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To stabilize Aspergillus awamori glucoamylase (GA), three proline substitution mutations were constructed. When expressed in Saccharomyces cerevisiae, Ser30--&gt;Pro (S30P) stabilized the enzyme without decreased activity, whereas Asp345--&gt;Pro (D345P) did not significantly alter and Glu408--&gt;Pro (E408P) greatly decreased enzyme thermostability. The S30P mutation was combined with two previously identified stabilizing mutations: Gly137--&gt;Ala, and Asn20--&gt;Cys/Ala27--&gt;Cys (which creates a disulfide bond between positions 20 and 27). The combined mutants demonstrated cumulative stabilization as shown by decreased irreversible thermoinactivation rates between 65 and 80 degrees C. Additionally, two of the combined mutants outperformed wild-type GA in high-temperature (65 degrees C) saccharifications of DE 10 maltodextrin and were more active than the wild-type enzyme when assayed using maltose as substrate.

Stabilization of Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations