• Korean Journal of Food Science and Technology
• /
• v.10 no.2
• /
• pp.237-244
• /
• 1978

Among the strains isolated form the various sources, the strain AC-12 producing a powerful pectinase was selected by the extensive screening test. The selected strain was indentified and its toxicity investigated. The conditions of the pectinase production, the characteristics of the purified enzyme and the clarification effect on the apple juice were studied. 1. The selected strain AC-12 was identified by the classification method of paper and fennel and named as Aspergillus sp. AC-12. 2. As a result of the breeding test of the white mouse, no toxicity was found from this enzyme. 3. The yield of pectinase in the medium of defatted rice bran was much better than that in the medium of wheat bran. 4. The optimum conditions for the culture of the strain in the medium of defatted rice bran were that the cultural time was 72hrs, the amount of water to be added about 80%, temperature $30{\sim}35^{\circ}C$ and pH $3.0{\sim}5.0$. 5. The yield of pectinase was slightly increased by the addition of pectin to the medium of defatted rice bran and by the addition of pectin, $NaNO_3$ and $K_2HPO_4$ to the medium of wheat bran, respectively. 6. The optimum conditions for the enzyme activity were pH $3.0{\sim}4.0$ and temperature $40{\sim}50^{\circ}C$. The enzyme was stable below $40^{\circ}C$ and pH $2.0{\sim}8.0$, respectively. But above $50^{\circ}C,$ this enzyme was abruptly inactivated. The activity was slightly increased by the addition of $MnSO_4\;and\;CuSO_4.$ 7. It was regarded that the opimum temperature for the clarification of the apple juice was $40{\sim}50^{\circ}C$, the optimum pH 3.0 and the optimun concentration of the enzyme 0.1%, and the apple juice was almost clarified by the reaction at $45^{\circ}C$ for 60 minutes.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.36 no.11
• /
• pp.1482-1485
• /
• 2007

In this study, extraction yield of ginseng and contents of phenolic compounds were increased through enzyme and heat treatment, and antioxidant activities of each treatment group were investigated. In the case of enzyme treatment groups, the extraction yields showed remarkable difference: pectinase (76.0%)> cellulase (44.7%)> ${\alpha}-amylase$ (43.1%)> protease (34.3%). Heat treatment groups did not show much difference in extraction yields $(51.1{\sim}53.1%)$ except for $90^{\circ}C-treated$ group (48.7%). Pectinase-treated group (2.21%) and $90^{\circ}C$ heat treatment group (2.34%) showed the highest total phenol contents. DPPH radical scavenging activities of the solvent-treated, enzyme-treated and heat-treated extracts were $12.3{\sim}33.2%$, $29.7{\sim}40.3%$ and $57.8{\sim}75.2%$, respectively, at 100 mg/mL concentration. The pectinase-treated extract exhibited the greatest ABTS radical scavenging activity (60%), followed by $150^{\circ}C$, $ 120^{\circ}C$, and $90^{\circ}C-treated$ groups.

• Journal of Life Science
• /
• v.10 no.1
• /
• pp.1-5
• /
• 2000

Pectinase was isolated from culture medium of Bacillus sp. BS-214 and purified 105-fold with 3.4% yield by ammonium sulfate precipitation, gel filteration using Sephadex G-75 and DEAE-cellulose followed by gel filteration through Sephadex G-100. The molecular weight of the purified enzyme was estimated to be about 43 kDa on SDS-PAGE and by gel filtration, indicating that the enzyme is a monomer. the optium pH and temperature of the enzyme were 9.0 and 55$^{\circ}C$, respectively. the enzyme was stable at 60$^{\circ}C$ for 30min and in a pH range from 7.5 to 10.5 for 12 h ant 4$^{\circ}C$. The enzyme activity was highly enhanced by Ca2+, and also K+, Li+ and Na+showed a positive effect, while stongly inhibited by Zn2+ and Hg2+.

• Journal of Microbiology and Biotechnology
• /
• v.30 no.6
• /
• pp.946-954
• /
• 2020

Platycodon grandiflorum root (Platycodi radix) saponins, platycosides, have been used as health supplements and food items for the treatment of respiratory disorders and pulmonary diseases. Deglycosylated saponins have been known to exert stronger biological effects than their glycosylated forms. In the present study, glycosylated platycosides in Platycodi radix extract were biotransformed into deglycosylated 3-O-β-ᴅ-glucopyranosyl platycosides, including 3-O-β-ᴅ-glucopyranosyl platycodigenin, 3-O-β-ᴅ-glucopyranosyl polygalacic acid, and 3-O-β-ᴅ-glucopyranosyl platyconic acid, by pectinase from Aspergillus aculeatus. This is the first report on the quantitative enzymatic production of 3-O-β-ᴅ-glucopyranosyl platycosides. The chemical structures of 3-O-β-ᴅ-glucopyranosyl platycosides were identified with LC/MS. Moreover, the biotransformation pathways of the three types of platycosides in Platycodi radix into 3-O-β-ᴅ-glucopyranosyl platycosides were established.

