scholarly journals Studies on Chitin

1955 ◽  
Vol 8 (4) ◽  
pp. 530 ◽  
Author(s):  
RH Hackman

The effects of pH, salt concentration, and temperature on the adsorption of a water-soluble insect cuticular protein to chitin have been investigated. The adsorption is dependent upon pH, decreasing rapidly as the pH increases from the region of the isoelectric point of the protein. Increase in salt concentration decreases adsorption but the adsorption appears to be little influenced by changes in temperature. Tyrosine-rich protein fractions are preferentially adsorbed. The adsorption is partly irreversible and an increase to pH 9 is necessary before all the adsorbed protein can be removed. It is concluded that there is only a weak bonding between the chitin and the water-soluble cuticular protein.

2016 ◽  
Vol 41 (4) ◽  
pp. e13073 ◽  
Author(s):  
Toan Thuc Pham ◽  
Thi Thu Tra Tran ◽  
Nu Minh Nguyet Ton ◽  
Van Viet Man Le

Fisheries ◽  
2020 ◽  
Vol 2020 (2) ◽  
pp. 113-117
Author(s):  
Olga Mezenova ◽  
Vladimir Wolkov ◽  
Larisa Baydalinova ◽  
Natalia Mezenova ◽  
Svetlana Agafonova ◽  
...  

The authors study three fractions obtained as a result of hydrolysis of smoked sprat heads (under temperature of 130oC and presser of 0.25 MPa) – fat, protein water-soluble, and protein-and-mineral ones. Waste from sprat production of two fish canning complexes of the Kaliningrad Region - “RosCon” and “Kolkhoz for the Motherland” - was used as raw material. Hydrolysis was carried out in an aqueous medium in two ways - with preliminary separation of fat and without this operation. The protein fraction was sublimated and its quantitative and qualitative indices were examined - mass yield, solubility, chemical composition and molecular fractional composition of the obtained peptide fractions were determined. The output of sublimated protein fractions is practically independent of the type of raw material and the method of pre-treatment and is 6.47.9% of the mass of raw materials. The chemical composition of protein fractions varies widely in terms of fat (1.4–8.3%), minerals (9.8–13.4%) and proteins (72.1–80.2%). The solubility of the peptide fractions ranged from 91-98%. The molecular weight assessment results showed a high content of a low molecular weight fraction of peptides with an MM of less than 10 kDa in all experimental samples (about 38%). This indicates a high digestibility and biological value of the obtained peptide compositions. Sublimated peptide compositions had typical organoleptic characteristics, pleasant aroma and taste of smoked fish. Ключевые


2018 ◽  
Vol 114 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Vinícius Martins de Oliveira ◽  
Vinícius de Godoi Contessoto ◽  
Fernando Bruno da Silva ◽  
Daniel Lucas Zago Caetano ◽  
Sidney Jurado de Carvalho ◽  
...  

2012 ◽  
Vol 507 ◽  
pp. 149-153 ◽  
Author(s):  
Jae Ik Choi ◽  
Esther Sluzky ◽  
Maria Anc ◽  
Alan Piquette ◽  
Mark E. Hannah ◽  
...  

Electrophoretic deposition (EPD) has been used for phosphor screening for a variety of emissive information displays and more recently, for solid state lighting. EPD is well suited to deposit the fine (nanometer to micrometer diameter) phosphor particles needed for high resolution displays. The fundamentals of the EPD process in an isopropanol (IPA) bath have been characterized by the dissociation behavior of nitrate salts in IPA, measurement of the effects of pH and nitrate salt concentration on the zeta potential of the particles, studying of the processing conditions and modeling of the deposition rates. The electrochemical precipitation reactions form an adhesive agent for the particles and the adhesion strength can be enhanced by various methods to meet the requirements of these technologies.


1986 ◽  
Vol 6 (7) ◽  
pp. 685-689 ◽  
Author(s):  
F. A. Hashim ◽  
E. Davies Jones ◽  
R. D. Howells ◽  
B. Rees Smith

The water soluble A subunit of the human TSH receptor has been shown to have an isoelectric point of 5. As both TSH and TSH receptor antibodies have isoelectric points in the region of 8–10, charge-charge interactions must be of major importance in the binding of hormone or antibody to the TSH receptor A subunit.


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