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FURTHER CHARACTERIZATION OF THE 12 kDa PROTEASE/ALPHA AMYLASE INHIBITOR PRESENT IN MAIZE SEEDS
Author(s) -
BLANCOLABRA A.,
CHAGOLLALOPEZ A.,
MARÍNEZGALLARDO N.,
VALDESRODRIGUEZ S.
Publication year - 1995
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1995.tb00518.x
Subject(s) - trypsin , proteases , protease , trypsin inhibitor , amylase , enzyme , protease inhibitor (pharmacology) , biochemistry , kunitz sti protease inhibitor , biology , enzyme inhibitor , virus , antiretroviral therapy , viral load , virology
A 12 kDa protease/α‐amylase inhibitor was purified from maize seeds and studied. Its trypsin‐ and amylase‐inhibitor activities against enzymes from different origins were determined, as well as its optimal pH for inhibition. Eight different proteases, extracted from insects and fungi which attack grains during storage, were tested with the inhibitor. Bovine trypsin and trypsin‐like proteases from the insect P. truncatus, and the fungi A. niger and A. fumigatus, were recognized by this inhibitor. Out of 11 α‐amylases tested, only those from T. castaneum and C. maculatus were recognized by this inhibitor. The optimal pH's for the inhibition of trypsin and the trypsin‐like protease from P. truncatus were 8.0 and 7.5, respectively. The optimal pH activity was 5.0 for the inhibition of amylases from T. castaneum and C. maculatus.