Results 231 to 240 of about 5,709,630 (288)
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Journal of Agricultural and Food Chemistry, 2019
Protein hydrolysates, as surfactants, can scavenge radicals, but their poor distributions at the oil-water interface limit their storage stability. Therefore, we studied covalent interaction between rice protein hydrolysates and chlorogenic acid under ...
Xin Pan +10 more
semanticscholar +1 more source
Protein hydrolysates, as surfactants, can scavenge radicals, but their poor distributions at the oil-water interface limit their storage stability. Therefore, we studied covalent interaction between rice protein hydrolysates and chlorogenic acid under ...
Xin Pan +10 more
semanticscholar +1 more source
Food Hydrocolloids, 2019
The effect of porcine bone protein hydrolysates (PBPH)-rutin conjugates on the physical and oxidative stability of PBPH-coated emulsions was investigated.
Haotian Liu +4 more
semanticscholar +1 more source
The effect of porcine bone protein hydrolysates (PBPH)-rutin conjugates on the physical and oxidative stability of PBPH-coated emulsions was investigated.
Haotian Liu +4 more
semanticscholar +1 more source
Functional Fish Protein Hydrolysates
2020Underutilized fish species such as male and spent capelin (Mallotus villosus) were used to prepare functional protein hydrolysates by various enzymatic treatments. Three commercial proteases namely Alcalase, Neutrase and Papain were employed for the preparation of fish protein hydrolysates.
Fereidoon Shahidi +2 more
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Non-bitter Protein Hydrolysates
Canadian Institute of Food Science and Technology Journal, 1981Abstract Deboned, defatted chicken meat (78% protein, d.b.) was reacted with pancreatin to produce a bitter hydrolysate as judged by a trained sensory panel. The hydrolysis was carried out at 60°C, an enzyme concentration of 4.3%, pH of 8.55 (carbonate buffer) and a salt concentration of 0.6 M (KC1).
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Nucleotide Exchange on RAS Proteins Using Hydrolysable and Non-hydrolysable Nucleotides
Biochemical and biophysical assays using recombinant RAS require the protein to be in either the active or inactive state. Here we describe methods to exchange the nucleotide present in the purified RAS protein with either GDPβS, GppNHp, or GTP depending on the assay requirement.Timothy, Waybright, Andrew G, Stephen
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