Open AccessBiochemical characterization of a Ca 2+ ‐dependent acid trehalase activity from the thermophilic fungus Chaetomium thermophilum var. coprophilum
Author(s) -
Almeida Elzira Maria,
Lourdes Polizeli Maria,
Terenzi Héctor Francisco,
Jorge João Atilio
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13406.x
Subject(s) - trehalase , thermophile , enzyme , chaetomium , biochemistry , mycelium , calcium , chemistry , fungus , molecular mass , biology , food science , botany , organic chemistry , penicillium
A trehalase activity was purified from the mycelium of Chaetomium thermophilum var. corpophilum. The enzyme was composed of two identical polypeptides of apparent molecular mass of 98 kDa. The p I of the enzyme was about 3.9. The purified trehalase was stimulated by calcium, manganese and cobalt and inhibited by EDTA, ADP and ATP. The enzyme exhibited a K m of 0.63 mM, optimum pH of 6.5, and optimum temperature of 55°C. The C . thermophilum trehalase is another example of calcium‐dependent, thermophilic acid trehalases which exhibit mixed properties of regulated (neutral) and non‐regulated (acid) trehalases.