• Korean Journal of Microbiology
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• v.36 no.1
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• pp.14-19
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• 2000

Algal lytic enzyme, an extracellular enzyme, was purified from the culture filtrate of Penicillium oxalicum(HCLF-34) by ultrafiltration, gel filtration chromatography, and anion exchange chromatography. The enzyme has a molecular mass of approximately 22 kDa, an it is a monomer by renaturation SDS-PAGE. The amino acid sequences of the enzyme was revealed to be NH2-Glu-Ser-Tyr-Ser-Ser-Asn-Ala-Ala-Gly-Ala-Val-Leu-Ile---, had about 84% identity with the mature light chain of aspergillopepsin II precursor and 81% identity with the mature protein of the acid proteinase EapC precursor.

• Microbiology and Biotechnology Letters
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• v.22 no.1
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• pp.23-30
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• 1994

Intergeneric hybrids formed between Aspergillus oryzae var oryzae and Penicillium verruculosum F-3 were obtained by nuclear transfer technique. Several auxotrophic mutants isolated fromconidio-spores of the two strains mutagenized with ultraviolet and N-methyl-N-nitrosoguanidine. Optimal conditions for formation of intergeneric hybrids were investigated. Frequencies of hybrid formation by nuclear transfer were 3$\times $10$^{-5}$ $~$1$\times $10$^{-5}$. From observation of genetic stability, conidial size, DNA content, nuclear stain, it was suggested that their karyptypes are aneuploid. The hybrid posses the 1.3$~$2.2 fold higher amylase activities than those of parental strains. It was also revealed that some hybids had different isozyme patterns compared to those of parental strains by amylase activity assays.

• Korean Journal of Food Science and Technology
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• v.18 no.1
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• pp.1-5
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• 1986

Putrefactive microorganisms from infected onion bulbs collected at several areas were isolated and identified. The infecting microorganisms were mostly the species of Botrytis, Fusarium, Penicillium, Ericinia and Pseudomonas, among which the last was not pathogenic to onion bulbs. Fumigation of onion bulbs with Tetrachloroisophthalonitrile cut down decay rate by half of the control and the onion bulbs stored at 80% RH showed slow decay rate than those stored at 90% RH. The decay of onion bulbs was mainly caused by molds and the portions of them were 78-85% of Botrytis, 11-17% of Fusarium and 3-5% of Penicillium.

• Mycobiology
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• v.35 no.1
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• pp.36-38
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• 2007

Stored rice was collected from rice processing complexes of National Agricultural Cooperative Federation of 11 regions in Korea to evaluate the occurrence of fungi and bacteria and to identify the predominant fungi and bacteria to the genus levels. Most rice samples generally produced the higher levels of fungi and bacteria than white rice. The occurrence of fungi and bacteria varied in various locations of Korea. Among fungi observed, Aspergillus spp. and Penicillium spp. were dominant in the samples and Aspergillus spp. were observed more frequently than Penicillium spp. Predominant bacteria from rice and white rice samples tentatively belonged to the Genus Bacillus, Pectobacterium, Pantoea, and Microbacterium according to BIOLOG and FAME analyses. The results of this study showed that rice in Korea was contaminated in a relatively high level by two dominant storage fungi such as Aspergillus spp. and Penicillium spp. In addition, occurrence of mycotoxins in rice by the fungi could be possible and thus it is necessary to control the storage fungi.

• Journal of Microbiology and Biotechnology
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• v.2 no.1
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• pp.14-20
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• 1992

Some microorganisms isolated from soil, including some bacteria and fungi, were found to secrete an extracellular soymilk-clotting enzyme. Among them, an isolated fungus showed the highest soymilk-clotting activity and the strain was assigned to genus Penicillium based on its cultural and morphological characteristics, and designated as Penicillium sp. L-151K. Soymilk-clotting enzymes A and B produced by Penicillium sp. L-151K were purified by ammonium sulfate precipitation and chromatographies on Sephadex G-25, CM-Sephadex, Sephadex G-100 and phenyl-Toyopearl gel. The two purified enzymes A and B were found to be homogeneous by polyacrylamide gel electrophoresis at pH 9.5. The molecular weights of enzyme A and B were 24, 000 and 40, 000, respectively, by gel filtration on Sephadex G-100. Enzymes A and B coagulated soymilk optimally at $60^\circ{C}$ and were stable up to $50^\circ{C}$. Both enzymes were most active at pH 5.8 for soymilk coagulation, and were stable with approximately 80% of original activity from pH 3.0 to 5.0. Each enzyme was an acidic protease with an optimum pH of 3.0 for casein digestion. The soymilk-clotting efficiency of these enzymes was improved with $CaCl_2\;or\;MgCl_2$ when making soymilk-curd.

