Polyelectrolytes-protein complexes: a viable platform in the downstream processes of industrial enzymes at scaling up level
Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and cha...
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Published in | Journal of chemical technology and biotechnology (1986) Vol. 91; no. 12; pp. 2921 - 2928 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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Chichester, UK
John Wiley & Sons, Ltd
01.12.2016
Wiley Subscription Services, Inc |
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Abstract | Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non‐soluble complex, separated and then re‐dissolved, thus the method works, at the same time, like concentrative and pre‐purification steps together. © 2016 Society of Chemical Industry |
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AbstractList | Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non-soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non-soluble complex, separated and then re-dissolved, thus the method works, at the same time, like concentrative and pre-purification steps together. Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non-soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non-soluble complex, separated and then re-dissolved, thus the method works, at the same time, like concentrative and pre-purification steps together. © 2016 Society of Chemical Industry Abstract Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non‐soluble complex, separated and then re‐dissolved, thus the method works, at the same time, like concentrative and pre‐purification steps together. © 2016 Society of Chemical Industry |
Author | Brassesco, M Emilia Woitovich Valetti, Nadia Picó, Guillermo Alfredo |
Author_xml | – sequence: 1 givenname: Nadia surname: Woitovich Valetti fullname: Woitovich Valetti, Nadia organization: Institute of Biotechnological and Chemical Processes (IPROBYQ - CONICET) and Technology Department, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002RLK, Rosario, Argentina – sequence: 2 givenname: M Emilia surname: Brassesco fullname: Brassesco, M Emilia organization: Institute of Biotechnological and Chemical Processes (IPROBYQ - CONICET) and Technology Department, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002RLK, Rosario, Argentina – sequence: 3 givenname: Guillermo Alfredo surname: Picó fullname: Picó, Guillermo Alfredo email: gpico@fbioyf.unr.edu.ar, pico@iprobyq-conicet.gov.ar, gpico@fbioyf.unr.edu.ar organization: Institute of Biotechnological and Chemical Processes (IPROBYQ - CONICET) and Technology Department, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002RLK, Rosario, Argentina |
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Snippet | Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase... Abstract Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase... Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non-soluble complexes, leading to phase... |
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SubjectTerms | bioseparation Chromium downstream processes downstream processes, bioseparation Electrostatics enzyme purification Enzymes Phase separation Polyelectrolytes Precipitation (chemistry) Proteins Scaling up |
Title | Polyelectrolytes-protein complexes: a viable platform in the downstream processes of industrial enzymes at scaling up level |
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