scholarly journals Combining Alcalase hydrolysis and transglutaminase-cross-linking improved bitterness and techno-functional properties of hypoallergenic soybean protein hydrolysates through structural modifications

LWT ◽  
2021 ◽  
pp. 112096
Author(s):  
Qiaozhi Zhang ◽  
Zhouzhou Cheng ◽  
Yong Wang ◽  
Shuyao Zheng ◽  
Yanbo Wang ◽  
...  
Keyword(s):  
Functional Properties ◽  
Soybean Protein ◽  
Protein Hydrolysates ◽  
Cross Linking ◽  
Structural Modifications

Effect of pH and Pepsin Limited Hydrolysis on the Structure and Functional Properties of Soybean Protein Hydrolysates

2013 ◽  
Vol 78 (12) ◽  
pp. C1871-C1877 ◽  
Author(s):  
Chun Cui ◽  
Mouming Zhao ◽  
Boen Yuan ◽  
Yuanhong Zhang ◽  
Jiaoyan Ren
Keyword(s):  
Functional Properties ◽  
Soybean Protein ◽  
Protein Hydrolysates ◽  
Effect Of Ph

scholarly journals Formation of Amphiphilic Molecules from the Most Common Marine Polysaccharides, toward a Sustainable Alternative?

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4445
Author(s):  
Tiphaine Wong ◽  
Lorette Brault ◽  
Eric Gasparotto ◽  
Romuald Vallée ◽  
Pierre-Yves Morvan ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Carboxylic Acid ◽  
Bioactive Compounds ◽  
Biological Properties ◽  
Cross Linking ◽  
Structural Modifications ◽  
Chemical Structures ◽  
Amphiphilic Molecules

Marine polysaccharides are part of the huge seaweeds resources and present many applications for several industries. In order to widen their potential as additives or bioactive compounds, some structural modifications have been studied. Among them, simple hydrophobization reactions have been developed in order to yield to grafted polysaccharides bearing acyl-, aryl-, alkyl-, and alkenyl-groups or fatty acid chains. The resulting polymers are able to present modified physicochemical and/or biological properties of interest in the current pharmaceutical, cosmetics, or food fields. This review covers the chemical structures of the main marine polysaccharides, and then focuses on their structural modifications, and especially on hydrophobization reactions mainly esterification, acylation, alkylation, amidation, or even cross-linking reaction on native hydroxyl-, amine, or carboxylic acid functions. Finally, the question of the necessary requirement for more sustainable processes around these structural modulations of marine polysaccharides is addressed, considering the development of greener technologies applied to traditional polysaccharides.

scholarly journals Impact of Immunoglobulin Isotype and Epitope on the Functional Properties of Vibrio cholerae O-Specific Polysaccharide-Specific Monoclonal Antibodies

mBio ◽  
2021 ◽  
Vol 12 (2) ◽  
Author(s):  
Robert C. Kauffman ◽  
Oluwaseyi Adekunle ◽  
Hanyi Yu ◽  
Alice Cho ◽  
Lindsay E. Nyhoff ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Functional Properties ◽  
Diarrheal Disease ◽  
Cross Linking ◽  
Specific Antibodies ◽  
Immunoglobulin Isotype ◽  
High Affinity ◽  
O Antigen ◽  
The Impact ◽  
Motility Inhibition

ABSTRACT Vibrio cholerae causes the severe diarrheal disease cholera. Clinical disease and current oral cholera vaccines generate antibody responses associated with protection. Immunity is thought to be largely mediated by lipopolysaccharide (LPS)-specific antibodies, primarily targeting the O-antigen. However, the properties and protective mechanism of functionally relevant antibodies have not been well defined. We previously reported on the early B cell response to cholera in a cohort of Bangladeshi patients, from which we characterized a panel of human monoclonal antibodies (MAbs) isolated from acutely induced plasmablasts. All antibodies in that previous study were expressed in an IgG1 backbone irrespective of their original isotype. To clearly determine the impact of affinity, immunoglobulin isotype and subclass on the functional properties of these MAbs, we re-engineered a subset of low- and high-affinity antibodies in different isotype and subclass immunoglobulin backbones and characterized the impact of these changes on binding, vibriocidal, agglutination, and motility inhibition activity. While the high-affinity antibodies bound similarly to O-antigen, irrespective of isotype, the low-affinity antibodies displayed significant avidity differences. Interestingly, despite exhibiting lower binding properties, variants derived from the low-affinity MAbs had comparable agglutination and motility inhibition properties to the potently binding antibodies, suggesting that how the MAb binds to the O-antigen may be critical to function. In addition, not only pentameric IgM and dimeric IgA, but also monomeric IgA, was remarkably more potent than their IgG counterparts at inhibiting motility. Finally, analyzing highly purified F(ab) versions of these antibodies, we show that LPS cross-linking is essential for motility inhibition. IMPORTANCE Immunity to the severe diarrheal disease cholera is largely mediated by lipopolysaccharide (LPS)-specific antibodies. However, the properties and protective mechanisms of functionally relevant antibodies have not been well defined. Here, we have engineered low and high-affinity LPS-specific antibodies in different immunoglobulin backbones in order to assess the impact of affinity, immunoglobulin isotype, and subclass on binding, vibriocidal, agglutination, and motility inhibition functional properties. Importantly, we found that affinity did not directly dictate functional potency since variants derived from the low-affinity MAbs had comparable agglutination and motility inhibition properties to the potently binding antibodies. This suggests that how the antibody binds sterically may be critical to function. In addition, not only pentameric IgM and dimeric IgA, but also monomeric IgA, was remarkably more potent than their IgG counterparts at inhibiting motility. Finally, analyzing highly purified F(ab) versions of these antibodies, we show that LPS cross-linking is essential for motility inhibition.

scholarly journals Production of Lupinus angustifolius protein hydrolysates with improved functional properties

2005 ◽  
Vol 56 (2) ◽  
Author(s):  
Hassane Lqari ◽  
Justo Pedroche ◽  
Julio Girón-Calle ◽  
Javier Vioque ◽  
Francisco Millán
Keyword(s):  
Functional Properties ◽  
Protein Hydrolysates ◽  
Lupinus Angustifolius
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