• Journal of Ginseng Research
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• v.14 no.1
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• pp.21-26
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• 1990

The chemical composition and stabilities of the purified ginseng invertase were investigated. The purified enzyme was found to be a glycoprotein composed of 80.2% protein and 19.7% total sugar. The protein component of the enzyme was composed of acidic amino acid (9.3%), basic amino acid (48.9%), nonpolar amino acid (21.4%), polar amino acid (20.4%) and 6.1% S-containing amino acid. It showed especially high contents of histidine and serine. The enzyme was inactivated almost completely by the treatment with some proteases (papain, pepsin. trypsin, pancreatin and microbial alkaline pretense) and protein denatllrants (8M urea and 6M guanidine-HC1), bolt not with glyrosidase (${\alpha}$-amylase, ${\beta}$-amylase. glcoamylese and cellullase). btonosaccharides sllch as glilrose, fructose, galactose and mannose did not exert any influence on the enzyme activity. The activity of the enzyme was inhibited by Ag+, Mn2+, Hg2+, Zn2+ and Al3+, whereas Ca2+, Mg2+, Ba2+ and Fe3+ gave rather activating effects on the enzyme activity. The enzyme was relatively stable in the VH range of VH 6 and 8, and at the temperatures below 35$^{\circ}C$.

• Journal of Plant Biology
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• v.34 no.2
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• pp.113-119
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• 1991

The contents of reducing sugar, sucrose, starch and fructose-2,6-bisphosphate (F-Z,$6-P_2$) in relation to the activities of amylase, invertase and fructose-1,6-bisphosphatase (FBPase) were investigated from the leaves of rice (Oryza sativa L. cv. Samjin) seedlings grown at $4^{\circ}C$ for 3 days_ In the seedlings, the contents of reducing sugar and sucrose were increased, but soluble and insoluble starch were declined. Under this condition, amylase activity was increased. but acid invertase activity was declined and alkaline invertase activity was not changed. Cytosolic and stromal FBPase activities were increased. But F-2,$6-P_2$ content was declined. It seemed that the increase of reducing sugar content might be due to the increased activity of amylase and the increase of sucrose content might be related to the increased activity of cytosolic FBPase, reduced content of F-Z,$6-P_2$ and reduced rate of hydrolysis of sucrose during the cold treatment. These results suggested that the changes in carbohydrate rnetabolim of rice seedlings under low temperature reflect one of the protection mechanism to the low temperature during the cold treatment.atment.

• Journal of Plant Biology
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• v.38 no.3
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• pp.251-258
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• 1995

The soluble acid 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 to apparent homogeneity by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, Concanavalin (Con) A affinity and Sephacryl S-300 chromatography. The overall purification was about 148-fold with a yield of about 15%. The finally purified enzyme exhibited a specific activity of about 139 $\mu$mol of glucose produced mg-1 protein min-1 at pH 5.0 and appeared to be a single protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and nondenaturing PAGE. The enzyme had the native molecular weight of 70 kD and subunit molecular weight of 70 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme was composed of a monomeric protein. On the other hand, the enzyme appeared to be a glycoprotein containing N-linked high mannose oligosaccharide chain on the basis of its ability to bind to the immobilized C on A. The enzyme had a Km for sucrose of 1.8 mM at pH 5.0 and maximum activity around pH 5.0. The enzyme showed highest enzyme activity with sucrose as substrate, but the activity was slightly measured with raffinose and cellobise. No activity was measured with maltose and lactose. These results indicate the soluble acid invertase is a $\beta$-fructofuranosidase.

• KSBB Journal
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• v.25 no.1
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• pp.79-84
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• 2010

In the present study, we isolated a new bacterial strain producing invertase (EC 3.2.1.26) and determined optimized culture condition in flask culture. The strain was identified as Bacilus flexus determined by the 16S rDNA sequencing method. The invertase was produced only in the sucrose medium as the sole carbon source. Potassium nitrate was an adequate nitrogen source for enzyme production, whereas meat peptone showed the highest bacterial growth. Enzyme production was increased about 2-fold when $MgSO_4\cdot7H_2O$ was supplemented to the growth media. The optimum temperature was found to be $30^{\circ}C$ for both enzyme production and bacterial growth. Invertase exhibited pH optima in the range 5.0-6.0 and have a temperature optimum at $40^{\circ}C$, similarly to other invertases found from different microbial sources. Several mineral ions (K and Fe) stimulated the invertase activity, whereas some bioelements (Ag, Mg, and Mn) inhibited enzyme activity. Under the optimized culture condition, the maximum enzyme production (over 250 units/mL) was achieved at 20 h. To the best of our knowledge, this is the first time to report on invertase production by Bacilus flexus.

• Korean Journal of Food Science and Technology
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• v.5 no.3
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• pp.157-162
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• 1973

Mode of action study of irradiation was performed with potato tuber slices, $1mm{\times}1.5cm,$ aged on moist filter paper under aseptic technique. The time courses of invertase activity, nucleic acids and respiratory activity were determined, and sensitivities of these three processes to ionizing radiation were measured. None of those processes was severely inhibited by the dosage suppressing cell division. The result of $^3H-thymidine$ incorporation suggests that the reaction site of ionizing radiation might be existent during mitosis or $G_2$ period.

