77
more potent. It had less translation-inhibitory potency. The antifungal, protease,
RNase, mitogenic, antimitogenic, nitric oxide-inducing, hemagglutinating, and
trypsin inhibitory activities were not observed for marmorin (Wong et al. 2008).
5.6 Antibacterial
A protein purified from an aqueous extract of the dried fruiting bodies of Lentinula
edodes showed growth inhibition of Escherichia coli and Staphylococcus aureus.
The antimicrobial activity was evaluated by diffusion disk technique. The isolated
protein (9.69 mg/l) formed bacterial inhibition zone of 2.48 cm for Escherichia coli
and 2.68 cm for Staphylococcus aureus and their size was almost equal to that
observed with 50 mg/l gentamicin. Its molecular weight was 87.2 kDa and has a
specific activity of 28 cm/mg (Sánchez-Minutti et al. 2016).
A novel protein isolated from dried fruiting bodies of the wild mushroom
Clitocybe sinopica showed antibacterial activity. The protein was composed of two
subunits each with a molecular weight of 22 kDa (determined by SDS-PAGE), and
its N-terminal amino acid sequence (SVQATVNGDKML) has not been reported for
other antimicrobial proteins. The protein showed potent antibacterial activity against
Agrobacterium rhizogenes, Agrobacterium tumefaciens, Agrobacterium vitis,
Xanthomonas oryzae, and Xanthomonas malvacearum with a minimum inhibitory
concentration, below 0.6 μM. However, Pseudomonas batatae, Erwinia herbicola,
Escherichia coli, and Staphylococcus aureus were not affected. The antifungal
activity assay against Setosphaeria turcica, Fusarium oxysporum, Verticillium dahliae, Bipolaris maydis, and Bipolaris sativum was negative. The antibacterial activity
against Agrobacterium tumefaciens was stable after exposure to 20–60 °C for
30 min and to pH 4–9 for 1 h (Zheng et al. 2010).
The antibacterial activity of proteins isolated from fruiting bodies of Agaricus
bisporus against both Gram-positive and Gram-negative bacteria was evaluated.
The antibacterial activity of total extract proteins and protein fractions was evaluated by the method of microdilution. The isolated proteins showed growth inhibition against Staphylococcus aureus and methicillin-resistant Staphylococcus aureus
(Houshdar-Tehrani et al. 2012).
A novel defensin called copsin was identified in the coprophilous basidiomycete
Coprinopsis cinerea. The peptide was recombinantly produced in Pichia pastoris,
and the three-dimensional structure was solved by NMR. Copsin was extremely
stable against high temperatures and protease digestion possibly because the cysteine stabilized α-/β-fold with a unique disulfide connectivity, and an N-terminal
pyroglutamate. Copsin had bactericidal activity against different Gram-positive
bacteria, including human pathogens such as Enterococcus faecium and Listeria
monocytogenes. Characterization of this activity revealed that copsin bound specifically to the peptidoglycan precursor lipid II and therefore interfered in the cell wall
biosynthesis. In this case and unlike lantibiotics and other defensins, the third position of the lipid II pentapeptide is essential for effective copsin binding, which
5 Fungal Productions of Biological Active Proteins
more potent. It had less translation-inhibitory potency. The antifungal, protease,
RNase, mitogenic, antimitogenic, nitric oxide-inducing, hemagglutinating, and
trypsin inhibitory activities were not observed for marmorin (Wong et al. 2008).
5.6 Antibacterial
A protein purified from an aqueous extract of the dried fruiting bodies of Lentinula
edodes showed growth inhibition of Escherichia coli and Staphylococcus aureus.
The antimicrobial activity was evaluated by diffusion disk technique. The isolated
protein (9.69 mg/l) formed bacterial inhibition zone of 2.48 cm for Escherichia coli
and 2.68 cm for Staphylococcus aureus and their size was almost equal to that
observed with 50 mg/l gentamicin. Its molecular weight was 87.2 kDa and has a
specific activity of 28 cm/mg (Sánchez-Minutti et al. 2016).
A novel protein isolated from dried fruiting bodies of the wild mushroom
Clitocybe sinopica showed antibacterial activity. The protein was composed of two
subunits each with a molecular weight of 22 kDa (determined by SDS-PAGE), and
its N-terminal amino acid sequence (SVQATVNGDKML) has not been reported for
other antimicrobial proteins. The protein showed potent antibacterial activity against
Agrobacterium rhizogenes, Agrobacterium tumefaciens, Agrobacterium vitis,
Xanthomonas oryzae, and Xanthomonas malvacearum with a minimum inhibitory
concentration, below 0.6 μM. However, Pseudomonas batatae, Erwinia herbicola,
Escherichia coli, and Staphylococcus aureus were not affected. The antifungal
activity assay against Setosphaeria turcica, Fusarium oxysporum, Verticillium dahliae, Bipolaris maydis, and Bipolaris sativum was negative. The antibacterial activity
against Agrobacterium tumefaciens was stable after exposure to 20–60 °C for
30 min and to pH 4–9 for 1 h (Zheng et al. 2010).
The antibacterial activity of proteins isolated from fruiting bodies of Agaricus
bisporus against both Gram-positive and Gram-negative bacteria was evaluated.
The antibacterial activity of total extract proteins and protein fractions was evaluated by the method of microdilution. The isolated proteins showed growth inhibition against Staphylococcus aureus and methicillin-resistant Staphylococcus aureus
(Houshdar-Tehrani et al. 2012).
A novel defensin called copsin was identified in the coprophilous basidiomycete
Coprinopsis cinerea. The peptide was recombinantly produced in Pichia pastoris,
and the three-dimensional structure was solved by NMR. Copsin was extremely
stable against high temperatures and protease digestion possibly because the cysteine stabilized α-/β-fold with a unique disulfide connectivity, and an N-terminal
pyroglutamate. Copsin had bactericidal activity against different Gram-positive
bacteria, including human pathogens such as Enterococcus faecium and Listeria
monocytogenes. Characterization of this activity revealed that copsin bound specifically to the peptidoglycan precursor lipid II and therefore interfered in the cell wall
biosynthesis. In this case and unlike lantibiotics and other defensins, the third position of the lipid II pentapeptide is essential for effective copsin binding, which
5 Fungal Productions of Biological Active Proteins