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MULTIPLE FORMS OF α‐AMYLASE IN MALTING BARLEY VAR. EMMA.
Author(s) -
Hayes Breda,
Harmey Matthew A.,
Byrne Henry
Publication year - 1988
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1988.tb04582.x
Subject(s) - proteolysis , amylase , cleavage (geology) , chemistry , starch , enzyme , biochemistry , biology , paleontology , fracture (geology)
Multiple forms of α‐amylase arise from translation of separate messages and post‐translational proteolytic modification during malting. α‐amylase activity is tolerant of proteolysis. The enzyme appears to have two domains one of which is associated with starch cleavage. The second site which binds cyclodextrin is destroyed by proteolysis. Cleavage yields a low molecular weight form which retains α‐amylase activity.