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- W2002856853 abstract "α-Amylase from germinated mung beans (Vigna radiata) has been purified 600-fold to electrophoretic homogeneity and a final specific activity of 437 U/mg. SDS–PAGE of the final preparation revealed a single protein band of 46 kDa. The optimum pH was 5.6. The energy of activation was determined to be 7.03 kcal/mol in the temperature range 15–55 °C. Km for starch was 1.6 mg/mL in 50 mM sodium acetate buffer, pH 5.5. Thermal inactivation studies at 70 °C showed first-order kinetics with rate constant (k) equal to 0.005 min−1. Mung bean α-amylase showed high specificity for its primary substrate starch. Addition of EDTA (10 mM) caused irreversible loss of activity. Mung bean α-amylase is inhibited in a non-competitive manner by heavy metal ions, for example, mercury with a Ki of 110 μM. Homology modelling studies with mung bean α-amylase using barley α-amylases Amy 1 and Amy 2 as templates showed a very similar structure as expected from the high sequence identity. The model showed that α-amylase from mung beans has no sugar-binding site, instead it has a methionine. Furthermore, instead of two trptophans, it has Val277 and Lys278, which are the conserved residues, important for proper folding and conformational stability." @default.
- W2002856853 created "2016-06-24" @default.
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- W2002856853 date "2007-06-01" @default.
- W2002856853 modified "2023-10-18" @default.
- W2002856853 title "α-Amylase from mung beans (Vigna radiata) – Correlation of biochemical properties and tertiary structure by homology modelling" @default.
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- W2002856853 doi "https://doi.org/10.1016/j.phytochem.2007.04.006" @default.
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