Rheological Properties of Fast Skeletal Myosin Rod and Light Meromyosin from Walleye Pollack and White Croaker:  Contribution of Myosin Fragments to Thermal Gel Formation

2005 ◽  
Vol 53 (23) ◽  
pp. 9193-9198 ◽  
Author(s):  
Hideto Fukushima ◽  
Yoshie Satoh ◽  
Sung Ho Yoon ◽  
Marie Togashi ◽  
Misako Nakaya ◽  
...  
2006 ◽  
Vol 72 (3) ◽  
pp. 646-655 ◽  
Author(s):  
Yoshie SATOH ◽  
Misako NAKAYA ◽  
Yoshihiro OCHIAI ◽  
Shugo WATABE

2002 ◽  
Vol 68 (sup2) ◽  
pp. 1545-1548
Author(s):  
HIDETO FUKUSHIMA ◽  
YOSHIE SATOH ◽  
MISAKO NAKAYA ◽  
SHOICHIRO ISHIZAKI ◽  
SHUGO WATABE

2017 ◽  
Vol 232 ◽  
pp. 369-378 ◽  
Author(s):  
Camila Sampaio Mangolim ◽  
Thamara Thaiane da Silva ◽  
Vanderson Carvalho Fenelon ◽  
Adriane do Nascimento ◽  
Francielle Sato ◽  
...  

1994 ◽  
Vol 61 (2) ◽  
pp. 221-232 ◽  
Author(s):  
Mary McSwiney ◽  
Harjinder Singh ◽  
Osvaldo Campanella ◽  
Lawrence K. Creamer

SummaryHeat-induced gelation, an important functional property of β-lactoglobulin, was studied by measuring the rheological properties of both the A and B variants of the protein during and after heat treatment within a range of pH, temperature and concentration. Gel electrophoresis was used to determine the extent of denaturation and disulphide bond crosslinking of some samples. Both variants formed gel networks on heating at temperatures > 75 °C, and under most conditions the storage modulus (G′) of βlactoglobulin A gels was higher than the G′ of β-lactoglobulin B gels, in particular after cooling to 25 °C. A minimum protein concentration of 50 g/1 was required for gel formation at pH 7·0 in 0·1 M-NaCl by both variants at 80 °C. Increasing the protein concentration above 50 g/1 increased G′, the extent of increase being much greater for the A variant than the B variant. G′ of variant A gels was not much influenced by pH whereas G′ of variant B gels decreased slightly from pH 3 to pH 6 and increased between pH 6 and pH 9. When mixtures of the two variants were gelled G′ increased at the temperature of heating (80 °C) and after cooling (25 °C) as the relative quantity of variant A was increased. Comparisons of the loss of discrete protein bands from electrophoretic gels (native-PAGE, SDS-PAGE and SDS-PAGE of reduced samples) showed that heating β-lactoglobulin solutions of 100 g/1 at pH 7 in 0·1 M-NaCl and at 75, 80 and 85 °C caused a faster loss of both native and SDS-soluble β-lactoglobulin A than of β-lactoglobulin B. It was concluded that the loss of native β-lactoglobulin structure from these solutions during heating was faster than the formation of disulphidelinked aggregates, which was faster than gel formation for both β-lactoglobulin A and β-lactoglobulin B, and that each of these reactions was faster for β-lactoglobulin A than for β-lactoglobulin B. This contrasts with conclusions drawn from some previous studies and may arise from the differences in protein concentration between the present study (∼ 100 g/1) and the previous ones (< ∼ 10 g/1).


2013 ◽  
Vol 79 (4) ◽  
pp. 715-724 ◽  
Author(s):  
Yoko Matsuoka ◽  
Jianrong Wan ◽  
Hideki Ushio ◽  
Shugo Watabe

Soft Matter ◽  
2015 ◽  
Vol 11 (4) ◽  
pp. 741-748 ◽  
Author(s):  
Ming-Ming Su ◽  
Hai-Kuan Yang ◽  
Li-Jun Ren ◽  
Ping Zheng ◽  
Wei Wang

We report that the gel formation, supramolecular structures and performance of organogels in the cholesterol–POM–cholesterol hybrid gelator within the toluene/DMF mixed solvents can be solvent-mediated.


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