scholarly journals How Charge and Triple Size-Selective Membrane Separation of Peptides from Salmon Protein Hydrolysate Orientate their Biological Response on Glucose Uptake

2019 ◽  
Vol 20 (8) ◽  
pp. 1939 ◽  
Author(s):  
Loïc Henaux ◽  
Jacinthe Thibodeau ◽  
Geneviève Pilon ◽  
Tom Gill ◽  
André Marette ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Glucose Uptake ◽  
Membrane Separation ◽  
Protein Hydrolysate ◽  
Biological Response ◽  
Ultrafiltration Membranes ◽  
Selective Membrane ◽  
Insulin Control ◽  
By Products ◽  
Different Molecular Weight

The valorization of by-products from natural organic sources is an international priority to respond to environmental and economic challenges. In this context, electrodialysis with filtration membrane (EDFM), a green and ultra-selective process, was used to separate peptides from salmon frame protein hydrolysate. For the first time, the simultaneous separation of peptides by three ultrafiltration membranes of different molecular-weight exclusion limits (50, 20, and 5 kDa) stacked in an electrodialysis system, allowed for the generation of specific cationic and anionic fractions with different molecular weight profiles and bioactivity responses. Significant decreases in peptide recovery, yield, and molecular weight (MW) range were observed in the recovery compartments depending on whether peptides had to cross one, two, or three ultrafiltration membranes. Moreover, the Cationic Recovery Compartment 1 fraction demonstrated the highest increase (42%) in glucose uptake on L6 muscle cells. While, in the anionic configuration, both Anionic Recovery Compartment 2 and Anionic Recovery Compartment 3 fractions presented a glucose uptake response in basal condition similar to the insulin control. Furthermore, Cationic Recovery Compartment 3 was found to contain inhibitory peptides. Finally, LC-MS analyses of the bioassay-guided bioactive fractions allowed us to identify 11 peptides from salmon by-products that are potentially responsible for the glucose uptake improvement.

Effect of Composition of Calcium Lignosulfonate on Setting of Portland Cement with Anhydrite

2012 ◽  
Vol 557-559 ◽  
pp. 877-882
Author(s):  
Xiao Ping Wang ◽  
Yu Xia Pang ◽  
Dong Jie Yang ◽  
Hong Ming Lou ◽  
Xue Qing Qiu
Keyword(s):  
Molecular Weight ◽  
Portland Cement ◽  
Setting Time ◽  
Reducing Sugar ◽  
Ultrafiltration Membranes ◽  
Main Components ◽  
Effect Of The Composition ◽  
Different Molecular Weight

Calcium lignosulfonate (CL) was separated into three fractions with different molecular weight by using ultrafiltration membranes, and the effect of the composition of commercial CL on the setting time of Portland cement with anhydrite was studied in this paper. Results show that the CL fraction with the cut-off molecular weight of less than 150 (CL-A) shortens setting time most. Further analysis indicates that the content of reducing sugar in CL-A reaches to 15.3%, including mannose, glucose, galactose, xylose and arabinose, and these five kinds of monosaccharides are found to be the main components of inducing quick set of cement. Ultrafiltration is an effective method to remove most of the reducing sugar in CL and weaken the quick set of Portland cement with anhydrite.

Protein Hydrolysate from Brewer’s Spent Grain and its Inhibitory Ability of α-Glucosidase

2012 ◽  
Vol 581-582 ◽  
pp. 138-141 ◽  
Author(s):  
Hong Jia Lin ◽  
Lin Li ◽  
Ying Juan Tian ◽  
Xia Zhang ◽  
Bing Li
Keyword(s):  
Molecular Weight ◽  
Protein Hydrolysate ◽  
Weight Fraction ◽  
Hydrolysis Time ◽  
Brewer’S Spent Grain ◽  
Inhibitory Ability ◽  
Spent Grain ◽  
By Products

Brewer’s spent grain (BSG) rich in proteins is the main by-products in brewery. BSC proteins were extracted and hydrolyzed by Alcalase. The effects of hydrolysis time, temperature, pH and amount of enzyme added on the peptide yield were investigated. Inhibition of BSG protein hydrolysate against α-glucosidase was evaluated in vitro. BSG protein hydrolysate at 4.0 mg/mL showed the inhibition of 21.42% against α-glucosidase. The BSG protein hydrolysate after ultrafiltration purification exhibited much higher inhibition than that without ultrafiltration purification. The inhibition of BSC protein hydrolysate fraction with molecular weight fraction less than 5 kDa was 56.41%.

scholarly journals Nano-Assemblies from Amphiphilic PnBA-b-POEGA Copolymers as Drug Nanocarriers

Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1164
Author(s):  
Angeliki Chroni ◽  
Thomas Mavromoustakos ◽  
Stergios Pispas
Keyword(s):  
Molecular Weight ◽  
Chain Transfer ◽  
Raft Polymerization ◽  
Polymeric Nanocarriers ◽  
Reversible Addition ◽  
2D Noesy ◽  
Drug Nanocarriers ◽  
Glycol Methyl Ether ◽  
Different Molecular Weight

The focus of this study is the development of highly stable losartan potassium (LSR) polymeric nanocarriers. Two novel amphiphilic poly(n-butyl acrylate)-block-poly(oligo(ethylene glycol) methyl ether acrylate) (PnBA-b-POEGA) copolymers with different molecular weight (Mw) of PnBA are synthesized via reversible addition fragmentation chain transfer (RAFT) polymerization, followed by the encapsulation of LSR into both PnBA-b-POEGA micelles. Based on dynamic light scattering (DLS), the PnBA30-b-POEGA70 and PnBA27-b-POEGA73 (where the subscripts denote wt.% composition of the components) copolymers formed micelles of 10 nm and 24 nm in water. The LSR-loaded PnBA-b-POEGA nanocarriers presented increased size and greater mass nanostructures compared to empty micelles, implying the successful loading of LSR into the inner hydrophobic domains. A thorough NMR (nuclear magnetic resonance) characterization of the LSR-loaded PnBA-b-POEGA nanocarriers was conducted. Strong intermolecular interactions between the biphenyl ring and the butyl chain of LSR with the methylene signals of PnBA were evidenced by 2D-NOESY experiments. The highest hydrophobicity of the PnBA27-b-POEGA73 micelles contributed to an efficient encapsulation of LSR into the micelles exhibiting a greater value of %EE compared to PnBA30-b-POEGA70 + 50% LSR nanocarriers. Ultrasound release profiles of LSR signified that a great amount of the encapsulated LSR is strongly attached to both PnBA30-b-POEGA70 and PnBA27-b-POEGA73 micelles.

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