Results 31 to 40 of about 1,963,376 (294)
Research Progress on the Improvement and Evaluation of the Heat Stability of Whey Protein [PDF]
Shipin KexueWhey protein (WP), an important protein in dairy products, is rich in amino acids and bioactive peptides, and possesses high nutritional value. However, its poor thermal stability leads to issues such as protein denaturation, precipitation, and oxidation
DONG Xuan, PANG Xiaoyang, LU Ruqing, WANG Yunna, YU Jinghua, LÜ Jiaping, ZHANG Shuwen, LI Hongjuan
doaj +1 more source
Decoupling enzyme catalysis from thermal denaturation [PDF]
, 2010 The equilibrium model (EM) (Daniel et al., 2001) postulates two forms of a folded enzyme, one catalytically active (Eact) and the other inactive (Einact), which interconvert via a fast thermal equilibrium (Keq) (Figure A). This model for enzyme catalysis
Easter, Ashley Davys
core
FEBS Open Bio, EarlyView.TisIBP8, a fungal‐derived hyperactive ice‐binding protein, helps Caenorhabditis elegans survive dehydration. It localizes near cell membranes, reduces cell damage, and helps maintain membrane structure during drying. These results suggest that ice‐binding proteins can protect cells from dehydration stress as well as freezing stress.
Daiki Shimose +9 more
wiley +1 more source
Shipin gongye ke-jiProtein denaturation is the key point affecting quality attributes of the scallop adductors (SA) during thermal processing such as drying, sous-vide cooking and traditional cooking.
Qilong SHI, Jing LIU, Ya ZHAO
doaj +1 more source
Foods, 2021 Being widely abundant, grass proteins could be a novel source of plant proteins for human foods. In this study, ryegrass proteins extracted using two different approaches-chemical and enzymatic extraction, were characterised for their physico-chemical ...
Lovedeep Kaur +6 more
doaj +1 more source
, 2015 Thermal denaturation profile of WT (blue), P61S (green), P61SR100E (red), R100E (purple) hNGF (panel A), hproNGF (panel B) measured as a thermal shift assay by Differential Scanning Fluorimetry (DSF).
Francesca Malerba (161148) +9 more
core +1 more source
Optimizing photoexcitation conditions for time‐resolved X‐ray solution scattering experiments
FEBS Open Bio, EarlyView.Time‐resolved X‐ray solution scattering (TR‐XSS) is a powerful technique to visualize how proteins change their structure in real time after light activation. Selecting the right laser photoexcitation conditions—fluence, excitation geometry, and sample refresh rate—is critical to maximize the experimental signal while avoiding unwanted side effects ...
Matteo Levantino
wiley +1 more source
Honey-Induced Protein Stabilization as Studied by Fluorescein Isothiocyanate Fluorescence
The Scientific World Journal, 2013 Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe.
Yin How Wong +2 more
doaj +1 more source
Hydrogen exchange in thermally denatured ribonuclease [PDF]
Biochemistry, 1991 Hydrogen exchange has been used to test for the presence of nonrandom structure in thermally denatured ribonuclease A (RNase A). Quenched-flow methods and 2D 1H NMR spectroscopy were used to measure exchange rates for 36 backbone amide protons (NHs) at 65 degrees C and at pH* (uncorrected pH measured in D2O) values ranging from 1.5 to 3.8.
A D, Robertson, R L, Baldwin
openaire +2 more sources
Single-molecule chemical denaturation of riboswitches [PDF]
, 2013 To date, single-molecule RNA science has been developed almost exclusively around the effect of metal ions as folding promoters and stabilizers of the RNA structure.
St-Pierre, Patrick +14 more
core +1 more source