Table 5.
Kinetic equations and parametric assignments for β-amylase.
| Maltose formation from soluble starch |  |
|---|---|
| Maltotriose formation from soluble starch |  |
| Release of linear linkage groups from starch1 |  |
| Maltopentaose degradation to Maltose and Maltotriose |  |
The kinetic model includes formation of maltose and maltotriose from starch and maltopentaose. β-Amylase turnover numbers 
and 
, mass concentration Eβ, equilibrium constant between maltose and maltotetraose Keq, Michaelis constants 
and 
, inhibition constant associated with maltotetraose formation 
, mass concentration of debranching enzyme Ed, and rate constant for debranching kd are taken from reference [29]. M denotes the mass concentration of maltose, and terms containing M2 are related to β-amylase-catalyzed maltose condensation to yield maltotetraose.
1 kd is bi-valued, with 
for Sdb/Sdf < 0.3, and 
for Sdb/Sdf ≥ 0.3.