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• W2078681775 abstract "A 43 kDa α-amylase was purified from Tinospora cordifolia by glycogen precipitation, ammonium sulfate precipitation, gel filtration chromatography, and HPGPLC. The enzyme was optimally active in pH 6.0 at 60 °C and had specific activity of 546.2 U/mg of protein. Activity was stable in the pH range of 4–7 and at temperatures up to 60 °C. PCMB, iodoacetic acid, iodoacetamide, DTNB, and heavy metal ions Hg2+ > Ag+ > Cd2+ inhibited enzyme activity while Ca2+ improved both activity and thermostability. The enzyme was a thiol amylase (3 SH group/mole) and DTNB inhibition of activity was released by cysteine. N-terminal sequence of the enzyme had poor similarity (12–24%) with those of plant and microbial amylases. The enzyme was equally active on soluble starch and amylopectin and released maltose as the major end product." @default.
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• W2078681775 date "2010-12-01" @default.
• W2078681775 modified "2023-10-16" @default.
• W2078681775 title "Purification and characterization of a thiol amylase over produced by a non-cereal non-leguminous plant, Tinospora cordifolia" @default.
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• W2078681775 doi "https://doi.org/10.1016/j.carres.2010.09.029" @default.
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