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C-type lectin 7, which accumulates at the late stage of the sixth instar in diapause-destined larvae, may be highly stable at low temperature and can be used by diapausing individuals.
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Lipase was highly stable at 55 °C 200 bar.
These proteases were highly stable at temperature below 50°C but had rapid activity loss of 10-30% from 50°C onward.
Both the two aminosilane-modified PSi structures (PSi-Me,f-NH2) were highly stable at this condition.
The purified protein is highly stable at room temperature, which makes it potentially valuable for protein crystallization.
They can be used as a sweetening agent in all foods because they are highly stable at high temperatures and in acid environments.
Immobilized inulinase was highly stable at 60 °C and retained 80%% of its activity after 4 h whereas free inulinase retained 70%% of its initial activity.
This enzyme was highly stable at wide pH range (7.0 9.0) and showed 32% enzyme activity after initial denaturation at 50 °C for 1 h.
pH stability assays indicated that Spr Cel8A was highly stable at a pH range between 4 and 8.5, retaining 40 90 % of its original activity after 1 h of incubation at 28 °C (Fig. 3b).
SDS-PAGE analysis showed that while V1F, V1D and V1L mutants are highly stable at high concentrations of SDS, the V1G is highly susceptible to denaturation.
On the other hand, Glac15 was highly stable at pH 5.0 to 7.0.
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