scholarly journals Oleogels—Their Applicability and Methods of Characterization

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1673
Author(s):  
Eckhard Flöter ◽  
Till Wettlaufer ◽  
Valentina Conty ◽  
Maria Scharfe
Keyword(s):  
Knowledge Base ◽  
Binding Capacity ◽  
Current Method ◽  
Solubility Data ◽  
Product Innovations ◽  
Laboratory Bench ◽  
Comprehensive Knowledge ◽  
Technology Area ◽  
Oil Binding

Oleogels or, more precisely, non-triglyceride structured lipid phases have been researched excessively in the last decade. Yet, no comprehensive knowledge base has emerged, allowing technology elevation from the laboratory bench into the industrial food application. That is partly due to insufficient characterization of the structuring systems studied. Examining a single composition decided upon by arbitrary methods does not stimulate progress in the research and technology area. A framework that gives much better guidance to product applications can easily be derived. For example, the incremental structure contribution concept is advocated as a parameter to compare the potency of structuring systems. These can straightforwardly be determined by combining solubility data and structural measurements in the recommended manner. The current method to determine the oil-binding capacity suffers from reproducibility and relevance. A newly developed method is suggested to overcome these shortcomings. The recommended new characterization of oleogels should contribute to a more comprehensive knowledge base necessary for product innovations.

scholarly journals Valorization of Flaxseed Oil Cake Residual from Cold-Press Oil Production as a Material for Preparation of Spray-Dried Functional Powders for Food Applications as Emulsion Stabilizers

Biomolecules ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 153 ◽  
Author(s):  
Emilia Drozłowska ◽  
Łukasz Łopusiewicz ◽  
Monika Mężyńska ◽  
Artur Bartkowiak
Keyword(s):  
Antioxidant Activity ◽  
Binding Capacity ◽  
Flaxseed Oil ◽  
Inlet Temperature ◽  
Emulsifying Activity ◽  
Cold Press ◽  
Food Applications ◽  
Water Holding ◽  
Spray Dried ◽  
Oil Binding

Flaxseed oil cake extract (residual from cold-press oil production and rich in proteins and polysaccharides) was evaluated as a potential substrate for the preparation of spray-dried powders with emulsifying activity. Three variants of powders were obtained using different spray-drying process inlet temperatures: 160 °C, 180 °C, and 200 °C. The influence of temperature on physicochemical features (water holding capacity, oil binding capacity, water activity, solubility, color, chemical composition, antioxidant activity, and surface morphology) of the powders was estimated. Additionally, the emulsifying activity of the powders and the stability of oil-in-water emulsions prepared with their various content (0.5%, 1%, and 3%) were determined. Results showed that inlet temperature had significant influence on all physicochemical and functional properties of the powders. Increased inlet temperature decreased solubility and antioxidant activity but increased water-holding capacity, oil-binding capacity, and emulsifying activity. The emulsions prepared with the powder obtained at 200 °C showed the highest stability. SEM images showed the production of relatively spherical particles which were folded or wrinkled with a lot of dentures. This study could open a promising pathway for producing natural and plant-based spray-dried powders for food applications as emulsion stabilizers.

Electrolysis soy protein isolate-based oleogels prepared with an emulsion-templated approach

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Dianyu Yu ◽  
Yan Chen ◽  
Xing Chen ◽  
Yunyan Huang ◽  
Liqi Wang ◽  
...  
Keyword(s):  
Soy Protein ◽  
Xanthan Gum ◽  
Binding Capacity ◽  
Soy Protein Isolate ◽  
Single Layer ◽  
Protein Isolate ◽  
Regulatory Limits ◽  
Order Of Magnitude ◽  
The Stability ◽  
Oil Binding

Abstract This research focuses on the use of protein-polyphenol complex and protein-polyphenol: polysaccharide complexes to prepare oleogels through an emulsion-templated approach. Electrolysis soy protein isolate (ESPI) could be effectively adsorbed on the surface of a single-layer emulsion to increase the particle size. The order of the negative charges of the emulsion after adding polysaccharides was xanthan gum (XG)> pectin> carboxymethyl cellulose (CMC). Rheological behavior showed that the stability of the double-layer emulsions increased, and the viscoelasticity increased around one order of magnitude with the addition of polysaccharides. The oil binding capacity (OBC) of the oleogel prepared by adding polysaccharides increased to more than 97%. The peroxide value (PV) and anisidine value (AV) of XG oleogel were the minimum values in all samples. The AV and POV were within the regulatory limits of China after storage for 21 days. This provides a reference to design of ESPI-based oleogel for different applications.

scholarly journals A g-Type Lysozyme from Deep-Sea Hydrothermal Vent Shrimp Kills Selectively Gram-Negative Bacteria

Molecules ◽  
2021 ◽  
Vol 26 (24) ◽  
pp. 7624
Author(s):  
Jing-Chang Luo ◽  
Jian Zhang ◽  
Li Sun
Keyword(s):  
Deep Sea ◽  
Hydrothermal Vent ◽  
Binding Capacity ◽  
Cellular Membrane ◽  
Structural Features ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Bacterial Binding ◽  
Muramidase Activity

