Amylases are some of the most important industrial enzymes. Their family is
comprised of enzymes with different specificities against a broad range of substrates.
The group of endoamylases, which includes α-amylases, catalyzes the cleavage of
internal α-1,4 linkages in amylose and amylopectin structures, releasing dextrins of
various lengths. Exoamylases, on the other hand, act preferentially in external regions of
the substrate, being represented by several enzymes which act towards molecules as
small as maltose (e.g., maltase) until polysaccharides (e.g., glucoamylases). The third
group comprises debranching amylases, including pullulanases and isoamylases, which
act in α-1,6 bonds (branching linkages). Synergy between these groups of enzymes is
crucial for the improvement of product release rate. Therefore, it is important to assess
methods for the more specific detection as possible for each main group of amylolytic
enzymes, in order to understand their synergy and evaluate potential microbial strains
for their production. This chapter contains an overview of the mode of action of the
main amylolytic enzymes and presents protocols for the quantification of the activity of
the three major groups of amylases.
Keywords: Amylase, starch, amylose amylopectin, endoamylases, exoamylases,
pullulanase, glycogen, polysaccharides.
