scholarly journals Improvement of Functional Properties of Fish Water Soluble Proteins with Glucose-6-phosphate through the Maillard Reaction

1999 ◽  
Vol 65 (4) ◽  
pp. 618-622 ◽  
Author(s):  
Mita Wahyuni ◽  
Shoichiro Ishizaki ◽  
Munehiko Tanaka
Keyword(s):  
Functional Properties ◽  
Maillard Reaction ◽  
Soluble Proteins ◽  
Water Soluble

Preparation and important functional properties of water-soluble chitosan produced through Maillard reaction

2005 ◽  
Vol 96 (13) ◽  
pp. 1473-1482 ◽  
Author(s):  
Ying-Chien Chung ◽  
Cheng-Lang Kuo ◽  
Chiing-Chang Chen
Keyword(s):  
Functional Properties ◽  
Maillard Reaction ◽  
Water Soluble

scholarly journals Characteristics, Functional Properties, and Antioxidant Activities of Water-Soluble Proteins Extracted from Grasshoppers, Patanga succincta and Chondracris roseapbrunner

2018 ◽  
Vol 2018 ◽  
pp. 1-11 ◽  
Author(s):  
Niphattha Chatsuwan ◽  
Sitthipong Nalinanon ◽  
Yuporn Puechkamut ◽  
Buddhi P. Lamsal ◽  
Praphan Pinsirodom
Keyword(s):  
Functional Properties ◽  
Structural Integrity ◽  
Antioxidant Activities ◽  
Sulfhydryl Group ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Major Protein ◽  
Electrophoretic Study ◽  
Antioxidant Power ◽  
Significant Difference

Water-soluble proteins extracted from two species of grasshoppers, Patanga succincta (WSPP) and Chondracris roseapbrunner (WSPC), were characterized as well as their functional properties and antioxidant activities were investigated. The extraction yield, on a wet weight basis, was 7.35% and 7.46% for WSPP and WSPC, respectively. The most abundant amino acid in both proteins was glutamic acid, followed by aspartic, alanine, and leucine, in that order. The electrophoretic study revealed that proteins with MW of 29, 42, 50, 69, and 146 kDa were the major protein components in WSPP and WSPC. FTIR analysis showed that those proteins remained their structural integrity. The surface hydrophobicity at pH 7 of WSPC was higher than WSPP, but the sulfhydryl group content did not show significant difference between the proteins from two species. Both grasshopper proteins were mostly soluble in strong acidic and alkaline aqueous solutions with a minimum value at pH 4. Those proteins exhibited poor emulsifying properties and foaming capacity, but they had greater foaming stability compared with bovine serum albumin (BSA) (p<0.05). WSPC showed greater DPPH• and ABTS•+ scavenging activities and ferric-reducing antioxidant power (FRAP) than did WSPP (p<0.05). Therefore, based on characteristics and functional properties, water-soluble proteins from both edible grasshoppers can be used as an ingredient in food applications.

scholarly journals Ultrasound-assisted Maillard reaction of ovalbumin/xylose: The enhancement of functional properties and its mechanism

2021 ◽  
Vol 73 ◽  
pp. 105477
Author(s):  
Xuanting Liu ◽  
Qi Yang ◽  
Meng Yang ◽  
Zhiyang Du ◽  
Chen Wei ◽  
...  
Keyword(s):  
Functional Properties ◽  
Maillard Reaction ◽  
Ultrasound Assisted

The cellular basis of corneal transparency: evidence for ‘corneal crystallins’

1999 ◽  
Vol 112 (5) ◽  
pp. 613-622 ◽  
Author(s):  
J.V. Jester ◽  
T. Moller-Pedersen ◽  
J. Huang ◽  
C.M. Sax ◽  
W.T. Kays ◽  
...  
Keyword(s):  
Cellular Level ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Corneal Tissue ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Transparency ◽  
Scattering Measurements ◽  
Class 1

In vivo corneal light scattering measurements using a novel confocal microscope demonstrated greatly increased backscatter from corneal stromal fibrocytes (keratocytes) in opaque compared to transparent corneal tissue in both humans and rabbits. Additionally, two water-soluble proteins, transketolase (TKT) and aldehyde dehydrogenase class 1 (ALDH1), isolated from rabbit keratocytes showed unexpectedly abundant expression (approximately 30% of the soluble protein) in transparent corneas and markedly reduced levels in opaque scleral fibroblasts or keratocytes from hazy, freeze injured regions of the cornea. Together these data suggest that the relatively high expressions of TKT and ALDH1 contribute to corneal transparency in the rabbit at the cellular level, reminiscent of enzyme-crystallins in the lens. We also note that ALDH1 accumulates in the rabbit corneal epithelial cells, rather than ALDH3 as seen in other mammals, consistent with the taxon-specificity observed among lens enzyme-crystallins. Our results suggest that corneal cells, like lens cells, may preferentially express water-soluble proteins, often enzymes, for controlling their optical properties.

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