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- W2052134750 abstract "Abstract Fractionation of proteins secreted by protoplasts and intact cells of Saccharomyces cerevisiae by DEAE-cellullose chromatography in 0.05 M phosphate buffer (pH 7) using a linear gradient of NaCl revealed the presence of at least three different fractions hydrolyzing laminarin (β-1,3-glucan). The first fraction, not retained by the column, appeared to consist of two enzymes exhibiting activity for laminarin, p- nitrophenyl -β- d -glucopyranoside , pustulan (β-1,6-glucan) and a low but detectable activity for laminarin treated with NaIO4. The second fraction, eluted from the DEAE-cellulose column at 0.23 M NaCl possessed the substrate specificity of an endo-β-1,3-glucanase. It exhibited the maximum activity at pH 5.5 in 0.1 M acetate buffer. The third fraction, eluted from the column at 0.35 M NaCl, was an unspecific exo-β-glucanase hydrolyzing terminally both laminarin and pustulan. The pH optimum of the latter enzyme was in the range 4.5–5.0 with laminarin, p- nitrophenyl -β- d -glucopyranoside or pustulan as substrates. The β-glucanases found extracellularly were compared with those occurring in protoplast lysates and cell-free extracts of intact cells." @default.
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- W2052134750 date "1973-09-01" @default.
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- W2052134750 title "Extracellular β-glucanases of the yeast, Saccharomyces cerevisiae" @default.
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- W2052134750 doi "https://doi.org/10.1016/0005-2744(73)90079-x" @default.
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