Covalent attachment of poly(L-methionine) to food proteins for nutritional and functional improvement

1984 ◽  
Vol 32 (6) ◽  
pp. 1371-1376 ◽  
Author(s):  
Hubert F. Gaertner ◽  
Antoine J. Puigserver
Keyword(s):  
Covalent Attachment ◽  
Functional Improvement ◽  
Food Proteins

Food Safety of Functional Neoglycoproteins Prepared by Covalent Attachment of Galactomannan to Food Proteins

2002 ◽  
Vol 7 (2) ◽  
pp. 139-145 ◽  
Author(s):  
Soichiro Nakamura ◽  
Kazumi Dokai ◽  
Megumi Matsuura ◽  
Junya Hata ◽  
Hiroki Saeki
Keyword(s):  
Food Safety ◽  
Covalent Attachment ◽  
Food Proteins

scholarly journals Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins

Catalysts ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 305
Author(s):  
Marko Jonović ◽  
Milena Žuža ◽  
Verica Đorđević ◽  
Nataša Šekuljica ◽  
Milan Milivojević ◽  
...  
Keyword(s):  
Food System ◽  
Physiological Activity ◽  
Egg White ◽  
Alginate Beads ◽  
Covalent Attachment ◽  
Soy Proteins ◽  
Food Proteins ◽  
Enzyme Loading ◽  
Ultrasonic Spray ◽  
Hydrolysis Of

Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 ± 23 µm) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 ± 103 nm and 394 ± 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 ± 4 mg g−1 on the carrier and the highest immobilized alcalase activity of 2716.1 IU g−1 in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.

Stroke Therapy Using Wearable Robots and Ramachandran Mirror Technique Produces Functional Improvement

2007 ◽  
Author(s):  
Michael K. McBeath ◽  
Flavio DaSilva ◽  
Thomas G. Sugar ◽  
Nancy E. Wechsler ◽  
James Koeneman
Keyword(s):  
Functional Improvement ◽  
Stroke Therapy ◽  
Wearable Robots

Photochemical and Electrochemical Reduction of Carbon Dioxide Catalyzed by a Polyoxometalate-Organic Photosensitizer Complex

2018 ◽  
Author(s):  
Chandan Dey ◽  
Ronny Neumann
Keyword(s):  
Carbon Dioxide ◽  
Cyclic Voltammetry ◽  
Formic Acid ◽  
Electrochemical Reduction ◽  
Mass Spectroscopy ◽  
Photochemical Reactions ◽  
Reducing Agent ◽  
Covalent Attachment ◽  
Hybrid Complex ◽  
Open Face

<p>A manganese substituted Anderson type polyoxometalate, [MnMo<sub>6</sub>O<sub>24</sub>]<sup>9-</sup>, tethered with an anthracene photosensitizer was prepared and used as catalyst for CO<sub>2</sub> reduction. The polyoxometalate-photosensitizer hybrid complex, obtained by covalent attachment of the sensitizer to only one face of the planar polyoxometalate, was characterized by NMR, IR and mass spectroscopy. Cyclic voltammetry measurements show a catalytic response for the reduction of carbon dioxide, thereby suggesting catalysis at the manganese site on the open face of the polyoxometalate. Controlled potentiometric electrolysis showed the reduction of CO<sub>2</sub> to CO with a TOF of ~15 sec<sup>-1</sup>. Further photochemical reactions showed that the polyoxometalate-anthracene hybrid complex was active for the reduction of CO<sub>2</sub> to yield formic acid and/or CO in varying amounts dependent on the reducing agent used. Control experiments showed that the attachment of the photosensitizer to [MnMo<sub>6</sub>O<sub>24</sub>]<sup>9-</sup> is necessary for photocatalysis.</p><div><br></div>

Site-Specific Protein Covalent Attachment to Nanotubes and Its Electronic Impact on Single Molecule Function

2019 ◽  
Author(s):  
Adam Beachey ◽  
Harley Worthy ◽  
William David Jamieson ◽  
Suzanne Thomas ◽  
Benjamin Bowen ◽  
...  
Keyword(s):  
Single Molecule ◽  
Fluorescent Protein ◽  
Functional Integration ◽  
Attachment Site ◽  
Covalent Attachment ◽  
Great Promise ◽  
Functional Coupling ◽  
Phenyl Azide ◽  
Electronic Impact ◽  
Protein Attachment

<p>Functional integration of proteins with carbon-based nanomaterials such as nanotubes holds great promise in emerging electronic and optoelectronic applications. Control over protein attachment poses a major challenge for consistent and useful device fabrication, especially when utilizing single/few molecule properties. Here, we exploit genetically encoded phenyl azide photochemistry to define the direct covalent attachment of three different proteins, including the fluorescent protein GFP, to carbon nanotube side walls. Single molecule fluorescence revealed that on attachment to SWCNTs GFP’s fluorescence changed in terms of intensity and improved resistance to photobleaching; essentially GFP is fluorescent for much longer on attachment. The site of attachment proved important in terms of electronic impact on GFP function, with the attachment site furthest from the functional center having the larger effect on fluorescence. Our approach provides a versatile and general method for generating intimate protein-CNT hybrid bioconjugates. It can be potentially applied easily to any protein of choice; attachment position and thus interface characteristics with the CNT can easily be changed by simply placing the phenyl azide chemistry at different residues by gene mutagenesis. Thus, our approach will allow consistent construction and modulate functional coupling through changing the protein attachment position.</p>

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