaz UMP TP156.C5 A36 2014 r Bc. Siti Nor Ainda Mazlan Mixed matrix membrane chromatography based on lewatit mp500 anion exchanger resin and lewatit cnp105 cation exchanger resin for whey protein fractionation / Siti Nor Ainda Mazlan Kuantan, Pahang : UMP, 2014 xv, 73 p. : ill. ; 30 cm. + 1 CD-ROM Faculty of Chemical & Natural Resources Engineering Project paper (Bachelor of Chemical Engineering) -- Universiti Malaysia Pahang – 2014 Bibliography : p. 57-69 The concept of mixed matrix membrane (MMM) chromatography is an alternative that provides a simple method for the preparation of adsorptive membranes, yet results in high quality membrane chromatography performance. MMMs are prepared by incorporating an ion exchange resin (or any adsorptive resin) into a membrane polymer solution prior to membrane casting. In this study, MMM will be prepared by combining cation and anion simultaneously in EVAL based polymer solution. The membrane will be used for whey protein fractionation to recover both acidic and basic protein. Whey is the liquid byproduct of casein precipitation of milk in the cheese or casein manufacturing industries and of milk concentration prior to milk powder production (Saufi, 2010). Rather than using the high cost ion exchange resin that purposely design for protein fractionation, this study will using a low cost ion exchanger resin that commonly used at the industry. The 7.5 wt% anion resin (MP500) will be bland with 7.5 wt% cation resin (CNP105) in the 15wt% EVAL based polymer solution. This mixed mode interaction MMM will applied for whey protein fractionation. The feasibility of MMM was tested in whey protein fractionation processes. WPI solutions were diluted to 2mg/mL with different pH binding buffer solution (pH 4, 5, 6, 7, and 8). The whey protein compositions after binding were assayed using UPLC column ACQUITY UPLC PrST using a C4 Jupiter column. A combination of pH and salt elution using different pH elution buffers will be performed to selectively elute the bound protein on the membrane. This membrane had a maximum static binding capacity of 0.260 mg/mL β-Lac, 0.214 mg/mL BSA, and 0.118 mg/mL α-Lac per membrane at pH 5. The membrane was successfully applied to bind acidic and basic proteins simultaneously from a mixture. Based on batch elution experimental results, a productivity of 0.156 mg whey protein mL-1 membrane h-1 was calculated using this customized mixed mode MMM Chromatography Chromatography Analysis http://ecollib.ump.edu.my/9684/ Access in library only 0 0 0 6 10000 10000 2019-09-04 0 TP156.C5 A36 2014 r Bc. 0000092099 2019-09-04 00:00:00 1 2019-09-04 PSM 0 0 0 1 10000 10000 2019-09-04 0 CD 8654 | TP156.C5 A36 2014 r Bc. 0000092100 2019-09-04 00:00:00 1 2019-09-04 PSM VIRTUA40 5782 5788 VTLSSORT0080*0200*0400*0900*1000*2450*2600*3000*5000*5020*5040*5200*6500*6501*8560*9992