Lysozyme is a key effector molecule of the innate immune system in both vertebrate and invertebrate. It is classified into six types, one of which is the goose-type (g-type). To date, no study on g-type lysozyme in crustacean has been documented. Here, we report the identification and characterization of a g-type lysozyme (named LysG1) from the shrimp inhabiting a deep-sea hydrothermal vent in Manus Basin. LysG1 possesses conserved structural features of g-type lysozymes. The recombinant LysG1 (rLysG1) exhibited no muramidase activity and killed selectively Gram-negative bacteria in a manner that depended on temperature, pH, and metal ions. rLysG1 bound target bacteria via interaction with bacterial cell wall components, notably lipopolysaccharide (LPS), and induced cellular membrane permeabilization, which eventually caused cell lysis. The endotoxin-binding capacity enabled rLysG1 to alleviate the inflammatory response induced by LPS. Mutation analysis showed that the bacterial binding and killing activities of rLysG1 required the integrity of the conserved α3 and 4 helixes of the protein. Together, these results provide the first insight into the activity and working mechanism of g-type lysozyme in crustacean and deep-sea organisms.

scholarly journals MIKB: A Manually Curated and Comprehensive Knowledge Base for Myocardial Infarction

2021 ◽  
Author(s):  
Chaoying Zhan ◽  
Yingbo Zhang ◽  
Xingyun Liu ◽  
Rongrong Wu ◽  
Ke Zhang ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Knowledge Base ◽  
Comprehensive Knowledge

scholarly journals Human xylosyltransferase I and N-terminal truncated forms: functional characterization of the core enzyme

2006 ◽  
Vol 394 (1) ◽  
pp. 163-171 ◽  
Author(s):  
Sandra Müller ◽  
Jennifer Disse ◽  
Manuela Schöttler ◽  
Sylvia Schön ◽  
Christian Prante ◽  
...  
Keyword(s):  
Amino Acids ◽  
Catalytic Activity ◽  
Binding Capacity ◽  
Functional Characterization ◽  
Terminal Region ◽  
Binding Motif ◽  
Heparin Binding ◽  
Loss Of Function ◽  
The Impact

Human XT-I (xylosyltransferase I; EC 2.4.2.26) initiates the biosynthesis of the glycosaminoglycan linkage region and is a diagnostic marker of an enhanced proteoglycan biosynthesis. In the present study, we have investigated mutant enzymes of human XT-I and assessed the impact of the N-terminal region on the enzymatic activity. Soluble mutant enzymes of human XT-I with deletions at the N-terminal domain were expressed in insect cells and analysed for catalytic activity. As many as 260 amino acids could be truncated at the N-terminal region of the enzyme without affecting its catalytic activity. However, truncation of 266, 272 and 273 amino acids resulted in a 70, 90 and >98% loss in catalytic activity. Interestingly, deletion of the single 12 amino acid motif G261KEAISALSRAK272 leads to a loss-of-function XT-I mutant. This is in agreement with our findings analysing the importance of the Cys residues where we have shown that C276A mutation resulted in a nearly inactive XT-I enzyme. Moreover, we investigated the location of the heparin-binding site of human XT-I using the truncated mutants. Heparin binding was observed to be slightly altered in mutants lacking 289 or 568 amino acids, but deletion of the potential heparin-binding motif P721KKVFKI727 did not lead to a loss of heparin binding capacity. The effect of heparin or UDP on the XT-I activity of all mutants was not significantly different from that of the wild-type. Our study demonstrates that over 80% of the nucleotide sequence of the XT-I-cDNA is necessary for expressing a recombinant enzyme with full catalytic activity.

scholarly journals Modification of structural and functional properties of sunflower 11S globulin hydrolysates

2016 ◽  
Vol 33 (No. 5) ◽  
pp. 474-479 ◽  
Author(s):  
J. Ren ◽  
Ch. Song ◽  
P. Wang ◽  
S. Li ◽  
N. Kopparapu ◽  
...  
Keyword(s):  
Functional Properties ◽  
Emulsion Stability ◽  
Activity Index ◽  
Binding Capacity ◽  
Surface Hydrophobicity ◽  
Foaming Properties ◽  
Hydrolysis Time ◽  
Structural And Functional Properties ◽  
11S Globulin ◽  
Oil Binding

The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

scholarly journals CitrusKB: a comprehensive knowledge base for transcriptome and interactome of Citrus spp. infected by Xanthomonas citri subsp. citri at different infection stages

Database ◽  
2020 ◽  
Vol 2020 ◽  
Author(s):  
Adriano Ferrasa ◽  
Mayara M Murata ◽  
Teresa D C G Cofre ◽  
Juliana S Cavallini ◽  
Gustavo Peron ◽  
...  
Keyword(s):  
Knowledge Base ◽  
Citrus Canker ◽  
Limited Information ◽  
Xanthomonas Citri ◽  
Comprehensive Knowledge ◽  
Genetic Mechanisms ◽  
Serious Disease ◽  
Canker Development ◽  
User Friendly

Abstract Citrus canker type A is a serious disease caused by Xanthomonas citri subsp. citri (X. citri), which is responsible for severe losses to growers and to the citrus industry worldwide. To date, no canker-resistant citrus genotypes are available, and there is limited information regarding the molecular and genetic mechanisms involved in the early stages of the citrus canker development. Here, we present the CitrusKB knowledge base. This is the first in vivo interactome database for different citrus cultivars, and it was produced to provide a valuable resource of information on citrus and their interaction with the citrus canker bacterium X. citri. CitrusKB provides tools for a user-friendly web interface to let users search and analyse a large amount of information regarding eight citrus cultivars with distinct levels of susceptibility to the disease, with controls and infected plants at different stages of infection by the citrus canker bacterium X. citri. Currently, CitrusKB comprises a reference citrus genome and its transcriptome, expressed transcripts, pseudogenes and predicted genomic variations (SNPs and SSRs). The updating process will continue over time by the incorporation of novel annotations and analysis tools. We expect that CitrusKB may substantially contribute to the field of citrus genomics. CitrusKB is accessible at http://bioinfo.deinfo.uepg.br/citrus. Users can download all the generated raw sequences and generated datasets by this study from the CitrusKB website.

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