• Korean Journal of Food Science and Technology
• /
• v.45 no.5
• /
• pp.636-641
• /
• 2013

We prepared 2 different crude polysaccharides from persimmon leaves, by hot water (PLW-0) and pectinase digestion (PLE-0), respectively. PLW-0 and PLE-0 showed similar sugar compositions and contained 11 different sugars, including rarely observed sugars such as 2-methyl-fucose, 2-methyl-xylose, apiose, and aceric acid. However, the uronic acid content of PLE-0 was lower than that of PLW-0, because of pectinase treatment. In normal mice, administration of PLW-0 and PLE-0 increased the spleen index and splenocyte proliferation. The effect of PLE-0 on the spleen index and splenocyte proliferation was greater than that of PLW-0. We subsequently assessed the immunomodulatory activities of PLW-0 and PLE-0 on cyclophosphamide (CY)-induced immunosuppressed mice. We revealed that mice treated with PLW- 0 or PLE-0 showed increased splenocyte proliferation, NK cell activity, and white blood cell numbers. Taken together, our results indicate that PLW-0 and PLE-0 can enhance immune function in normal mice and modulate CY-induced immune suppression.

• Food Science and Preservation
• /
• v.14 no.6
• /
• pp.702-708
• /
• 2007

The effects of pectinase treatment and other processing conditions on juice yield from Rubus coreanus, and physicochemical changes during alcohol fermentation, were investigated. The yield from R. coreanus increased by 8.60% with Pectinex 100L treatment (500 ppm, 30 min) compared to a control group. The soluble solid content in the group fermented at $24^{\circ}Brix$ by addition of sucrose (24B-group), and the group fermented at $8^{\circ}Brix$ by addition of 16% sucrose after 4 days of fermentation (8B-group) decreased to $8.2{\sim}8.3$ and $7.7{\sim}8.0%$ after 10 days of fermentation, respectively, and no significant differences were observed with Pectinex 100L treatment. Initial titratable acidity in the enzyme treatment was slightly higher ($1.18{\sim}1.22%$) than for the control group (1.02%). The initial $L^*$ and $b^*$ values of R. coreanus juice decreased with enzyme treatment, and the $a^*$ value increased, but the color difference (${\Delta}E$) between the control and enzyme treatment gradually decreased with fermentation time. The ethanol contents in the 24B-group and the 8B-group were $16.01{\sim}16.22%$ and $13.29{\sim}13.52%$, respectively, after 10 days of fermentation. The methanol contents in the enzyme treatment and the control were $0.359{\sim}0.404$ and $0.520{\sim}0.604$ mg/mL, respectively, and within standard regulations (1 mg/mL).

• Food Science and Preservation
• /
• v.21 no.4
• /
• pp.506-511
• /
• 2014

In Gyeongsangbuk-do seongju area, hundreds of tons of spoiled oriental melon are harvested annually. Therefore, ways to prevent such spoilage are needed. This study was conducted to investigate the quality characteristics of spoiled oriental melon juice after enzyme treatment for the production of oriental melon concentrate. The treatment of the oriental melon juice with three kinds of enzymes with variable concentrations showed the following results. PECE(1), which was compounded pectinase and cellulase at 0.01% (v/v), gave the melon a 0.16 brown color and 0.01 turbidity, and the highest L value of 97.00. The detected free sugar contents were fructose, glucose and sucrose, with the amount of sucrose the highest at roughly 4,000 mg%. The mixture of different enzyme treatments resulted in a 0.15 brown color and 0.01 turbidity at 60 minutes, and the L value was high at 97.25. The enzyme treatment temperatures of $50^{\circ}C$ and $60^{\circ}C$ yielded a low-level brown color and low turbidity, but the L values were high at $60^{\circ}C$ and $70^{\circ}C$. These results showed that 0.01% (v/v) mixing enzyme, i.e., pectinase and cellulose compounded at $60^{\circ}C$ for 60 min, must be used for the production of oriental melon concentrate.

• The Korean Journal of Food And Nutrition
• /
• v.9 no.4
• /
• pp.409-412
• /
• 1996

본 연구는 '96학년도 배재대학교 교내 학술 연구비 지원으로 수행되었다. ^x Juice yield of peach "Yoo Myung" by pretreatment of various enzymes and heat was determined, and physicochemical properties of peach wine fermented by some Saccharomyces cerevisiae were also investigated. 89.2% of juice yield was showed in mixture treatment of pectinase and cellulase at 35$^{\circ}C$ for 8 hrs, 82% of yield was also showed in single treatment of pectinase and cellulase. Ethyl alcohol content of peach wine fermented by wild type Saccharomyces cerevisiae 49-2 was 14.55. However, wine from thermophilic Saccharomyces cerevisiae D-71 was excellent in taste and flavor.nd flavor.

• Mycobiology
• /
• v.39 no.2
• /
• pp.118-120
• /
• 2011

The ability of Ganoderma to produce extracellular enzymes, including ${\beta}$-glucosidase, cellulase, avicelase, pectinase, xylanase, protease, amylase, and ligninase was tested in chromogenic media. ${\beta}$-glucosidase showed the highest activity, among the eight tested enzymes. In particular, Ganoderma neo-japonicum showed significantly stronger activity for ${\beta}$-glucosidase than that of the other enzymes. Two Ganoderma lucidum isolates showed moderate activity for avicelase; however, Ganoderma neojaponicum showed the strongest activity. Moderate ligninase activity was only observed in Ganoderma neo-japonicum. In contrast, pectinase, amylase, protease, and cellulase were not present in Ganoderma. The results show that the degree of activity of the tested enzymes varied depending on the Ganoderma species tested.

• Journal of agriculture & life science
• /
• v.45 no.1
• /
• pp.119-124
• /
• 2011

Trichoderma spp. are very important as being a major source for the industrial production of various secreting enzymes in the field of white biotechnology. In this work, Agrobacterium-mediated transformation (AMT) was studied using Trichoderma sp. KACC 40541 which has high activities of amylase, pectinase, cellobiohydrolase and xylanase. In principal, optimized NaOH treatment, prior to Agrobacterium infection, to the mycelium was determined to be very effective for AMT.