Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability

Santos, Monique Barreto; Carvalho, Carlos Wanderlei Piler de; Garcia‐Rojas, Edwin Elard

doi:10.1016/j.foodhyd.2017.08.016

Cited by 46 publications

(25 citation statements)

References 47 publications

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“…A similar study was performed by Santos et al. () using BSA and lysozyme. The complexes formed in the pH range between 8.0 and 11.0, presenting maximum complexion at pH 9.0.…”

Section: Whey Proteinssupporting

confidence: 58%

“…They observed a shift in the band representing the stretching of N–H and O–H groups, indicating the presence of hydrogen bonds, and therefore concluded that the hydrogen bonds represent a significant force in the stability of the protein–polysaccharide complexes. Likewise, Santos, de Carvalho, and Garcia‐Rojas () verified the participation of electrostatic interactions in the reduction of bands related to amides and the participation of hydrogen bonds in the reduction of bands representing the stretching of N–H and O–H groups in their study of heteroprotein complexes between BSA and lysozyme.…”

Section: Whey Proteinsmentioning

confidence: 84%

“…In the case of interactions between proteins, thermodynamic incompatibility occurs when the pH of the medium is not between the p I of the proteins. At this point, the two proteins have the same charge and, therefore, interactions with the solvent are stronger (Santos, Carvalho, & Garcia‐Rojas, ).…”

Section: Whey Proteinsmentioning

confidence: 99%

“…Similar to the formation of complexes between proteins and polysaccharides, the formation of heteroprotein complexes is distinguished by the formation of complexes at pH values between the p I of the proteins. In this case, one protein behaves as a negatively charged anionic biopolymer (below its p I ), and the other behaves as a positively charged cationic biopolymer (above its p I ; Santos et al., ). The effect of pH on heteroprotein complex formation between β ‐ Lg and lysozyme was studied by Diarrassouba et al.…”

Section: Whey Proteinsmentioning

confidence: 99%

“…Graphical representation of the turbidity variation as a function of pH of a system composed of BSA and lysozyme. The turbidity value has a small increase from pH c followed by a sharp rise in pH θ1 , to maximum value (pH max ) with subsequent reduction in pH θ2 (Adapted Santos et al., ).…”

Section: Whey Proteinsmentioning

confidence: 99%

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Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Santos

Costa

Garcia‐Rojas

2018

Comp Rev Food Sci Food Safe

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Whey proteins are obtained from dairy industry waste. Studies involving the analysis of the bioactive compounds in whey show health benefits, as it is an excellent source of indispensable amino acids. Milk whey contains principally β-lactoglobulin, α-lactoglobulin, bovine serum albumin, and lactoferrin, proteins with innumerable functional and technological properties. One application of these proteins in food is the formation of interpolymer complexes, along with other proteins or anionic polysaccharides. The formation of complexes occurs mainly through electrostatic interactions between a negatively charged biopolymer and a positively charged biopolymer. This formation is influenced by factors such as pH, ionic strength, and biopolymer ratio. Because they do not use high temperatures and chemical reagents and have additional nutritional and functional value, these complexes have been used as encapsulating agents for bioactive ingredients. Recent studies on their training and applications are addressed in this review to boost new research and applications in the food industry, thus increasing opportunities for utilizing whey proteins.

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“…A similar study was performed by Santos et al. () using BSA and lysozyme. The complexes formed in the pH range between 8.0 and 11.0, presenting maximum complexion at pH 9.0.…”

Section: Whey Proteinssupporting

confidence: 58%

Section: Whey Proteinsmentioning

confidence: 84%

Section: Whey Proteinsmentioning

confidence: 99%

Section: Whey Proteinsmentioning

confidence: 99%

Section: Whey Proteinsmentioning

confidence: 99%

See 3 more Smart Citations

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Santos

Costa

Garcia‐Rojas

2018

Comp Rev Food Sci Food Safe

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Protein/Polysaccharide Composite toward Multi‐in‐One Toxin Removal in Blood with Self‐Anticoagulation and Biocompatibility

Chen

Yang

et al. 2023

Adv Healthcare Materials

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Biocompatible adsorbents play an essential role in hemoperfusion. Nevertheless, there are no hemoperfusion adsorbents that can simultaneously remove small and medium toxins, including bilirubin, urea, phosphor, heavy metals, and antibiotics. This bottleneck significantly impedes the miniaturization and portability of hemoperfusion materials and devices. Herein, a biocompatible protein‐polysaccharide complex is reported that exhibits “multi‐in‐one” removal efficacy for liver and kidney metabolism wastes, toxic metal ions, and antibiotics. Through electrostatic interactions and polysaccharide‐mediated coacervation, adsorbents can be prepared by simply mixing lysozyme (LZ) and sodium alginate (SA) together in seconds. The LZ/SA absorbent presented high adsorption capacities for bilirubin, urea, and Hg2+ of up to 468, 331, and 497 mg g−1, respectively, and the excellent anti‐protein adsorption endowed LZ/SA with a record‐high adsorption capacity for bilirubin in the interference of serum albumin to simulate the physiological environment. The LZ/SA adsorbent also has effective adsorption capacity for heavy metals (Pb2+, Cu2+, Cr3+, and Cd2+) and multiple antibiotics (terramycin, tetracycline, enrofloxacin, norfloxacin, roxithromycin, erythromycin, sulfapyrimidine, and sulfamethoxazole). Various adsorption functional groups exposed on the adsorbent surface significantly contribute to the excellent adsorption capacity. This fully bio‐derived protein/alginate‐based hemoperfusion adsorbent has great application prospects in the treatment of blood‐related diseases.

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Interactions between paramyosin and actin greatly improve their thermostability and gel properties

Yin,

Duan,

Zhang

et al. 2023

J Sci Food Agric

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BackgroundMyofibrillar proteins, the main contributors to the quality of meat products, are the main structural protein component of muscle and have functional properties such as the formation of a three‐dimensional protein gel network and water binding. The susceptibility of meat‐derived proteins to heat‐induced aggregation is the functional constraint that hinders their applications in industry, so establishing an effective but simple method to improve their thermostability of the proteins is of great importance.ResultsIn this work, we describe an easy approach to perform high colloidal thermostability of both paramyosin and actin by simply mixing them at low ionic strength. The improvement in thermal stability was found to be derived from intermolecular interactions between these two different proteins through noncovalent binding with each other. Consequently, such interactions protected each of them from thermal‐induced degradation as compared to individual components. Notably, this binary native protein mixture rather than single paramyosin or actin component has the ability to form protein hydrogels with a shear‐thinning and reversible sol‐gel transformation behavior, which is markedly different from most of reported heat‐induced, denatured protein hydrogels.ConclusionThis work not only presents a facile and effective strategy for improvement of the thermal stability and gel properties of a binary paramyosin and actin mixture, but also enhances our understanding of how mutual interactions of protein components affect their physicochemical and functional properties.This article is protected by copyright. All rights reserved.

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Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability

Cited by 46 publications

References 47 publications

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Protein/Polysaccharide Composite toward Multi‐in‐One Toxin Removal in Blood with Self‐Anticoagulation and Biocompatibility

Interactions between paramyosin and actin greatly improve their thermostability and gel properties

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