Aspergillus welwitschiae: A Potential amylases Producer
Amylases , glycoside hydrolases widely used in several industrial processes, can be produced by many animals, plants, bacteria, and fungi. Fungal amylases from Aspergillus sp. hold remarkable importance in biotechnological applications for presenting a great catalysis efficiency in a wide range of p...
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Veröffentlicht in: | Current microbiology 2022-10, Vol.79 (10), p.307-307, Article 307 |
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Sprache: | eng |
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Zusammenfassung: | Amylases
, glycoside hydrolases widely used in several industrial processes, can be produced by many animals, plants, bacteria, and fungi. Fungal
amylases
from
Aspergillus
sp. hold remarkable importance in biotechnological applications for presenting a great catalysis efficiency in a wide range of pH and temperature. The production of
amylases
is mainly dependent on the genetic background of the species, i.e.,
Aspergillus
strains, and abiotic factors. Among the major producers of
amylases
are the species of
Aspergillus
section
Nigri
, including
Aspergillus welwitschiae
. In this study,
Aspergillus welwitschiae
strains were evaluated for their ability to produce extracellular
amylases
. Among the 24 strains, wild
Aspergillus welwitschiae
UELAs 15.262 and mutant
A. welwitschiae
UELAs 15.262/35 strains showed greater potential for
amylases
production. The
A. welwitschiae
UELAs 15.262 produced more
amylases
(8645 U/mg) when compared to
A. welwitschiae
UELAs 15.262/35 (6666 U/mg). The
amylases
activity from partially purified crude enzymatic extract of
A. welwitschiae
UELAs 15.262 strain obtained at pH 5.5, 60 °C, resulted in 1.98-fold (3837 U/mg) increase in enzymatic activity. Likewise, the
amylases
activity from partially purified crude extract of
A. welwitschiae
UELAs 15.262/35 obtained at pH 5.0, 60 °C resulted in 2.2-fold (9077 U/mg) increase in
amylases
activity. The presence of metallic ions (Cu
2+
and Fe
3+
) also provided an increase of
amylases
activity for both strains. To our knowledge, this is the first study reporting the ability of
Aspergillus welwitschiae
strains in order to produce
amylases
. |
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ISSN: | 0343-8651 1432-0991 |
DOI: | 10.1007/s00284-022-03005-1 |