Glucoamylase is an economically important enzyme in many industrial processes because 

it is used to sacharify in commercial alcohol production and  starch enzymatic conversion . 

The Enzyme catalyzes the release of b-D-glucose from the non-reducing ends of starch and related 

polysacharides and oligosaccharides. It was first purified from Rhizopus delemar in 1958.

( Tsujisaka et al. 1958). So for there are 66  glucoamylase found in many microoganisms. 

Structure

    Glucoamylase comprises two domains: one is a catalytical domain, and the other 

is responsible for binding granular starch. Take Aspergillus niger glucoamylase for 

example. The catalytic domain is from residue 1 to residue 470 and the binding domain 

is from residue 471 to residue 616. Here are shown structures of Glucoamylase.

full protein(ASPERGILLUS AWAMORI)

Catalytic domain,

starch binding domain (ASPERGILLUS NIGER)

Glucoamylase found since 1958