Effect of tyrosinase and caffeic acid crosslinking of turbot parvalbumin on the digestibility, and release of mediators and cytokines from activated RBL-2H3 cells

Ahmed, Ifty; Ma, Jian; Liu, Zhenxing; Lin, Hong; Xu, Lili; Sun, Lirui; Tian, Shenglan

doi:10.1016/j.foodchem.2019.125209

Cited by 26 publications

(16 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…No network was formed in the absence of tyrosinase. Enzymatic cross-linking of proteins has gained increasing interest in food technology to create novel food products or improve textural properties of dairy products and biopolymers ( Ahmed et al., 2019 ). Permana et al.…”

Section: Resultsmentioning

confidence: 99%

“…Purified enzymes with improved activity and stability could easily be manipulated for use in several biotechnological processes such as synthesis of organic compound, ability to form cross-linked protein networks etc. Enzymatic cross-linking of proteins has gained increasing interest in food technology to create novel food products or improve textural properties of dairy products and biopolymers ( Ahmed et al., 2019 ).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Potentials of purified tyrosinase from yam (Dioscorea spp) as a biocatalyst in the synthesis of cross-linked protein networks

Ilesanmi

Adedugbe

Adewale

2021

Heliyon

View full text Add to dashboard Cite

We report the usefulness of yam tyrosinase as a catalyst in the synthesis of cross-linked protein networks for biopolymers. The enzyme was purified using aqueous two-phase partitioning (ATPs) and peptide mapping on SDS-PAGE was carried out to ascertain degree of similarities of tyrosinase from the yam species. The mapping revealed distinct peptide bands of 3, 4, 4 and 2 for tyrosinase from D. praehensilis , D. alata , D. rotundata and C. esculenta respectively purified using conventional method. In contrast, continuous broad band was noticed for the ATPS-purified enzymes due to bound polyethylene glycol (PEG). Tyrosinase from D. praehensilis with overall better properties was used in the synthesis of cross-linked protein networks. The enzyme catalyzed conversion of soluble proteins from whey, moringa leaves, pumpkin leaves and cow blood into fibrous (cross-linked) protein networks for improved properties and functionalities. The purified tyrosinase from D. praehensilis was also covalently bonded to bovine serum albumin (BSA) forming tyrosinase-BSA adduct with molecular weight of 118 ± 2.0 kDa, revealing its potential as a reporter enzyme by reporting BSA. The overall result further reinforces yam tyrosinase as an enzyme of interest in various biotechnological applications.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Potentials of purified tyrosinase from yam (Dioscorea spp) as a biocatalyst in the synthesis of cross-linked protein networks

Ilesanmi

Adedugbe

Adewale

2021

Heliyon

View full text Add to dashboard Cite

show abstract

“…The secretions of histamine and β-hexosaminidase decreased by 66.9% and 35.6%, respectively, in the RBL-2H3 cell assay. In another study, Ahmed et al (2019) reported that the immunoreactivity of PV was drastically reduced in simulated gastric fluid and simulated intestinal fluid. Enzymatic crosslinking hampered the release of cellular degranulation process in RBL-2H3 cell lines by inhibiting the release of histamine (35.01%), β-hexosaminidase (66.02%), prostaglandin D2 (34.96%), tryptase (29.25%), cysteinyl leukotrienes (29.72%), IL-13 (38.93%) and IL-4 (43.99%).…”

Section: Fish Allergymentioning

confidence: 95%

“…The reduction in the immunoreactivity of food allergens could subsequently alter the original way of antigen presentation and cause oral tolerance. Enzymatic crosslinking technique has proved to be a remarkable alternative to physical and chemical processing methods in mitigating the allergenicity of food allergens by suppressing the degranulation of mast cells (Ahmed et al, 2019(Ahmed et al, , 2020Fei et al, 2016;Yu et al, 2016). Overall, the crosslinked allergens have shown to have therapeutic effects in relieving food allergies due to their potent immunomodulatory and immunosuppressive effects.…”

Section: Facets Of the Application Of Enzymatic Crosslinking Techniquementioning

confidence: 99%

“…Enzymatic crosslinking of dietary proteins can alter the conformational structures, surface properties, charge moieties, and molecular weights of proteins. Moreover, the enzymatic process assists in the modification of biological properties of allergenic proteins, including solubility, ligand binding, digestibility, antigenicity, and IgE binding potentials (Ahmed et al, 2019(Ahmed et al, , 2020Yuan et al, 2018). Two types of enzymatic methods are used currently to reduce the allergenic potential of food allergens.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enzymatic crosslinking and food allergenicity: A comprehensive review

Ahmed

Chen

et al. 2021

Comp Rev Food Sci Food Safe

Self Cite

View full text Add to dashboard Cite

Food allergy has become a major global public health concern. In the past decades, enzymatic crosslinking technique has been employed to mitigate the immunoreactivity of food allergens. It is an emerging non-thermal technique that can serve as a great alternative to conventional food processing approaches in developing hypoallergenic food products, owing to their benefits of high specificity and selectivity. Enzymatic crosslinking via tyrosinase (TYR), laccase (LAC), peroxidase (PO), and transglutaminase (TG) modifies the structural and biochemical properties of food allergens that subsequently cause denaturation and masking of the antigenic epitopes. LAC, TYR, and PO catalyze the oxidation of tyrosine side chains to initiate protein crosslinking, while TG initiates isopeptide bonding between lysine and glutamine residues. Enzymatic treatment produces a high molecular weight crosslinked polymer with reduced immunoreactivity and IgE-binding potential. Crosslinked allergens further inhibit mast cell degranulation due to the lower immunostimulatory potential that assists in the equilibration of T-helper (Th)1/Th2 immunobalance. This review provides an updated overview of the studies carried out in the last decade on the potential application of enzymatic crosslinking for mitigating food allergenicity that can be of importance in the context of developing hypoallergenic/non-allergenic food products.

show abstract

Comparison of immunological properties of recombinant and natural turbot (Scophthalmus maximus) parvalbumin

Huang

Liu

et al. 2021

Eur Food Res Technol

View full text Add to dashboard Cite

Effect of tyrosinase and caffeic acid crosslinking of turbot parvalbumin on the digestibility, and release of mediators and cytokines from activated RBL-2H3 cells

Cited by 26 publications

References 37 publications

Potentials of purified tyrosinase from yam (Dioscorea spp) as a biocatalyst in the synthesis of cross-linked protein networks

Potentials of purified tyrosinase from yam (Dioscorea spp) as a biocatalyst in the synthesis of cross-linked protein networks

Enzymatic crosslinking and food allergenicity: A comprehensive review

Comparison of immunological properties of recombinant and natural turbot (Scophthalmus maximus) parvalbumin

Contact Info

Product

Resources

About