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Table 2 Kinetic parameters of Bgl1B and Novozyme 188 in the hydrolysis of different types of substrates

From: A novel β-glucosidase from Saccharophagus degradans 2-40T for the efficient hydrolysis of laminarin from brown macroalgae

Enzyme Substrate Glycosidic linkage Vmax (Ua mg−1 protein) Km (mM) kcat (s−1) kcat/Km (mM−1 s−1)
Bgl1B Laminaribiose β-1,3 1.1 × 102 9.9 × 10−1 9.1 × 101 9.2 × 101
Cellobiose β-1,4 1.6 × 101 2.0 × 101 1.3 × 101 6.5 × 10−1
Novozyme 188 Laminaribiose β-1,3 4.2 × 10−1 2.5 × 100 8.5 × 10−1 3.4 × 10−1
Cellobiose β-1,4 3.9 × 100 3.4 × 100 7.8 × 100 2.3 × 100
  1. Kinetic parameters: each value of parameter is the mean of experimental triplicates
  2. aOne unit (U) of Bgl1B was defined as the amount of enzyme required to produce 1 μmol of glucose per min from 0.1% (w/v) cellobiose in 20 mM sodium phosphate buffer (pH 6.0) at 40 °C