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Table 5 Kinetic equations and parametric assignments for β-amylase.

From: Kinetic modeling and exploratory numerical simulation of chloroplastic starch degradation

Maltose formation from soluble starch
Maltotriose formation from soluble starch
Release of linear linkage groups from starch1
Maltopentaose degradation to Maltose and Maltotriose
  1. The kinetic model includes formation of maltose and maltotriose from starch and maltopentaose. β-Amylase turnover numbers and , mass concentration E β , equilibrium constant between maltose and maltotetraose K eq , Michaelis constants and , inhibition constant associated with maltotetraose formation , mass concentration of debranching enzyme E d , and rate constant for debranching k d 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.
  2. 1 k d is bi-valued, with for S db /S df < 0.3, and for S db /S df ≥ 0.3.