protein dispersion
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2021 ◽  
pp. 110357
Author(s):  
Akihiro Nakamura ◽  
Hitomi Ohboshi ◽  
Madoka Sakai ◽  
Kei Nomura ◽  
Setsuko Nishiyama ◽  
...  


2021 ◽  
Author(s):  
L. Jiménez-Munoz ◽  
A. Brodkorb ◽  
L. G. Gómez-Mascaraque ◽  
M. Corredig

In the present study, the structuring and breakdown of a 5% protein dispersion prepared with commercial fractions of pea and rice isolates (PPI and RPI, respectively) were monitored by in vitro digestion.



PLoS ONE ◽  
2020 ◽  
Vol 15 (12) ◽  
pp. e0243273
Author(s):  
Rod S. Hobbs ◽  
Jennifer R. Hall ◽  
Laurie A. Graham ◽  
Peter L. Davies ◽  
Garth L. Fletcher

Antifreeze proteins inhibit ice growth and are crucial for the survival of supercooled fish living in icy seawater. Of the four antifreeze protein types found in fishes, the globular type III from eelpouts is the one restricted to a single infraorder (Zoarcales), which is the only clade know to have antifreeze protein-producing species at both poles. Our analysis of over 60 unique antifreeze protein gene sequences from several Zoarcales species indicates this gene family arose around 18 Ma ago, in the Northern Hemisphere, supporting recent data suggesting that the Arctic Seas were ice-laden earlier than originally thought. The Antarctic was subject to widespread glaciation over 30 Ma and the Notothenioid fishes that produce an unrelated antifreeze glycoprotein extensively exploited the adjoining seas. We show that species from one Zoarcales family only encroached on this niche in the last few Ma, entering an environment already dominated by ice-resistant fishes, long after the onset of glaciation. As eelpouts are one of the dominant benthic fish groups of the deep ocean, they likely migrated from the north to Antarctica via the cold depths, losing all but the fully active isoform gene along the way. In contrast, northern species have retained both the fully active (QAE) and partially active (SP) isoforms for at least 15 Ma, which suggests that the combination of isoforms is functionally advantageous.



Author(s):  
M Mahendradatta ◽  
YL Imran ◽  
Zainal ◽  
AB Tawali ◽  
M Asfar


Pharmaceutics ◽  
2018 ◽  
Vol 10 (3) ◽  
pp. 94 ◽  
Author(s):  
Simone Aleandri ◽  
Andrea Vaccaro ◽  
Ricardo Armenta ◽  
Andreas Völker ◽  
Martin Kuentz

Background: Dynamic light scattering (DLS) is an important tool to characterize colloidal systems and adequate sizing is particularly critical in the field of protein formulations. Among the different factors that can influence the measurement result, the effect of laser power has so far not been studied thoroughly. Methods: The sensitivity of a DLS instrument was first considered on a theoretical level, followed by experiments using DLS instruments, equipped with two different lasers of (nominal) 45 mW, and 100 mW, respectively. This work analyzes dilute colloidal dispersions of lysozyme as model protein. Results: Theoretical findings agreed with experiments in that only enhanced laser power of 100 mW laser allowed measuring a 0.1 mg/mL protein dispersion in a reliable manner. Results confirmed the usefulness of the presented theoretical considerations in improving a general understanding of the limiting factors in DLS. Conclusions: Laser power is a critical aspect regarding adequate colloidal analysis by DLS. Practical guidance is provided to help scientists specifically with measuring dilute samples to choose both an optimal instrument configuration as well as a robust experimental procedure.



2018 ◽  
Vol 543 (1-2) ◽  
pp. 257-268 ◽  
Author(s):  
J. Gross-Rother ◽  
N. Herrmann ◽  
M. Blech ◽  
S.R. Pinnapireddy ◽  
P. Garidel ◽  
...  
Keyword(s):  


Author(s):  
Chonghao Bi ◽  
◽  
Fei Gao ◽  
Yingdan Zhu ◽  
Fang Ji ◽  
...  


2014 ◽  
Vol 34 ◽  
pp. 39-45 ◽  
Author(s):  
Tatsunori Nobuhara ◽  
Kentaro Matsumiya ◽  
Yuko Nambu ◽  
Akihiro Nakamura ◽  
Nanae Fujii ◽  
...  


2011 ◽  
Vol 18 (06) ◽  
pp. 267-279 ◽  
Author(s):  
PRABIR PAL ◽  
TAPANENDU KAMILYA ◽  
MRITYUNJOY MAHATO ◽  
G. B. TALAPATRA

The interfacial surface activity of a protein, ovalbumin (OVA) at bare air/water interface in presence and also in absence of electrolyte (KCl) in subphase has been investigated. The surface activity was measured as a function of time. It has been found that, the presence of KCl in aqueous subphase enhances the adsorption rate of the protein. The changes of area/molecule, compressibility, rigidity and unfolding of OVA are trivial up to 10 mM KCl concentration. These properties of OVA, above 10 mM KCl concentration are significant and have been explained in the perspective of DLVO theory and many-body ion–protein dispersion potentials. The presence of high concentration of electrolyte increases the β-structure of OVA, resulting into larger unfolding as well as larger intermolecular aggregates. The overall study indicates that KCl perturbs the OVA monolayer.



2007 ◽  
Vol 18 (1) ◽  
pp. 223-230 ◽  
Author(s):  
Livia A. Moreira ◽  
Mathias Boström ◽  
Barry W. Ninham ◽  
Evaristo C. Biscaia ◽  
Frederico W. Tavares


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