Journal of Microbiology

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Diversity and enzyme activity of Penicillium species associated with macroalgae in Jeju Island: Myung Soo Park , Seobihn Lee , Seung-Yoon Oh , Ga Youn Cho , Young Woon Lim; J. Microbiol. 2016;54(10):646-654. Published online September 30, 2016; DOI: https://doi.org/10.1007/s12275-016-6324-0

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A total of 28 strains of 19 Penicillium species were isolated in a survey of extracellular enzyme-producing fungi from macroalgae along the coast of Jeju Island of Korea. Penicillium species were identified based on morphological and β-tubulin sequence analyses. In addition, the halo-tolerance and enzyme activity of all strains were evaluated. The diversity of Penicillium strains isolated from brown algae was higher than the diversity of strains isolated from green and red algae. The commonly isolated species were Penicillium antarcticum, P. bialowiezense, P. brevicompactum, P. crustosum, P. oxalicum, P. rubens, P. sumatrense, and P. terrigenum. While many strains showed endoglucanase, β-glucosidase, and protease activity, no alginase activity was detected. There was a positive correlation between halo-tolerance and endoglucanase activity within Penicillium species. Among 19 Penicillium species, three species–P. kongii, P. olsonii, and P. viticola– have not been previously recorded in Korea.

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Plastic-inhabiting fungi in marine environments and PCL degradation activity
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Antonie van Leeuwenhoek.2022; 115(12): 1379. CrossRef
Marine fungal abilities to enzymatically degrade algal polysaccharides, proteins and lipids: a review
Yoran Le Strat, Nicolas Ruiz, Joël Fleurence, Yves-François Pouchus, Paul Déléris, Justine Dumay
Journal of Applied Phycology.2022; 34(3): 1131. CrossRef
Characterization of two 1,3-β-glucan-modifying enzymes from Penicillium sumatraense reveals new insights into 1,3-β-glucan metabolism of fungal saprotrophs
Valentina Scafati, Francesca Troilo, Sara Ponziani, Moira Giovannoni, Anna Scortica, Daniela Pontiggia, Francesco Angelucci, Adele Di Matteo, Benedetta Mattei, Manuel Benedetti
Biotechnology for Biofuels and Bioproducts.2022;[Epub] CrossRef
Four Unrecorded Aspergillus Species from the Rhizosphere Soil in South Korea
Jun Won Lee, Sung Hyun Kim, Young-Hyun You, Young Woon Lim, Myung Soo Park
Mycobiology.2021; 49(4): 346. CrossRef
Advances in research on calf rennet substitutes and their effects on cheese quality
Xiaofeng Liu, Yuanfeng Wu, Rongfa Guan, Guochao Jia, YuChen Ma, Yao Zhang
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Mutation, Chemoprofiling, Dereplication, and Isolation of Natural Products from Penicillium oxalicum
Vidushi Abrol, Manoj Kushwaha, Divya Arora, Sharada Mallubhotla, Sundeep Jaglan
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Evaluating the xerophilic potential of moulds on selected egg tempera paints on glass and wooden supports using fluorescent microscopy
Janez Kosel, Maša Kavčič, Lea Legan, Klara Retko, Polonca Ropret
Journal of Cultural Heritage.2021; 52: 44. CrossRef
Dietary effects on gut microbiota of the mesquite lizard Sceloporus grammicus (Wiegmann, 1828) across different altitudes
Nina Montoya-Ciriaco, Selene Gómez-Acata, Ligia Catalina Muñoz-Arenas, Luc Dendooven, Arturo Estrada-Torres, Aníbal H. Díaz de la Vega-Pérez, Yendi E. Navarro-Noya
Microbiome.2020;[Epub] CrossRef
Penicillium from Rhizosphere Soil in Terrestrial and Coastal Environments in South Korea
Myung Soo Park, Jun Won Lee, Sung Hyun Kim, Ji-Hyun Park, Young-Hyun You, Young Woon Lim
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Three Unrecorded Species Belonging toPenicilliumSectionSclerotiorafrom Marine Environments in Korea
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Mycobiology.2019; 47(2): 165. CrossRef
Fungal Diversity and Enzyme Activity Associated with the Macroalgae, Agarum clathratum
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Characterization of Trichoderma reesei Endoglucanase II Expressed Heterologously in Pichia pastoris for Better Biofinishing and Biostoning: Sutanu Samanta , Asitava Basu , Umesh Chandra Halder , Soumitra Kumar Sen; J. Microbiol. 2012;50(3):518-525. Published online June 30, 2012; DOI: https://doi.org/10.1007/s12275-012-1207-5

