• The Korean Journal of Mycology
• /
• v.29 no.1
• /
• pp.1-8
• /
• 2001

To examine the structural properties of the proteoglycan (GMPG, Ganoderma lucidum mycelial proteoglycan) obtained from mycelia in Ganoderma lucidum IY009, we obtained the low and high molecular proteoglycan by ultrafiltration and sepharose CL-4B column chromatography. The physicochemical properties of these fractions were as follows. When the proteoglycan separated by ultrafiltration and sepharose CL-4B column chromatography, its was not fractionated completely. The molecular weight of high molecular proteoglycan by the gel column chromatography (CH) was 250 kD and 2,000 kD, and low molecular proteoglycan was 12kD. The total carbohydrate was consisted of 75.7% (UH) and 96.7% (CH), and the low fraction was 72.7% (UL) and 87.1% (CL), respectively. The sugar of high and low molecular proteoglycan composed of glucose, mannose, fructose, galactose, xylose, ribose and arabinose. Glucose contents of all fraction were ranged from $46.9%{\sim}82.4%$ of the total sugar and the ratio of ${\alpha}$\;and\;{\beta}-glucose$ was $0.84{\sim}1.14$, and its indicated the proteoglycan to be ${\beta}-glucan$. Amino acids pattern showed that the fractions contained a large amount of aspartie acid, glutamic acid, alanine and leucine. These fractions showed the characteristics of IR absorption for ${\beta}-glucan$ at $890\;cm^{-1}\;and\;^{13}C-NMR$ spectroscopy showed the presence of the ${\beta}-1,3-glucan$ and a ${\beta}-1,6-glucan$.

• Journal of Microbiology
• /
• v.40 no.3
• /
• pp.219-223
• /
• 2002

In order to investigate the function of Soo1p/${\alpha}$-COP during post-translational modification and intra-cellular transport of cell wall proteins in Saccharomyces cerevisiae, cell wall proteins from the soo1-1/ret1-1 mutant cells were analyzed. SDS-PAGE analysis of biotin labeled cell wall proteins suggested that the soo1-1 mutation impairs post-translational modification of cell wall proteins, such as N- and/ or Ο-glycosylation. Analysis of cell wall proteins with antibodies against ${\beta}$-1,3-glucan and ${\beta}$-1,6-glucan revealed alteration of the linkage between cell wall proteins and ${\beta}$-glucans in the soo1-1 mutant cells. Compositional sugar analysis of the cell wall proteins also suggested that the soo1-1 mutation impairs glycosylation of cell wall protein in the ER, which is crucial for the maintenance of cell wall integrity.

• Journal of Microbiology and Biotechnology
• /
• v.28 no.8
• /
• pp.1282-1292
• /
• 2018

The exopolysaccharide (EPS) produced by Bacillus amyloliquefaciens GSBa-1 was isolated and purified by ethanol precipitation, and DEAE-cellulose and Sepharose CL-6B chromatographies. The molecular mass of the purified EPS was determined to be 54 kDa. Monosaccharide analysis showed that the EPS was composed of predominantly glucose, and it was further confirmed by NMR spectroscopy to be ${\alpha}-glucan$ that consisted of a trisaccharide repeating unit with possible presence of two ${\alpha}-(1{\rightarrow}3)$ and one ${\alpha}-(1{\rightarrow}6)$ glucosidic linkages. Microstructural analysis showed that the EPS appeared as ellipsoid or globose with a smooth surface. The EPS had a degradation temperature at $240^{\circ}C$. Furthermore, the EPS had strong DPPH and hydroxyl radical scavenging activities, and moderate superoxidant anion scavenging and metal ion-chelating activities. This is the first characterization of a glucan produced by B. amyloliquefaciens with strong antioxidant activity. The results of this study suggest the potential of the EPS from B. amyloliquefaciens GSBa-1 to serve as a natural antioxidant for application in functional products.

