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Partial
purification and characterization of endo-b-1,4-mannanases
from Scopulariopsis candida strains isolated from
solar salterns
Mudau,
Mabyalwa Maria1, Setati, Mathabatha Evodia1,2*
1Department
of Microbial, Biochemical and Food Biotechnology, University
of the Free State, P.O. Box 339, Bloemfontein 9300, South
Africa.
2Microbiology
Discipline, School of Biochemistry, Genetics, Microbiology
and Plant Pathology, University of KwaZulu-Natal, P/Bag
X54001, Durban 4000, South Africa.
*Corresponding author. E-mail:
setatim@ukzn.ac.za.
Accepted 11 February, 2008 |
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Scopulariopsis candida
strains LMK004 and LMK008 previously isolated from a solar
saltern were cultivated in Vogel’s medium supplemented with
NaCl and locust bean gum galactomannan as carbon source and
inducer for
b-mannannase
production. S. candida LMK004 produced up to 180 nkat/ml
whereas LMK008 produced 116 nkat/ml. These levels dropped
significantly when
a-cellulose
was used as carbon source. Both enzymes were partially
purified by ammonium sulphate precipitation and
anion-exchange chromatography. The molecular mass of LMK004
and LMK008
b-mannanases
were estimated to be 41 and 28 kDa, respectively. The
b-mannanase
from LMK004 was most active at pH 5 and 50°C, and retained
³
80% of its activity at pH 5 – 6.5 after 24 h of incubation
at 4°C. In contrast, the LMK008
b-mannanase
retained
³
60% activity between pH 6 – 7. Both enzymes remained stable
for 3 h between 30 and 40°C, and showed loss of activity at
higher temperatures. The LMK008
b-mannanase
tolerated high NaCl concentrations with 70% activity
remaining after incubation for 2 h at 20% NaCl, whereas the
LMK004
b-mannanase
was only active between 0 - 10% NaCl. The current study
shows that fungi that inhabit hypersaline environments
produce plant cell wall degrading enzymes that display
similar properties to other fungi from low-salt
environments.
Key words:
Endo-b-1,4-mannanase,
halophiles, mannan, Scopulariopsis candida, solar
salterns. |