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Abstract: The endoglucanase II of Trichoderma reesei is considered the most effective enzyme for biofinishing cotton fabrics and biostoning denim garments. However, the commercially available preparation of endoglucanase II is usually mixed with other cellulase components, especially endoglucanase I, resulting in hydrolysis and weight loss of garments during biofinishing and biostoning. We thus isolated the endoglucanase II gene from T. reesei to express this in Pichia pastoris, under the control of a methanol-inducible AOX1 promoter, to avoid the presence of other cellulase components. A highly expressible Mut+ transformant was selected and its expression in BMMH medium was found most suitable for the production of large amounts of the recombinant protein. Recombinant endoglucanase II was purified to electrophoretic homogeneity, and functionally characterized by activity staining. The specific activity of recombinant endoglucanase II was found to be 220.57 EU/mg of protein. Purified recombinant endoglucanase II was estimated to have a molecular mass of 52.8 kDa. The increase in molecular mass was likely due to hyperglycosylation. Hyperglycosylation of recombinant endoglucanase II secreted by P. pastoris did not change the temperature or pH optima as compared to the native protein, but did result in increased thermostability. Kinetic analysis showed that recombinant endoglucanase was most active against amorphous cellulose, such as carboxymethyl cellulose, for which it also had a high affinity.

Research Support, Non-U.S. Gov'ts

Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea: Junli Dong , Yuzhi Hong , Zongze Shao , Ziduo Liu; J. Microbiol. 2010;48(3):393-398. Published online June 23, 2010; DOI: https://doi.org/10.1007/s12275-010-9361-0

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31 Scopus

Abstract: A novel gene encoding an endoglucanase designated Cel5D was cloned from a marine bacterium Martelella mediterranea by genomic library. The gene had a 1,113 bp opening reading frame encoding a 371-amino-acid protein with a molecular mass of 40,508 Da and containing a putative signal peptide (41 amino acids). Cel5D had low similarity (48-51% identity) with other known endoglucanases and consisted of one single catalytic domain, which belonged to the glycosyl hydrolase family 5. The maximum activity of Cel5D was observed at 60°C and pH 5.0. Cel5D displayed broad pH stability within the range of pH 3.0-11.0 and retained hydrolytic activity in the presence of a wide variety of metal ions and some chemical reagents. These characteristics suggest that the enzyme has considerable potential in industrial applications.

Cel8H, a Novel Endoglucanase from the Halophilic Bacterium Halomonas sp. S66-4: Molecular Cloning, Heterogonous Expression, and Biochemical Characterization: Xiaoluo Huang , Zongze Shao , Yuzhi Hong , Ling Lin , Chanjuan Li , Fei Huang , Hui Wang , Ziduo Liu; J. Microbiol. 2010;48(3):318-324. Published online June 23, 2010; DOI: https://doi.org/10.1007/s12275-009-0188-5

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28 Scopus

Abstract: A recombinant Escherichia coli clone expressing an endoglucanase was identified from a genomic library of the halophilic bacterium Halomonas sp. S66-4, and the enzyme was designated Cel8H. The cel8H gene consisted of 1,053 bp and encoded 350 amino acids sharing the highest identity of 48% to other known endoglucanases. The protein was expressed in E. coli BL21 (DE3) and purified to homogeneity. The purified recombinant enzyme had an optimal activity of 4.9 U/mg at pH 5 and 45°C toward the substrate carboxymethylcellulose. It exhibited extraordinary properties which differed from endoglucanases reported previously at the point of high salt tolerance above 5 M, simultaneously with high pH stability at pH 4-12 and high temperature stability at 40-60°C. Various substrate tests indicated that the enzyme hydrolyzes β-1,4-glucosidic bonds specifically.

Degradation of Crystalline Cellulose by the Brown-rot Basidiomycete Fomitopsis palustris: Jeong-Jun Yoon , Young-Kyoon Kim; J. Microbiol. 2005;43(6):487-492.; DOI: https://doi.org/2301 [pii]

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Abstract: This study demonstrated that the brown rot basidiomycete Fomitopsis palustris was able to degrade crystalline cellulose (Avicel). This fungus could also produce the three major cellulases (exoglucanases, endoglucanases, and -glucosidase) when the cells were grown on 2.0% Avicel. Avicel degraded by F. palustris showed a decrease in relative crystallinity from 83% to 78.5% after 14 days of incubation. The characterization study indicated that optimum pH was 4.5 and optimum temperature was 70oC for exoglucanase (cellobiohydrolase) activity. Hydrolysis of Avicel by the crude enzyme from F. palustris yielded 1.6 mg/ml of glucose after 43 h, which corresponded to a cellulose conversion degree of 3.2%. Therefore, this study revealed for the first time that the brown rot basidiomycete F. palustris produces cellulases capable of yielding soluble sugars from crystalline cellulose.

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