• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.2
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• pp.180-185
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• 1997

This work was carried out to investigate change of polygalacturonase activities and polygalacturonase patterns by gel filtration chromatography during softening of persimmon and jujube fruits. During softening of two kinds of fruit, polygalacturonase activities of water-soluble and salt-soluble proteins were increased, but that of cell wall-bound proteins was decreased. In water-soluble and salt-soluble proteins of persimmon fruits, two peaks of polygalacturonase activity were separated in mature stages, but one peak in soft stages. During softening of those fruits, the peaks of polygalacturonase activity in water-soluble and salt-soluble proteins appeared on the same fraction with the peaks of polygalacturonase activity in cell wall-bound proteins.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.6
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• pp.596-604
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• 1990

Polygalacturonase activity was not detected at turning stage but were 55.01 and 206.70 units/100g -fr. wt. in mature and soft persimmon, respectively. Polygalacturonase have two isoenzymes and its molecular weight was estimated to be 55,000 doltons by the method of gel filtration. Vmax and Km of polygalacturonase 1 were 0.195$\mu$ mole reducing-sugar/$m\ell$/30 min. and 3.50mg/$m\ell$, respectively. The optimum temperature and pH of the enzyme appeared to 4$0^{\circ}C$ and 3.5, respectively. Polygalacturonase I had Vmax of 0.110m mo1e reducing-sugar/$m\ell$/30min. and Km value of 2.50mg/$m\ell$, The optimum temperature and pH of polygalcturonase II appear 4$0^{\circ}C$ and 4.0, respectively. Polygalacturonase I was fairly stable at 6$0^{\circ}C$while polygalacturonase II appeared to be stable up to 4$0^{\circ}C$.

• The Korean Journal of Mycology
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• v.21 no.3
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• pp.195-199
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• 1993

This experiments was designed for development of Fusarium oxysporum strains with enhanced activity of polygalacturonase by means of mutants and protoplasts fusion. Six auxotrophic mutants of F. oxysporum were induced by treatment of MNNG. Protoplasts from mutants were formed from early exoponential mycelium after treatment with driselase(10 mg/ml) using 0.6 M KCl as osmotic stabilizer. Fusion experiments between protoplasts of several auxotrophic mutants were done using polyethyleneglycol 8,000 and $CaCl_2$. The frequency of fusion was $5.0{\times}10^{-3}$ as determined from several experiments. Activity of polygalacturonase was determined by the methods of modified DNS. Consequently, the polygalacturonase activities of mutants and fusant derived F. oxysporum were 1.4 to 3.5 times greater than that of the parental strain, and mutant Fx-2 seemed to be the best strain. Thus, the method we used seemed to be favorable for the improvement of strains.

• Korean Journal of Food Science and Technology
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• v.31 no.1
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• pp.263-266
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• 1999

Pectic substances are important to sustain the textural properties of kimchi during fermentation and distribution. Therefore proper control of pectin degrading enzyme activity is critical on quality control in kimchi industry. Pectin degrading enzymes of kimchi ingredients were assayed to improve the product quality. Among pectin degrading enzymes, polygalacturonase and pectinesterase were selected. The specific activity of polygalacturonase was the highest in salted and fermented anchovy, followed by chinese radish. Considering the amount of protein contents, salted and fermented anchovy and dried red pepper showed higher polygalacturonase activity than other ingredients. In terms of specific activity, chinese radish showed the highest pectinesterase activity, followed by salted and fermented anchovy. However, the total activity of salted and fermented anchovy was the highest. Chinese radish showed higher pectinesterase activity than any other ingredients.

• Microbiology and Biotechnology Letters
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• v.17 no.6
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• pp.580-586
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• 1989

Penicillium sp. CB-20 was selected for strong polygalacturonase activity among various strains of molds found in soil. The optimum pH for the enzyme activity was 5.0 and optimum temperature was 4$0^{\circ}C$. The enzyme was relatively stable in acidic condition and unstable by heat treatment. The activation energy, Km and V$_{max}$ for the polygalacturonase were 2.499 Kcal/mol, 2.13$\times$10$^{-2}$mol/l, and 104.17 $\mu$mol/min. The activity of polygalacturonase was inhibited by Ag$^{+}$, Cu$^{++}$, Pb$^{++}$, Fe$^{+++}$, $Ca^{++}$, Na$^+$, Mn$^{++}$. The enzyme can be inactivated by the treatment ethylenediamintetra acetic acid, 2,4-dinitrophenol and $H_2O$$_2$. The results indicate the possible involvement of histidine, chelate and terminal amino group as active site. The enzyme was endo-type polygalacturonase.

• The Korean Journal of Mycology
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• v.18 no.1
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• pp.7-12
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• 1990

Isolates of Penicillium expansum with reduced pathogenicity were arbitrarily selected among benomyl-resistant isolates in order to investigate relationship of their pectolytic enzyme acitivity with pathogenicity. In artificial medium, strongly pathogenic isolate $S_1$ and weakly pathogenic isolate $R_2$ produced considerable amonts of endo-polymethylgalacturonase, endo-polygalacturonase, pectin methyl-trans-eliminase, and polygalacturonate-trans-eliminase. No marked difference in enzyme activities was observed between two isolates. In apple medium, the activities of endo-polymethylgalacturonase and endo-polygalacturonase of isolate $S_1$ were over 6 times higher than those of isolate $R_2$. But pectin methyl-trans-eliminase and polygalacturonate-trans-­eliminase did not show a great difference. Activities of endo-polymethylgalacturonase and endo­polygalacturonase precipitated at 80-95% saturation of ammonium sulfate were highest, and addition of these enzyme solutions increased pathogenicity of weakly pathogenic isolates $R_{1-4}$.

