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A Simulation Model For Malt Enzyme Activities in Kilning: Jari J. Hämäläinen and Pekka Reinikainen
A Simulation Model For Malt Enzyme Activities in Kilning: Jari J. Hämäläinen and Pekka Reinikainen
k α (T1 (t )) = k 0α e RT1 ( t ) 1
RMSE = ∑i =1i ( xT (t i ) − xˆ T (t i ; p))2
M
(15)
Mi
␣(t) is the ␣-amylase activity at time t, k is the frequency ␣
0
factor for inactivation (1/min), and E␣ is the activation over the set was minimised. In (15) x̂T refers to the mea-
energy (J /mol). The inactivation rate is thus assumed to sured average grain moisture, i to the ith measurement,
be proportional to instantaneous ␣-amylase activity and and Mi to the number of measurements in an experiment.
Fig. 1. Simulated and measured malt moisture and drying tem- Fig. 2. Simulated and measured -glucanase activity for experi-
perature T1(t) for experiments 1 (A), 5 (B), and 9 (C). ments 1 (A), 5 (B), and 9 (C).
Fig. 3. Simulated and measured ␣-amylase activity for experi- Fig. 4. Simulated and measured diastatic power for experiments
ments 1 (A), 5 (B), and 9 (C). 1 (A), 5 (B), and 9 (C).
Simulations
The model identification results above show that the
prediction errors for the analysed variables are in the or-
der of 5–10% during kilning. By taking the variability
into account during the process and in the analysis meth-
ods, the predictions should be accurate enough to simulate
the effects of changes in the kilning programme on the
enzyme activities.
The thermostabilities of the enzymes were analysed by
varying the curing temperature during the last four hours
of kilning (Fig. 6). In the case of an 80°C curing tempera-
ture, the -glucanase activity of green malt was reduced
by 43%, ␣-amylase activity by 4%, diastatic power by
15%, and limit-dextrinase activity by 25%. The results
match well with the earlier reported findings. According
to Sissons et al.18 almost similar curing conditions in malt
kilning reduced the -glucanase activity of green malt by
44% and limit-dextrinase activity by 24%. According to
the simulation, increasing the curing temperature from
80°C to 90°C still causes a 10% reduction in the final
-glucanase activity, 5% reduction in ␣-amylase activity,
21% reduction in diastatic power, and 47% reduction in
limit-dextrinase activity (Fig. 6).
The effects of drying temperature T1(t) on the relative
enzyme inactivation rates k(T1(t))xT (t), k␣(T1(t)), k␦(T1(t)),
and k(T1(t)) are shown in Fig. 7 (see (11)–(14)). For -
glucanase, the effect of grain moisture xT (t) was also ana-
lysed (moisture on a wet basis in Fig. 7b).
For temperatures higher than 75°C, the relative inacti-
vation rates of starch hydrolysing enzymes are in decreas-
ing order: limit-dextrinase, diastatic power, and ␣-amy-
lase (Fig. 7a). Such a high temperature is normally only
applied during the last hours of kilning when the grain
moisture is already under 10%. Then the relative inactiva-
tion rate of -glucanase is between that of ␣-amylase and
limit-dextrinase (Fig. 7b). However, at higher moistures
-glucanase is inactivated faster than the starch hydrolys-
Fig. 5. Simulated and measured limit-dextrinase activity for ex- ing enzymes, a fact that is well known, for instance under
periments 1 (A), 5 (B), and 9 (C). mashing conditions (for example see Hämäläinen et al.7 ).