Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation

The conventional method to purify protein is by using packed bed column chromatography. However, this method had several limitations such as high pressure drop and limited flow rate operation. Membrane chromatography can be used to overcome the limitation of packed column but the preparation of adso...

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Main Author: Shiew, Chan Fong
Format: Undergraduates Project Papers
Language:English
Published: 2013
Subjects:
Online Access:http://umpir.ump.edu.my/id/eprint/7212/
http://umpir.ump.edu.my/id/eprint/7212/
http://umpir.ump.edu.my/id/eprint/7212/1/Development_of_multiple_interactions_mixed_matrix_membrane.pdf
id ump-7212
recordtype eprints
spelling ump-72122015-03-03T09:34:47Z http://umpir.ump.edu.my/id/eprint/7212/ Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation Shiew, Chan Fong QD Chemistry The conventional method to purify protein is by using packed bed column chromatography. However, this method had several limitations such as high pressure drop and limited flow rate operation. Membrane chromatography can be used to overcome the limitation of packed column but the preparation of adsorptive membrane requires harsh chemical modifications. Mixed matrix membrane (MMM) preparation concept can be used as an alternative route to prepare membrane chromatography by physical blending of adsorptive resin with membrane polymer solution. In the current research, multiple interactions MMM chromatography was developed for whey protein fractionation using 7.5 wt% CNP105 cation resin and 42.5 wt% MP500 anion resin relative to base polymer content. The resins were blend at different composition in EVAL and cellulose base polymer matrix. Based on HPLC and SDS-PAGE analysis, both acidic and basic whey proteins were bound to the multiple interactions MMM in single run of whey batch fractionation. The binding capacity for major acidic whey proteins using EVAL based MMM are 4.255 mg BSA bound/ g MMM, 60.887 mg α-Lac bound/ g MMM and 231.788 mg β-Lac/ g MMM. For CA based MMM, the binding capacity are 2.970 mg BSA bound/ g MMM, 42.392 mg α-Lac bound/ g MMM and 179.817 mg β-Lac/ g MMM. 2013 Undergraduates Project Papers NonPeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/7212/1/Development_of_multiple_interactions_mixed_matrix_membrane.pdf Shiew, Chan Fong (2013) Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation. Faculty of Chemical & Natural Resources Engineering, Universiti Malaysia Pahang. http://iportal.ump.edu.my/lib/item?id=chamo:76092&theme=UMP2
repository_type Digital Repository
institution_category Local University
institution Universiti Malaysia Pahang
building UMP Institutional Repository
collection Online Access
language English
topic QD Chemistry
spellingShingle QD Chemistry
Shiew, Chan Fong
Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation
description The conventional method to purify protein is by using packed bed column chromatography. However, this method had several limitations such as high pressure drop and limited flow rate operation. Membrane chromatography can be used to overcome the limitation of packed column but the preparation of adsorptive membrane requires harsh chemical modifications. Mixed matrix membrane (MMM) preparation concept can be used as an alternative route to prepare membrane chromatography by physical blending of adsorptive resin with membrane polymer solution. In the current research, multiple interactions MMM chromatography was developed for whey protein fractionation using 7.5 wt% CNP105 cation resin and 42.5 wt% MP500 anion resin relative to base polymer content. The resins were blend at different composition in EVAL and cellulose base polymer matrix. Based on HPLC and SDS-PAGE analysis, both acidic and basic whey proteins were bound to the multiple interactions MMM in single run of whey batch fractionation. The binding capacity for major acidic whey proteins using EVAL based MMM are 4.255 mg BSA bound/ g MMM, 60.887 mg α-Lac bound/ g MMM and 231.788 mg β-Lac/ g MMM. For CA based MMM, the binding capacity are 2.970 mg BSA bound/ g MMM, 42.392 mg α-Lac bound/ g MMM and 179.817 mg β-Lac/ g MMM.
format Undergraduates Project Papers
author Shiew, Chan Fong
author_facet Shiew, Chan Fong
author_sort Shiew, Chan Fong
title Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation
title_short Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation
title_full Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation
title_fullStr Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation
title_full_unstemmed Development of multiple interactions mixed matrix membrane chromatography using lewatit MP500 anion resin and lewatit CNP 105 cation resin for whey protein fractionation
title_sort development of multiple interactions mixed matrix membrane chromatography using lewatit mp500 anion resin and lewatit cnp 105 cation resin for whey protein fractionation
publishDate 2013
url http://umpir.ump.edu.my/id/eprint/7212/
http://umpir.ump.edu.my/id/eprint/7212/
http://umpir.ump.edu.my/id/eprint/7212/1/Development_of_multiple_interactions_mixed_matrix_membrane.pdf
first_indexed 2023-09-18T22:03:43Z
last_indexed 2023-09-18T22:03:43Z
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