• Microbiology and Biotechnology Letters
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• v.28 no.5
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• pp.291-297
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• 2000

A strain producing high levels of compaction was isolated from soil and identified as Penicillium sp. Y-8515 based on the morphological characteristics and ribosomal RNA sequence analysis. Optimization of several different carbon and nitrogen sources for the effective production of compaction was performed resulting in the medium compositions containing 5%(w/v) glucose, 1.0 % soybean meal, 0.5% yeast extract, 0.5%(NH$_4$)$_2$$SO_4$, 0.25%,$ NaH_2$$PO_4$, 0.25% $CaCO_3$. The fixed con-centration of glucose(5%, w/v) and relatively lower concentrations(less than 2.5%, w/v) of soybean meal stimu-lated the transformation of the growth morphology from filamentous to pellet form. Comparing to that by filamentous form, the production of compactin by pellet form increased up to 1.5 folds. In a fed-batch fermentation, continuous feeding of the mixture of glucose and nitrogen source at the ratio of 10:1 showed 3.5-fold more produc-tion yield of compaction comparing to the batch mode.

• Korean Journal of Microbiology
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• v.40 no.1
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• pp.12-16
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• 2004

Acid proteinase has been discovered in Aspergillus niger (acid protease A) and Cryphonectria parasitica (acid proteinase EapC) and it plays major roles in cheese formation from milk. In this study, a partial gene encoding acid proteinase in Penicillium oxalicum HCLF-34 was cloned by using PCR with degenerate primers corresponding to highly conserved regions of the acid proteinase. The partial acid proteinase gene in P. oxalicum HCLF-34 contains an open reading frame of 438 base pairs and encodes an acid proteinase protein of 146 amino aicds. The predicted amino acid sequences showed 71 % homology with acid protease A and 67% homology with EapC.

• The Korean Journal of Mycology
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• v.23 no.4 s.75
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• pp.318-324
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• 1995

The evolutionary relationships of the genus Trichoderma and related taxa were assessed using partial sequencing of 18S ribosomal RNA. Phylogenetic tree divided into three major groups; 1. Saccharomyces cerevisiae-Geotrichum klebahnii-Alternaria mali group; 2. Neurospora crassa-Aspergillus-Penicillium-Chrysosporium pannorum-Scopulariopsis sp. group; 3. Trichoderma group. The genus Trichoderma seemed to be phylogenetically separated from Saccharomyces cerevisiae, Aspergillus and Penicillium groups, and have passed through it's own evolutionary pathway.

• Journal of Microbiology and Biotechnology
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• v.18 no.10
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• pp.1663-1665
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• 2008

Acyl-coenzyme A: cholesterol acyltransferase (ACAT) catalyzes cholesterol esterification and plays an important role in the intestinal absorption of cholesterol, hepatic production of lipoproteins, and accumulation of cholesteryl ester within cells. During the course of screening to find ACAT inhibitors from microbial sources, the present authors isolated pyripyropene A from Penicillium griseofulvum F1959. Pyripyropene A, an ACAT2-specific inhibitor, has already been produced from Aspergillus fumigatus. Yet, Aspergillus fumigatus is a pathogen and only produces a limited amount of pyripyropene A, making the isolation of pyripyropene A troublesome. In contrast, Penicillium griseofulvum F1959 was found to produce approximately 28 times more pyripyropene A than Aspergillus fumigatus, plus this report also describes the ideal conditions for the production of pyripyropene A by Penicillium griseofulvum F1959 and its subsequent purification.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.3
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• pp.340-348
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• 1993

Cross-synergistic interactions were evaluated with purified enzymes from Trichoderma viride and Penicillium funiculosum cellulase. Different synergistic patterns between enzyme components were observed. Exo-exo type synergism was found to be the most effective for degrading Avicel in all cases. Exo-endo type synergism was found to be slightly less effective. Extended hydrolysis of Avicel was carried out using mixtures of purified enzyme components with the crude cellulase from a different source. Addition of $\beta$-glucosidase from P. funiculosum cellulase to T. viride cellulase provided the great enhancement of Avicel hydrolysis. In addition, exoglucanase from T. viride cellulase was found to enhance P. funiculosum cellulase in degradation of Avicel. In conclusion, it was possible to enhance the hydrolysis of Avicel by altering the proportions of enzyme components by supplementing enzyme components from a different source. Different types of synergisms acted together to achieve maximum conversion.