• The Korean Journal of Food And Nutrition
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• v.5 no.2
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• pp.144-149
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• 1992

Invertase was extracted from Korean ginseng(Panax ginseng C. A. Meyer) leaf with deionized water, and then prepared by ammonium sulfate(0.4~0.6 Sat.) fractionation, the enzymological properties of the invertase were investigated, and the results obtained were as follows. The optimum pH and temperature of the enzyme were pH 6.0 and 4$0^{\circ}C$ respectively. The enzyme was stable in the pH range of pH 6.0 to 8.0, and at the temperature below 4$0^{\circ}C$. The enzyme was inactivated completely by the treatment with some proteases(pepsin, trypsin, papain and ficin) and protein denaturants(8M urea and 6M guanidine-HCI), but not with glycosidases (a-amylase, $\beta$-amylase and glucoamylase). The enzyme catalyzed specifically the hydrolization of the $\beta$-fructofuranosides such as sucrose and inulin.

• Journal of Plant Biology
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• v.38 no.4
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• pp.349-357
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• 1995

The alkaline invertase ($\beta$-D-fructofuranoside fructohydrolase, EC 3.2.1.26) was isolated and characterized from the hypocotyls of mung bean (Phaseolus radiatus L.). The enzyme was purified by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, 1st Sephadex G-200, DEAE-Sephadex A50 and 2nd Sephadex G-200 chromatography. The overall purification was about 77-fold with a yield of about 6%. The finally purified enzyme exhibited a specific activity of about 48 $\mu$mol of glucose produced mg-1 protein min-1 at pH 7.0 and appeared to be a single protein by nondenaturing polyacrylamide gel electrophoresis (PAGE). The enzyme had the native molecular weight of 450 kD and subunits molecular weight of 63 kD and 38 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme is a heteromultimeric protein composed of two types of subunits. On the other hand, the enzyme appeared to be not a glycoprotein according to the results of Con A chromatography and glycoprotein staining. The enzyme had a Km for sucrose of 19.7 mM at pH 7.0 and maximum activity around pH 7.5. The enzyme was most active with sucrose as substrate, compared to raffinose, cellobiose, maltose and lactose. These results indicate the alkaline invertase is a $\beta$-fructofuranosidase.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.6
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• pp.725-730
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• 1992

The internal invertase was purified from cell free extract of Rhodosporidium toruloides IFO 0559-M-919 by acid precipitation, ion-exchange chromatography and gel filtration to the unique enzyme protein on disc electrophoresis. We have found out that molecular weight of purified internal invertase was 90,000 by gel filtration and the purified enzyme was protein with 4 homogeneous subunits appearing as single band of 22,000daltons on SDS-polyacrylamide gel electrophoresis.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.6
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• pp.577-582
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• 1990

Production and properties of invertase from Aspergillus niger were investigated. Inulin and sucrose were best carbon source and yeast extract was most suitable for the production of the enzyme among tested carbon and nitrogen sources. The enzyme among tested carbon and nitrogen sources. The enzyme was maximally produced by cultivating the organism at medium of pH 4.5 and temperature of 3$0^{\circ}C$ The optimum pH and temperature for the enzyme activity were pH 5.0 and temperature of 5$0^{\circ}C$, respectively. Among tested metal ions. Hg++, Cu++ and Ag+ ions Inhibited the enzyme activity drastically.

• The Korean Journal of Food And Nutrition
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• v.2 no.2
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• pp.14-20
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• 1989

A strain of Saccharomyces cerevisiae BY-366 was isolated to produce a strong sucrose-hydrolyzing enzyme. After entrapment of yeast cell invertase with alginate, enzymatic properties of immobilized cells were investigated. The results are as follows. 1. The optimum pH of invertase in immobilized cells and non- immobilized cells was 6.0 and 5.0, and pH stability of invertase in immobilized cells and non- immobilized cells was 6.0 and 5.0, respectively. 2 Activation energy of immobilized cells was 4.7 kcal/mol. 3 The immobilized preparation exhibited high resistance to heat and urea Induced denaturation. 4, The bead size less than 2 mm in diameter was desirable. 5. In spite of repeated use, the enzyme activity of immobilized cells was inhibited slightly in batch reaction, and a small column of the immobilized preparation could hydrolyze relatively high concentration of sucrose almost quantitatively to more than 6 days.

