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- W2017185956 abstract "Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60°C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn(2+), Ca(2+), Mg(2+), Cu(2+), Mn(2+)) and stimulated by 50mM Fe(2+). Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect." @default.
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- W2017185956 date "2012-03-01" @default.
- W2017185956 modified "2023-10-16" @default.
- W2017185956 title "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite" @default.
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- W2017185956 doi "https://doi.org/10.1016/j.biortech.2011.11.077" @default.
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