scholarly journals BODIPY-Based Fluorescent Probes for Sensing Protein Surface-Hydrophobicity

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Nethaniah Dorh ◽  
Shilei Zhu ◽  
Kamal B. Dhungana ◽  
Ranjit Pati ◽  
Fen-Tair Luo ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Surface Hydrophobicity ◽  
Protein Surface ◽  
Protein Surface Hydrophobicity

Coomassie Brilliant Blue-binding: a simple and effective method for the determination of water-insoluble protein surface hydrophobicity

2016 ◽  
Vol 8 (4) ◽  
pp. 790-795 ◽  
Author(s):  
Yungang Cao ◽  
Jing Zhao ◽  
Youling L. Xiong
Keyword(s):  
Surface Hydrophobicity ◽  
Fluorescence Method ◽  
Brilliant Blue ◽  
Insoluble Protein ◽  
Protein Surface ◽  
Coomassie Brilliant Blue ◽  
Protein Surface Hydrophobicity ◽  
Coomassie Brilliant

A novel Coomassie Brilliant Blue-binding method, which correlated well with the widely accepted ANS fluorescence method (R = 0.95), was developed to determine the surface hydrophobicity of water-insoluble proteins.

scholarly journals Physical Properties and Structural Changes of Myofibrillar Protein Gels Prepared with Basil Seed Gum at Different Salt Levels and Application to Sausages

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 702
Author(s):  
Chang Hoon Lee ◽  
Koo Bok Chin
Keyword(s):  
Physical Properties ◽  
Structural Changes ◽  
Surface Hydrophobicity ◽  
Myofibrillar Protein ◽  
Protein Surface ◽  
Salt Level ◽  
Low Salt ◽  
Protein Surface Hydrophobicity ◽  
Protein Gels ◽  
Seed Gum

The objective of this study was to evaluate physical properties and structural changes of myofibrillar protein gels with basil seed gum (BSG) at different salt levels and develop the low-salt sausages with BSG. Myofibrillar protein (MP) gels were prepared with or without BSG at different salt concentrations (0.15, 0.30, and 0.45 M). Cooking yield (CY, %), gel strength (GS, gf), viscosity, sulfhydryl contents, protein surface hydrophobicity, scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FTIR) of MP were measured. Pork sausages were manufactured with 1% BSG at both low-salt (1.0%) and regular-salt (1.5%) levels. pH, color, expressible moisture (EM, %), CY, textural profile analyses, FTIR, sulfhydryl group, and protein surface hydrophobicity (μg) were measured for analyzing the properties of sausages. The addition of 1% BSG to MP gels increased CY and shear stress. Among treatments with different salt concentrations, MP at 0.30 M salt level with 1% BSG had higher GS than that at 0.15 M salt level with BSG. In microstructure, swollen structures were shown in MP gels with BSG. Although CY of sausage at the low-salt concentration (1.0%) decreased, regardless of the BSG addition, hardness values of sausages with regular-salt level increased with the addition of 1% BSG was added. Protein surface hydrophobicity and sulfhydryl contents of sausages increased with the addition of 1% BSG, resulting in higher hardness and lower springiness than those without BSG. These results suggest that BSG could be used as a water-binding and gelling agent in processed meats.

scholarly journals Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain

1997 ◽  
Vol 72 (1) ◽  
pp. 18-23 ◽  
Author(s):  
M. Suzuki ◽  
J. Shigematsu ◽  
Y. Fukunishi ◽  
Y. Harada ◽  
T. Yanagida ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Surface Hydrophobicity ◽  
Motor Domain ◽  
Protein Surface ◽  
Myosin Motor ◽  
Myosin Motor Domain ◽  
Protein Surface Hydrophobicity
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