Effect of Disulfide Bond Reduction on Bovine Serum Albumin‐Stabilized Emulsion Gel Formed by Microbial Transglutaminase

Kang, Y.N.; Kim, Hakhyun; Shin, Weon‐Sun; Woo, Gregory; Moon, Tae Wha

doi:10.1111/j.1365-2621.2003.tb05749.x

Cited by 34 publications

(20 citation statements)

References 29 publications

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“…This includes gels prepared with proteins, such as whey protein (Rosa et al, 2006), beta-lactoglobulin (Line et al, 2005), sodium caseinate (Dickinson and Casanova, 1999), gelatin (Sala et al, 2009a), soy protein isolate (Tang and Liu, 2013), and bovine serum albumin; Kang et al, 2003), and polysaccharides: high acyl gellan gum (Lorenzo et al, 2013), kcarrageenan (Sala et al, 2009a,b) and alginate (Sato et al, 2014).…”

Section: Stabilisation Of Food Emulsionsmentioning

confidence: 98%

The effect of filler particles on the texture of food gels

Dille

Draget

Hattrem

2015

Modifying Food Texture

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Section: Stabilisation Of Food Emulsionsmentioning

confidence: 98%

The effect of filler particles on the texture of food gels

Dille

Draget

Hattrem

2015

Modifying Food Texture

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“…BSA has 17 interchain disulfide bonds formed by 34 oxidized cysteines and 1 free sulfhydryl group in one reduced cysteine. 16 …”

Section: Introductionmentioning

confidence: 99%

Studying the Effects of Cysteine Residues on Protein Interactions with Silver Nanoparticles

et al. 2015

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Studies of protein and organothiol interactions with silver nanoparticles (AgNPs) are important for understanding AgNP nanotoxicity, antimicrobial activity, and material fabrications. Reported herein is a systematic investigation of the effects of both reduced and oxidized protein cysteine residues on protein interactions with AgNPs. The model proteins included wild-type and mutated protein GB3 variants that contain 0, 1, or 2 reduced cysteine residues, respectively. Bovine serum albumin (BSA) that contains a total of 34 oxidized (disulfide-linked) cysteine residues and one reduced cysteine residue was also included. Protein cysteine content has no detectable effect on the kinetics of protein/AgNP binding. However, only proteins that contain reduced cysteine residues induce significant AgNP dissolution. Proteins can slow down, but do not prevent the AgNP dissolution induced by subsequently added organothiols. The insights provided in this work are important to the mechanistic understanding of AgNP stability in biofluids that are rich in proteins and amino acid thiols.

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“…The effective cross-linking of proteins by mTGase depends not solely on the presence of glutamine and lysine residues in the primary structure, but also on the tertiary structure of the protein. 13,14 In this study, gelatin was modified by cross-linking it with various concentrations of mTGase. The mechanical properties of cross-linked gels were characterized by dynamic rheological and static, unconfined compression tests.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic stabilization of gelatin‐based scaffolds

et al. 2004

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The definitive goal of this research is to develop protein-based scaffolds for use in soft tissue regeneration, particularly in the field of dermal healing. The premise of this investigation was to characterize the mechanical properties of gelatin cross-linked with microbial transglutaminase (mTGase) and to investigate the cytocompatibility of mTGase cross-linked gelatin. Dynamic rheological analysis revealed a significant increase in the storage modulus and thermal stability of gelatin after cross-linking with mTGase. Static, unconfined compression tests showed an increase in Young's modulus of gelatin gels after mTGase cross-linking. A comparable increase in gel strength was observed with 0.03% mTGase and 0.25% glutaraldehyde cross-linked gelatin gels. In vitro studies using 3T3 fibroblasts indicated cytotoxicity at a concentration of 0.05% mTGase after 72 h. However, no significant inhibition of cell proliferation was seen with cells grown on lower concentrations of mTGase cross-linked gelatin substrates. The mechanical improvement and cytocompatibility of mTGase crosslinked gelatin suggests mTGase has potential for use in stabilizing gelatin gels for tissueengineering applications.

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Effect of Disulfide Bond Reduction on Bovine Serum Albumin‐Stabilized Emulsion Gel Formed by Microbial Transglutaminase

Cited by 34 publications

References 29 publications

The effect of filler particles on the texture of food gels

The effect of filler particles on the texture of food gels

Studying the Effects of Cysteine Residues on Protein Interactions with Silver Nanoparticles

Enzymatic stabilization of gelatin‐based scaffolds

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