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Two additional disulfide bonds and combined thermostable mutations were introduced into Aspergillus awamori glucoamylase respectively to test the effects on thermostability and catalytic properties. Computer modeling suggested that a disulfide bond could be built into Aspergillus awamori glucoamylase between positions 20 (wild-type, Asn) and 27 (Ala) as well as positions 72 (Thr) and 471 (Ala) respectively. Amino acid sequence alignments among related glucoamylases showed that a disulfide bond exists in Neurospora crassa glucoamylase at positions 20 and 27. Single cysteines were introduced into positions 20 and 27, and 72 and 471. The corresponding double cysteine mutants were constructed and expressed in Saccharomyces cerevisiac. The double-cysteine mutants were secreted efficiently and disulfide bonds were formed spontaneously after fermentation. The disulfide bond between positions 20 and 27 connects the C-terminal of helix 1 (Asn 20) and a P-tum where residue Ala27 is located while the double mutant A471C/T72C facilitates a disulfide bond between the N-terminus of helix 3 and the end of the 30-residue highly O-glycosylated

Genetic construction and biochemical analysis of thermostability mutants of glucoamylase from Aspergillus awamori