scholarly journals Characterisation of Lactoferrin Isolated from Acid Whey Using Pilot-Scale Monolithic Ion-Exchange Chromatography

Processes ◽  
2020 ◽  
Vol 8 (7) ◽  
pp. 804
Author(s):  
Bojana Bogovič Matijašić ◽  
Jernej Oberčkal ◽  
Petra Mohar Lorbeg ◽  
Diana Paveljšek ◽  
Nina Skale ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Ion Exchange ◽  
Binding Capacity ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Iron Binding ◽  
E Coli ◽  
Freeze Dried ◽  
Acid Whey ◽  
Iron Binding Capacity

The aim of this study was to characterize the properties of lactoferrin (LF) obtained in a process developed for its isolation from acid whey derived from the production of fresh curd cheese, using a unique technology of ion-exchange chromatography on CIM® monolithic columns. The freeze-dried lactoferrin samples produced on the pilot plant (capacity 1 m3) were examined for the purity, iron-binding capacity, antibacterial activity, and pH- and temperature-stability. Apo-LF inhibited several tested strains (enterobacteria, Staphylococcus, Streptococcus salivarius) except clostridia, lactic acid bacteria, and bifidobacteria. Sample of LF intentionally saturated with Fe3+ lost its antibacterial activity, indicating the involvement of mechanisms based on depriving bacteria of an iron source. All samples, regardless of the iron-saturation level, exhibited stability in pH range 4.0 to 11.0. LF with higher iron content (A-value = 41.9%) showed better thermal stability. Heat treatment up to 72 °C/3 s did not reduce antimicrobial activity against E. coli O157: H7 tox-. Higher purity (above 91%), higher iron-binding capacity and higher inhibitory activity against E. coli O157: H7 tox- compared to some similar products from the market was observed. These results demonstrate a high potential of monolithic ion-exchange chromatography for industrial processing of acid whey as a source of LF that can be used in new products with high-added value. The upscaling of the process is ongoing on a demonstration plant (10–30 m3/day capacity).

scholarly journals Ion exchange chromatography of monoclonal antibodies: Effect of resin ligand density on dynamic binding capacity

2009 ◽  
Vol 1216 (20) ◽  
pp. 4366-4371 ◽  
Author(s):  
Ann Marie Hardin ◽  
Chithkala Harinarayan ◽  
Gunnar Malmquist ◽  
Andreas Axén ◽  
Robert van Reis
Keyword(s):  
Monoclonal Antibodies ◽  
Ion Exchange ◽  
Binding Capacity ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Dynamic Binding ◽  
Ligand Density ◽  
Dynamic Binding Capacity

Bilirubin binding capacity of albumin isolated from cord-blood serum is less than that from serum of adults.

1980 ◽  
Vol 26 (6) ◽  
pp. 738-740 ◽  
Author(s):  
A Alayoff ◽  
J Kapitulnik ◽  
A Konijn ◽  
N A Kaufmann ◽  
S H Blondheim
Keyword(s):  
Ion Exchange ◽  
Blood Serum ◽  
Cord Blood ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cord Blood Serum ◽  
Bilirubin Binding

Abstract As estimated by Sephadex gel filtration, the bilirubin binding capacity of albumin isolated from cord-blood serum by ion-exchange chromatography is less than that of albumin isolated from serum of adults. Albumin isolated from cord-blood serum showed increased bilirubin binding as compared with the albumin in the native serum. These findings suggest that the lower bilirubin binding capacity of serum from newborns as compared with serum from adults is a result of both an intrinsic deficiency in binding capacity of neonatal albumin and the presence of substances in neonatal serum that interfere with bilirubin binding.

Bilirubin binding capacity of albumin isolated from cord-blood serum is less than that from serum of adults.

1980 ◽  
Vol 26 (6) ◽  
pp. 738-740
Author(s):  
A Alayoff ◽  
J Kapitulnik ◽  
A Konijn ◽  
N A Kaufmann ◽  
S H Blondheim
Keyword(s):  
Ion Exchange ◽  
Blood Serum ◽  
Cord Blood ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cord Blood Serum ◽  
Bilirubin Binding

Abstract As estimated by Sephadex gel filtration, the bilirubin binding capacity of albumin isolated from cord-blood serum by ion-exchange chromatography is less than that of albumin isolated from serum of adults. Albumin isolated from cord-blood serum showed increased bilirubin binding as compared with the albumin in the native serum. These findings suggest that the lower bilirubin binding capacity of serum from newborns as compared with serum from adults is a result of both an intrinsic deficiency in binding capacity of neonatal albumin and the presence of substances in neonatal serum that interfere with bilirubin binding.

Isolation of human interferon β1b (Ser17) expressed in E. coli with the use of ion-exchange chromatography

2011 ◽  
Vol 37 (3) ◽  
pp. 292-297 ◽  
Author(s):  
V. P. Romanov ◽  
V. V. Bezuglov ◽  
M. Yu. Bobrov ◽  
T. I. Kostromina ◽  
S. A. Feofanov ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Interferon ◽  
E Coli

Effect of Pulsed Electric Fields on the Antibacterial Activity of Ovotransferrin and Mechanism of Action

2013 ◽  
Vol 734-737 ◽  
pp. 2260-2268
Author(s):  
Tie Hua Zhang ◽  
Di Ru Liu ◽  
Yuan Yuan ◽  
Jian Zheng ◽  
Hai Qing Ye ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Electric Fields ◽  
Field Intensity ◽  
Fluorescence Spectra ◽  
Binding Capacity ◽  
Pulse Number ◽  
Iron Binding ◽  
Electrical Field ◽  
Electrical Field Intensity ◽  
Iron Binding Capacity

Ovotransferrin (OVT) is an iron-binding glycoprotein, found in egg white and serum. It appears to be a multi-functional protein with a major role in avian natural immunity and antimicrobial activity. In this study, the effects of high-intensity pulsed electric fields (HIPEF) on antibacterial activity of OVT particularly forEscherichia coliand the changes in its iron-binding capacity were investigated. Fluorescence spectra technology was used to analyze possible structural changes of OVT, explaining and exploring the effects of the HIPEF technology on the mechanisms that determine the protein activity. The results showed that when the electrical field intensity was 40 kV.cm-1, the antibacterial activity of OVT solution was the highest 87.9% as compared to the control (6.052×107CFU.mL-1) and iron-binding capacity reached the maximum 0.733, which was 2.4 times higher as compared to the control. When the pulse number reached at 80, the antibacterial activity of OVT solution increased up to 74.5% as compared to the control (6.052×107CFU.ml-1) and iron-binding capacity was 1.9 times higher than that of control. With the change of pH values from 7.0 to 8.0, the iron-binding capacity was slightly decreased, the difference was not significant among the groups (P>0.05). Fluorescence spectra analysis showed that the microenvironment of OVT changed with the increase of the pulsed electric field intensity and number and changes in the fluorescence intensity were measured constantly with fluroescensce quench phenomena occurring. The fluorescence intensity was reduced to minimum at 40 kV.cm-1or 80 pulse number. The results showed that the changes of the iron-binding capacity after HIPEF treatment were strongly linked with the changes of the antibacterial activity. An increase of the electrical field intensity and change in treatment time induced higher inhibition ofEscherichia coliwith OVT.

A NEUROPHYSIN FROM COD (GADUS MORRHUA) PITUITARY GLANDS: ISOLATION AND PROPERTIES

1968 ◽  
Vol 42 (1) ◽  
pp. 143-NP ◽  
Author(s):  
B. T. PICKERING
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Arginine Vasopressin ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Maximum Binding Capacity ◽  
Pituitary Glands

SUMMARY A protein capable of binding neurohypophysial hormones has been isolated from cod pituitary glands using gel filtration and ion-exchange chromatography. The cod protein which was acidic and rich in cystine had an amino acid composition closely related to those of the mammalian neurophysins. It had a maximum binding capacity of 2·2 μmole/14mg. for oxytocin, 2·1 μmole/14 mg. for [8-arginine]-oxytocin and 1·1 μmole/14 mg. for [8-arginine]-vasopressin. Thus the cod protein had a greater capacity for the endogenous pressor-antidiuretic peptide than for the analogous mammalian hormone.

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