• Journal of Life Science
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• v.25 no.9
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• pp.1021-1026
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• 2015

Invertase (β-D-fructosfuranosidase, EC 3.2.1.26) catalyzes the hydrolysis of sucrose into D-glucose and D-fructose. Three biochemical subgroups of invertases have been investigated in plants: vacuolar (soluble acid), cytoplasmic (soluble alkaline), and cell wall-bound (insoluble acid) invertases. An isoform of neutral invertase was purified from pea seedlings (Pisum sativum L.) and treated with gibberellic acid (GA) by sequential procedures consisting of ammonium sulfate precipitation, ion-exchange chromatography, absorption chromatography, and reactive green-19 affinity chromatography. The results of the overall insoluble invertase purification were a 430-fold increase. The purified neutral invertase was not glycosylated and had an optimum pH between neutral and alkaline (pH 6.8-7.5). It was inhibited by Tris, as well as by heavy metals, such as Hg²⁺ and Cu²⁺. Typical Michaelis–Menten kinetics were observed when the activity of the purified invertase was measured, with sucrose concentrations up to 100 mM. The K_m and V_max values were 12.95 mM and 2.98 U/min, respectively. The molecular mass was around 20 kDa. The sucrose-cleaving enzyme activity of this enzyme is similar to that of sucrose synthase and fructosyltransferase, but its biochemical characteristics are different from those of sucrose synthase and fructosyltransferase. Based on this biochemical characterization and existing knowledge, neutral INV is an invertase isoform in plants.

• Journal of Environmental Science International
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• v.4 no.4
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• pp.21-21
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• 1995

The effects of plant hormones (NAA, $GA_3$ and BA) and light qualities (white, red, green and blue light) on the changes of reducing sugar contents and invertase isozyme activities in leaves of maize (Zea mars L.) and mung bean (Phseolw radiatus L.) seedlings were investigated. NAA accelerated the increase of reducing sugar contents and invertase isozyme activities, on the contrary, $GA_3$ had little effect in the accumulation of reducing sugar and in the increase of enzyme activities from the leaves of maize and mung bean seedlings. On the other hand, BA accelerated an increase in the activities of the invertase isozyme from the leaves of mung bean seedlings whereas it had little effect in the increase of the enzyme activities from those of maize seedlings. The accumulation of reducing sugar in leaves of both seedlings was promoted by red light irradiation compared to white light irradiation, while the activities of the enzyme were little affected by various light Qualities. In the simultaneous applications of plant hormone and light quality, NAA with white light was very effective in the increase of reducing sugar contents and the enzyme activities from the leaves of mung bean seedlings, whereas NAA application with blue light showed a prominent enhancement in the reducing sugar contents and the enzyme activities from those of maize seedlings. These results suggest that plant hormone, particularly NAA, may be a more important factor than various light Qualities in the stimulation of invertase activity.

• Journal of Environmental Science International
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• v.4 no.4
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• pp.323-333
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• 1995

The effects of plant hormones (NAA, $GA_3$ and BA) and light qualities (white, red, green and blue light) on the changes of reducing sugar contents and invertase isozyme activities in leaves of maize (Zea mars L.) and mung bean (Phseolw radiatus L.) seedlings were investigated. NAA accelerated the increase of reducing sugar contents and invertase isozyme activities, on the contrary, $GA_3$ had little effect in the accumulation of reducing sugar and in the increase of enzyme activities from the leaves of maize and mung bean seedlings. On the other hand, BA accelerated an increase in the activities of the invertase isozyme from the leaves of mung bean seedlings whereas it had little effect in the increase of the enzyme activities from those of maize seedlings. The accumulation of reducing sugar in leaves of both seedlings was promoted by red light irradiation compared to white light irradiation, while the activities of the enzyme were little affected by various light Qualities. In the simultaneous applications of plant hormone and light quality, NAA with white light was very effective in the increase of reducing sugar contents and the enzyme activities from the leaves of mung bean seedlings, whereas NAA application with blue light showed a prominent enhancement in the reducing sugar contents and the enzyme activities from those of maize seedlings. These results suggest that plant hormone, particularly NAA, may be a more important factor than various light Qualities in the stimulation of invertase activity.

• Microbiology and Biotechnology Letters
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• v.25 no.3
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• pp.258-265
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• 1997

The effects of medium pH and culture temperature on the expression and secretion of inulinase and invertase were investigated with recombinant Saccharomyces cerevisiae cells. These cells were obtained by transformation of 2$\mu$-based plasmids pYI10 and pYS10 which contain Kluyveromyces marxianus inulinase gene (INU1A) and S. cerevisiae invertase gene (SUC2), respectively, in the downstream of GAL1 promoter. The expression level and localization of inulinase and invertase were not affected significantly by the initial medium pH: secretion efficiencies of inulinase and invertase into the medium were about 90% and 60%, respectively, in the pH ranges of 4.0 to 6.5. However, the expression and secretion of both enzymes were strongly dependent on the culture temperature. The highest expression (7.7 units/mL) and secretion (6.7 units/mL) of inulinase were observed at 28$\circ$C and 30$\circ$C. As a consequence of decreased localization of inulinase in the periplasmic space, the secretion efficiency increased from 68% at 20$\circ$C, to 95% at 35$\circ$C,. The total expression level and secretion efficiency of invertase increased from 19 units/mL and 55% at 20$\circ$C to 25 units/mL and 68% at 35$\circ$C, respectively. Irrespective of the culture temperature, the invertase activity in the cellular fraction (periplasmic space and cytoplasmic fractions) was kept constant at around 33-45%.

• 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.