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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