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Thermophilic glucoamylase from Talaromyces flavus
Author(s) -
Hang Y. D.,
Woodams E. E.
Publication year - 1993
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1993.tb00383.x
Subject(s) - library science , thermophile , biology , computer science , biochemistry , enzyme
The heat‐resistant mold, Talaromyces flavus , was found to produce a thermophilic glucoamylase that exhibited the highest activity at 50°C and in the pH range of 4.0–4.8. The K m and V max values of the crude enzyme for amylopectin were 0.21% and 16.7 mg glucose 1 ‐1 , min ‐1 , respectively. The molecular weight of the enzyme as estimated by the gel filtration method was 42 kDa.

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