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Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase.

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Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied

Enzymatic degradation of Ginkgolic acid by Laccase Immobilized on Novel Electrospunned Nanofiber Mat.

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Ginkgo biloba leaf extract contains many health beneficial active ingredients. However, ginkgolic acid, one of the major components found in G. biloba extract, may cause serious allergic and toxic side effects to the living organisms. The purpose of this study is to immobilize the

Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein.

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Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom

Identification of a basidiomycete-specific Vilse-like GTPase activating proteins (GAPs) and its roles in the production of virulence factors in Cryptococcus neoformans.

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Cryptococcus neoformans is a basidiomycetous pathogenic yeast that causes fatal infections in both immunocompetent and immunocompromised patients. Regulation on the production of its virulence factors is not fully understood. Here we reported the characterization of a gene, named CVH1(CNA06260),

Phytoremediation of textile dyes and effluents: Current scenario and future prospects.

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Phytoremediation has emerged as a green, passive, solar energy driven and cost effective approach for environmental cleanup when compared to physico-chemical and even other biological methods. Textile dyes and effluents are condemned as one of the worst polluters of our precious water bodies and

R-SNARE homolog MoSec22 is required for conidiogenesis, cell wall integrity, and pathogenesis of Magnaporthe oryzae.

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Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediate intracellular vesicle fusion, which is an essential cellular process of the eukaryotic cells. To investigate the role of SNARE proteins in the rice blast fungus Magnaporthe oryzae, MoSec22, an ortholog of

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