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Table 2 Structural and biochemical properties of Lp_0179 and Lp_2757 α-amylases

From: Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1

  Lp_0179 Lp_2757
α-Amylase type Maltose-forming α-amylase Maltogenic amylase
Gene amy2
Lenght (amino acid residues) 440 574
Mw (kDa) 49.9 64.4
Ip 4.89 5.35
CAZy family GH13 GH13
Subfamily GH13_20
Intracellular Yes Yes
Presence of:   
 Domains A, B and C Yes Yes
 CSR I, II, III, and IV Yes Yes
 CSR V No Yes
 N-terminal domain No Yes
 Catalytic triad (D-E-D) Yes Yes
 MpKln motif No Yes
 VAnE motif No Yes
 Trp-47 (Lp_2757) No Yes
 Phe-295 (Lp_2757) No Yes
 Glu-338 (Lp_2757) No Yes
Hydrolysis of starchy carbohydrates
 Dextran (20 kDa) No No
 α-Cyclodextrin No Yes
 β-Cyclodextrin No Yes
 γ-Cyclodextrin No Yes
 Acarbose No Yes
 Panose No Yesa
 Amylopectin No Yes
 Maltopentaose Yes Yes
 Dextrin Yes Yes
 Starch No Yes
 Amylose No Yes
 Pullulan No Yes
Liberation of pNP from
 pNP-α-d-maltopentaoside No Yes
 pNP-α-d-maltopyranoside Yes Yes
  Vmax (μmol min−1) 0.017 ± 0.002 0.016 ± 0.001
  Km (mM) 0.32 ± 0.07 0.62 ± 0.12
  Kcat (min−1) 231.36 ± 0.002 294.85 ± 0.001
  Ecat (mM−1 min−1) 720.08 ± 152.85 480.76 ± 97.20
  Temperature (optimum) (°C) 4–65 30–37
  pH (optimum) 4–7 4–6
  Activators PMSF
  Inhibitors Hg2+ Hg2+, Cu2+, Ni2+
  1. aHydrolysis determined by the detection of very low levels of maltose and glucose