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- W2012191503 abstract "An endoglucanase liberated from Zea mays seedling cell-walls by LiCl was purified by using SP-Sephadex, CM-Sephadex, and gel filtration, resulting in a 98-fold increase in specific activity. It has a pH optimum of 4.5–5.0 and is heat stable up to 40–45°. Compounds that interact with sulfhydryl groups did not inhibit the activity of the enzyme, nor did EDTA, suggesting that the enzyme does not require free sulfhydryl groups or metal ions for activity. The endoglucanase has an apparent molecular weight of 20–25,000 and an isoelectric point of ⩾9. Hydrolytic activity against (1»3),(1»4)-β-d-glucans is restricted to isolated sites, with the release of high-molecular-weight products (10–15,000). Action on isolated, inactivated Zea cell-walls caused the release of approximately the same products as observed when the enzyme was incubated with soluble (1→3), (1→4)-β-d-glucans." @default.
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- W2012191503 date "1986-05-01" @default.
- W2012191503 modified "2023-10-16" @default.
- W2012191503 title "Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings" @default.
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- W2012191503 doi "https://doi.org/10.1016/s0008-6215(00)90394-x" @default.
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