• Korean Journal of Food Science and Technology
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• v.12 no.1
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• pp.1-5
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• 1980

Crude invertase was obtained from the water extracts of Korean ginseng, Panax ginseng C. A. Meyer, by fractionation with $0.8{\sim}1.0$ saturation of ammonium sulfate. The properties of the crude invertase were as follows: Crude invertase was stable in the pH range between 5 and 9, and at the temperature below $35^{\circ}C$. Crude invertase showed the optimum pH at 5.0 and the optimum temperature at $50^{\circ}C$. The activity of the crude invertase was inhibited by $Ag^{+}\;Mn^{+}\;Hg^{+}\;Zn^{+},\;and\;Rb^{+}$, while $Ca^{+}\;Cu^{+},\;and\;Fe^{3+}$ demonstrated remarkable increasing effects on the enzyme activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.5
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• pp.429-433
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• 1990

Production and properties of invertase from. Aspergillus niger were investigated. Inuli and sucrose were best carbon source and yeast extract was most suitable for the production of the enzyme among tested carbon and nitrogen sources. The enzyme was maximally produced by cultivating the organism at medium of pH 4.5 and temperature of 3$0^{\circ}C$ The optimum pH and temperature for the enzyme activity were pH 5.0 and temperature of 5$0^{\circ}C$ respectively Among tested metal ions Hg2+ Cu2+ and Ag+ ions inhibited the enzyme activity drastically.

• Mycobiology
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• v.30 no.3
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• pp.170-174
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• 2002

A total of twenty-nine species and one species variety belonging to 12 genera was isolated from 30 samples of molasses on 1% glucose(10 genera, 22 species and 1 variety) and 50% sucrose(7, 21 and 1) Czapek's agar at $25^{\circ}C$ media. Aspergillus, Mucor, Mycosphaerella and Penicillium were the most common genera on the two types of media. From the above genera, the most prevalent species were: Aspergillus flavus, A. fumigatus, A. niger, Mycosphaerella tassiana, Penicillium chrysogenum, P. oxalicum and P. purpurogenum. Also, some species were only isolated on 50% sucrose such as Eurotium amstelodami, E. chevalieri, E. repens, Humicola fuscoatra, Penicillium aurantiogriseum and P. puberulum. About 65 fungal isolates isolated from 50% sucrose agar were tested for their ability to produce invertase enzyme in liquid medium and 93.8% of the isolates could produce this enzyme. From the positive isolates, 32 showed high invertase activity, 21 had moderate activity and the remaining 8 isolates were of weak activity. Sixty isolates of Aspergillus, Emericella, Eurotium, Mycosphaerella and Penicillium from the preceding study were screened for the presence of their respective mycotoxins. Larva of brine shrimp(Artema sauna L.) were used for toxicity test of the fungal crude extracts. Three isolates out of 60 tested were toxic. Using thin-layer chromatographic technique, 5 different known mycotoxin were detected aflatoxins : B1, B2, G1, G2 and citrinin.

• Current Research on Agriculture and Life Sciences
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• v.6
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• pp.129-135
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• 1988

The changes of sugar content and invertase activity during maturation of plum fruits, and properties of the enzyme were investigated in this study. The soluble sugars in plum fruits were mainly sucrose, glucose and fructose. The sucrose content in the fruit increased slowly at the early stage of maturation and then decreased slightly. At the final stage, the sucrose content increased remarkably with maturation. The contents of glucose and fructose increased slowly at the early stage of maturation following decrement at middle stage. At the final stage, glucose content decreased continuously while fructose content increased again following decrement. Invertase activity in the fruit increased during maturation showing maximum at the onset of color change and after that, decreased remarkably. The optimum pH and temperature of invertase activity were pH 5.0 and $65^{\circ}C$, respectively. The enzyme was most stable at pH 5.0 and retained 75% of its activity after incubation at $70^{\circ}C$ for 15min. The enzyme was activated by $Cu^{{+}{+}}$, $Ca^{{+}{+}}$, but inhibited by $Hg^{{+}{+}}$ remarkably.

• Journal of the Korean Wood Science and Technology
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• v.30 no.3
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• pp.12-17
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• 2002

The extracellular invertase (EC 3.2.1.26) (Candida utilis) preparation was obtained from the liquid medium after desalting and freeze drying. This prepared enzyme was used for the comparative purification on 4 activated matrices by liquid column affinity chromatography method. In this method there were used controlled porous glass (CPG) silanized covalently activated by keratin, silanized silica gel and silica gel covalently covered by keratin. It was found that the invertase purification process was better using both CPG matrices (silanized CPG and keratin activated CPG) than these with two silica gel supports. Also the elution coefficient of the invertase from the two CPG columns was about 93 to 94%. Two silica gel supports found to be superior in terms of purification efficiency. The invertase purification process was confirmed by PAGE electrophoresis.