application in flour-processing industry. Supplementation with recombinant rice quiescin sulfhydryl oxidase (rQSOX) improves the farinograph properties of dough, indicated by the increased dough stability time and decreases degree of softening, and enhanced viscoelastic properties of the dough. Addition of rQSOX (10 IU/g flour) provides remarkable improvement in specific volume (37%) and springiness (17%) of the steamed bread, and significantly reduces the hardness by half, which is attributed to the strengthened gluten network
development of a fast and reliable qualitative plate test for screening secreted fungal sulfhydryl oxidases. Screening is based on the Ellman's reagent, i.e. 5,5'-dithiobis(2-nitrobenzoic acid)
development of a fast and reliable qualitative plate test for screening secreted fungal sulfhydryl oxidases. Screening is based on the Ellman's reagent, i.e. 5,5'-dithiobis(2-nitrobenzoic acid). Enzymes could be identified in Aspergillus tubingensis, Chaetomium globusum, Melanocarpus albomyces, Penicillium aurantiogriseum, Penicillium funiculosum, Coniophora puteana and Trametes hirsuta
the expression of QSOX1 in neuroblastoma tumors may influence its clinical course because this protein is involved in processes such as the maturation of the extracellular matrix and the induction of apoptosis in these tumors. The enzyme can be used as a prognostic biomarker to help better discriminate among risk groups
protective role of QSOX1 against apoptosis. QSOX1 short transcript overexpression slows down proliferation and protects cells from oxidative stress-induced cell death
mutation R194H has been isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins
overexpression of QSOX1a suppresses the lethality of a complete deletion of endoplasmic reticulum oxidase 1 in yeast and restores disulfide bond formation. The enzyme has a minimal role in catalysis of disulfide bonds within the endoplasmic reticulum
overexpression of QSOX1a suppresses the lethality of a complete deletion of endoplasmic reticulum oxidase 1 in yeast and restores disulfide bond formation. The enzyme has a minimal role in catalysis of disulfide bonds within the endoplasmic reticulum