• Journal of The Korean Society of Inherited Metabolic disease
• /
• v.12 no.2
• /
• pp.108-112
• /
• 2012

Glycogen storage disease type III (GSD type III, OMIM #232400) is a rare autosomal recessive disease caused by a deficiency of the glycogen-debranching enzyme (GDE) with a mutation in the AGL gene (OMIM *610860). It is known to be bifunctional enzyme, that is, having two independent catalytic activities; 1,4-${\alpha}$-D-glucan 4-${\alpha}$-D-glycosyltransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33) that occur at separate active sites on a single polypeptide chain. Most patients with GSD type III usually have symptoms related to decreased glycogenolysis in liver and muscles, such as hepatomegaly, hypoglycemia, failure to thrive, hyperlipidemia, muscle weakness and cardiomyopathy (type IIIa), however some patients show symptoms restricted to liver (type IIIb). GSD type III is diagnosed by enzyme test through liver or muscle biopsy or mutation analysis of the AGL gene. We report the case of GSD type III proven by gene study after liver biopsy, which revealed c.476delA, c.3444_3445insA in exon 6, 27 of AGL gene in Korean patient.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.46 no.1
• /
• pp.26-33
• /
• 2017

The objective of this study was to examine the immune-enhancing effects of polysaccharides isolated from Phellinus linteus mycelium on Mori ramulus. Crude polysaccharides were isolated by pressurized extraction ($121^{\circ}C$, $1.2kgf/cm^2$, 3 h), ethanol precipitation, and lyophilization. In addition, crude polysaccharides were further fractionated into unabsorbed fractions (PF-1, fraction No. 3~15) and absorbed fractions (PF-2, fraction No. 24~33) by DEAE-sepharose CL-6B column chromatography in order to isolate immune-regulating polysaccharides. The major constituents in PF-1 and PF-2 were total sugar (75.51% and 52.38%), total protein (1.63% and 8.41%), uronic acid (17.53% and 15.04%), and ${\beta}-glucan$ (28.33% and 25.04%), respectively. PF-1 increased production of nitric oxide (NO) and cytokines, such as tumor necrosis factor-alpha ($TNF-{\alpha}$) and interleukin-6 (IL-6) in a dose-dependent manner. The mRNA expression levels of inducible NO synthetase, cyclooxygenase-2, $TNF-{\alpha}$, and IL-6 markedly increased as determined by polymerase chain reaction analysis. The above data led us to conclude that macrophage activation of purified polysaccharides was higher than that of crude polysaccharides. The polysaccharides isolated from P. linteus mycelium on M. ramulus investigated herein are useful as natural immune-enhancing agents.

• Korean Journal of Food Science and Technology
• /
• v.48 no.5
• /
• pp.515-520
• /
• 2016

This study was carried out to investigate the component and immunoregulatory effects of Sparassis crispa stipe. Herein, S. crispa was divided into the pileus and stipe to compare their ingredients (${\beta}-glucan$), antioxidant activity (in vitro), and the immunoregulatory function (cytokines, leukocytes, and spleen weight). The ${\beta}-glucan$ content in each part showed about 1.8 times higher content in the stipe than that in the pileus. The stipe also showed a higher total phenol content and antioxidant activity than the pileus. The cytokines $TNF-{\alpha}$, IL-2, and IL-10 have adjusted in the S. crispa extract-injected groups. In addition, the number of leukocytes was also significantly elevated in the rats administered with the S. crispa stipe extract. These results suggest that the stipe of S. crispa has great potential as an ingredient in functional foods.

