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Protein Separation Coacervation with Carboxymethyl Cellulose of Different Substitution Degree: Noninteracting Behavior of Bowman-Birk Chymotrypsin Inhibitor
Protein Separation Coacervation with Carboxymethyl Cellulose of Different Substitution Degree: Noninteracting Behavior of Bowman-Birk Chymotrypsin Inhibitor
- Source :
- Journal of agricultural and food chemistry. 66(17)
- Publication Year :
- 2018
-
Abstract
- We first observed that protein/polysaccharide interaction exhibited noninteracting behavior which makes Bowman–Birk chymotrypsin inhibitor (BBI) always free of complexation, being separated from another protein with similar isoelectric points, Kunitz trypsin inhibitor (KTI). Turbidity titrations showed that the electrostatic attractions were much stronger between KTI/BBI (KBi) and carboxymethyl cellulose of higher substitution degree. Unchanged chymotrypsin inhibitory activity (CIA) indicated that BBI had negligible contribution to protein recovery and trypsin inhibitory activity (TIA). Tricine–SDS–PAGE revealed that, at r = 20:1–2:1, unbound BBI was left in the supernatant when bound KTI transferred into precipitates, even if there was excess negative charge. Thus, purified KTI or BBI was achieved easily at the given conditions. The noninteracting behavior of BBI was further confirmed by ITC, where the binding enthalpy of BBI to CMC was negligible compared with the high binding affinity (Kb) of KTI. This...
- Subjects :
- Stereochemistry
Trypsin inhibitor
Static Electricity
02 engineering and technology
010402 general chemistry
01 natural sciences
Polysaccharides
Protein purification
medicine
Chymotrypsin
Enzyme Inhibitors
Plant Proteins
Trypsin Inhibitor, Bowman-Birk Soybean
biology
Kunitz STI protease inhibitor
Chemistry
Isothermal titration calorimetry
General Chemistry
021001 nanoscience & nanotechnology
Trypsin
0104 chemical sciences
Carboxymethyl cellulose
Isoelectric point
Carboxymethylcellulose Sodium
biology.protein
Soybean Proteins
Thermodynamics
Trypsin Inhibitor, Kunitz Soybean
0210 nano-technology
General Agricultural and Biological Sciences
Trypsin Inhibitors
medicine.drug
Subjects
Details
- ISSN :
- 15205118
- Volume :
- 66
- Issue :
- 17
- Database :
- OpenAIRE
- Journal :
- Journal of agricultural and food chemistry
- Accession number :
- edsair.doi.dedup.....893cf3c6fc38ff6ea20bec1cb6a6b390