• Applied Biological Chemistry
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• v.37 no.5
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• pp.356-360
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• 1994

The optimum pH and temperature for endo-polygalacturonase activity from Jujube were 5.0 and $50^{\circ}C$. The range of its stability to pH was 4.0 to 5.0. The enzyme was inactivated about 35% by treatment at $70^{\circ}C$ for 1 hr. It was found that $Ag^+$, $Zn^{++}$ and $Mg^{++}$ increased the enzyme activity. In contrast, $Ba^{++}$, $Hg^{++}$, $Pb^{++}$, $Ca^{++}$, $Mn^{++}$, $Cu^{++}$, $Fe^{+++}$, $Na^+$ and $K^+$ decreased it. The enzyme was inactivated by treatment with maleic anhydride, iodine and 2,4-dinitrophenol. The results indicate that active site is a imidazole group on the enzyme.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.5
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• pp.796-802
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• 1995

Oyijangachi, a traditional Korean brinded cucumber, was prepared by brinning the cucumbers in five different solutions for 48 hrs and then, was dipped into dipping sources(Kochujang, Doenjang and Ganjang) for 30 days of aging. Firmness, calcium content and enzyme activities(pectinesterase and polygalacturonase) changes were measured among the cucumbers which were treated by five different solutions during aging. The firmness of Kochujang Oyijangachi were the lowest after 10 days of aging for all from the five brining solutions because of "hollow phenomena" of cucumbers. Calcium contents of cucumbers after dipping into the five solutiosn increased as calcium content of the solutions increased and also increased when the cucumbers dipped into the dipping bases(Kochujang, Doenjang and Ganjang) because of calcium migration from the dipping sources into the cucumbers during aging. The calcium contents of the three dipping bases were ranged from 70mg% to 120mg% of Ca. The activity of polygalacturonase in the Oyijangachi decreased generally during aging and decreased rapidly during initial 5 days of aging. The activity of pectinesterase of cucumbers treated with 12% salts solutions(treatment 3, 4 and 5) were higher than those of cucumbers treated with 6% salts solutions(treatment 1 and 2).

• The Korean Journal of Mycology
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• v.22 no.4
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• pp.298-308
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• 1994

The properties of polygalacturonase by Ganoderma lucidum in liquid culture were investigated. The enzyme was composed of an endo- and an exo-polygalacturonase. The endo- and exo-polygalacturonase were purified approximately 56 and 9.2-fold, respectively, through ammonium sulfate fractionation, gel filtration on Biogel P-100, anion exchange chromatography on DEAE-cellulose, gel chromatography on Sephadex G-150 and re-gel chromatography on Sephadex G-150. The endo- and exo-polygalacturonase had higher affinity for apple pectin than for citrus pectin or pectic acid. The Km values of the endo- and exo-polygalacturonase for apple pectin, determined on the Lineweaver-Burk plot, were 1.44 and 10.6 mg $ml^{-1}$ for apple pectin, respectively. Purified endo-polygalacturonase was found to be homogeneous electrophoretically and had a molecular weight of 54,000 estimated on SDS polyacrylamide gel. The optimal pH for the activity of the enzymes was 4.0. The endo- and exo-polygalacturonase were stable in the pH range of 4.0 to 6.0 and 3.5 to 5.5, respectively. The optimal temperatures of the endo- and exo-polygalacturonase were 40 and $60^{\circ}C$, respectively. The exo-polygalacturonase was more resistant to heat than the endo-polygalacturonase, requiring heating for 40 min at $80^{\circ}C$ for complete inactivation. The activity of the endo-polygalacturonase was increased by $Ca^{++}$ and $Mn^{++}\;ions$, while that of the exo-polygalacturonase was increased by $Ca^{++}\;ion$ only, and was not affected by $Mn^{++}\;ion$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.5
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• pp.611-616
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• 1993

This study was carried out to investigate change in the polygalacturonase and ${\beta}-galactosidase$ activities, pectins, cell wall structure of persimmon fruit during ripening and softening. Polygalacturonase and ${\beta}-galactosidase$ activities were not detected at turning stage. However polygalacturonase activities of mature and soft persimmon fruits were 55.01 and 206.70units/100g-fresh weight(fr. wt.), respectively. ${\beta}-Galactosidase$ activities of mature and soft persimmon fruits were 21.79 and 380.23unit/100g-fr. wt. respectively. The contents of total and insoluble pectins increased during maturation but decreased during softening. The content of water-soluble pectin increased during maturation and softening. The intercellular space was in larged during ripening, and middle lamella was degraded in mature persimmon fruit, and the cells of soft persimmon fruit were separated each other.