• Korean Journal of Medicinal Crop Science
• /
• v.12 no.1
• /
• pp.24-30
• /
• 2004

The immune activities of Ganoderma lucidum Mycelium added garlic extracts (GAM), Ganoderma lucidum Mycelium (GM), garlic extracts (GS) and standard $({\beta}-glucan)$ were compared. GAM enhanced the growth of human immune T cell up to $1.25{\sim}1.46$ times, compared to control group. GAM showed relatively lower cytotoxicity in using normal human lung cell, while GAM showed the most potent inhibitory effect on the human lung carcinoma, compared to GM and GS. The selectivity of GAM was also higher than that of GM and GS. GAM increased the secretion of cytokines, IL-6 and TNF- from human B cell as well as the growth of human immune cells. It can imply that GAM has higher immune activity than GM or GS.

• Korean Journal of Microbiology
• /
• v.22 no.4
• /
• pp.215-222
• /
• 1984

A fungus producing cell wall lytic enzyme for Rhodotorula glutinis was isolated from local soil and identified partially as a species of Aspergillus fumigatus group. Thd cell wall lytic enzyme was an inducible exoenzyme and composed of at least lytic polysaccharidase and protease which act cooperatively in the lysis of intact cells. The lytic polysaccharidase was not able to hydrolyze ${\beta}-1,\;3\;and\;{\beta}-1$, 6-glucan which have the same types of bond as found in the cell wall of Ascomycetous yeasts. The lytic polysaccharidase alone was sufficient to hydrolyze the fractionated cell wall (alkali-insoluble residues) of R. glutinis, whereas it showed low activity against intact cells.

• Food Science and Preservation
• /
• v.25 no.1
• /
• pp.124-135
• /
• 2018

This study investigated the nutritional properties and biological activities of Ganoderma lucidum (GL). The round type of GL contained higher carbohydrate content, while the Nokgak type of GL contained higher crude ash, crude fat, and crude protein content. The most abundant amino acid, fatty acid, mineral, and soluble vitamin observed were valine (round type: 11.90 mg/g and Nokgak type: 17.18 mg/g), linoleic acid (round type: 47.56% and Nokgak type: 75.68%), potassium (round type: 116.50 mg/100 g and Nokgak type: 184.36 mg/100 g), and vitamin B3 (round type: 1.78 mg/100 g and Nokgak type: 1.81 mg/100 g), respectively. In addition, the ${\beta}$-glucan content were 34.15 g/100 g (round type) and 30.07 g/100 g (Nokgak type). The GL 70% ethanol extract at $40^{\circ}C$ showed higher radical scavenging as well as carbohydrate and lipid enzyme inhibition than other conditions. At 1 mg/mL of treatment with the 70% ethanol extract at $40^{\circ}C$ of round type GL, the DPPH, ABTS, hydroxyl radical scavenging, and ${\alpha}$-glucosidase, ${\alpha}$-amylase, and pancreatic lipase inhibition activities obtained were approximately 92.85, 99.74, 58.09, 89.68, 44.68, and 67.56%, respectively.

• Microbiology and Biotechnology Letters
• /
• v.14 no.6
• /
• pp.479-485
• /
• 1986

A 5200 basepair DNA fragment containing the Bacillus amyloliquefaciens amyE gene, encoding liquefying $\alpha$-amylase (1,4-$\alpha$-1)-glucan glucanohydrolase, EC 3.2.1.1), has been inserted into BamHI site of the pUB110 and the hybrid plasmid was designated as pSKS3. The pSKS3 was transformed into the Bacillus subtilis KM2l3 as a host which is a saccharifying $\alpha$-amylase deficient mutant of Bacillus subtilis NA64, and the plasmid in the transformed cell was expressed $\alpha$-amylase production and kanamycin resistance. The $\alpha$-amylase production of the transformed cell was reduced to one fifth of that of the donor strain. The Bacillus subtilis KM2l3 tarring pSKS3 indicated that the amyE gene product is a polypeptide which has the same electrophoretic mobility with that of the Bacillus amyloliquefaciens, but different from the saccharifying $\alpha$-amylase of Bacillus subtilis NA64. It means that the amyE gene of pSKS3 originales from the Bacillus amyloliquefaciens.