• 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.

• Microbiology and Biotechnology Letters
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• v.20 no.4
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• pp.417-421
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• 1992

The expression pattern of the cloned SUC2 gene in recombinant Saccharomyces cerevisiae was investigated in a two-stage culture. The recombinant yeast grown in a glucose medium where the SUC2 gene was repressed was harvested and then resuspended in a sucrose medium to induce invertase expression. The maximum activity of 10 units was obtained in a medium containing 2 $g/\ell$ sucrose as a carbon source at $30^{\circ}C$ . The oscillatory behavior of invertase activity in response to glucose concentrations in the second stage was observed. This effect can be attributed to a series of events: invertase expression from the SUC2 gene. sucrose hydrolysis to glucose and fructose by invertase, SUC2 repression by high glucose concentration, invertase induction as a result of depletion of glucose used for the yeast growth. The invertase activity was increased by 72.5% when growth temperature changed from $30^{\circ}C$: to $35^{\circ}C$.

• The Korean Journal of Food And Nutrition
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• v.15 no.2
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• pp.126-130
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• 2002

Regulation of invertase biosynthesis was studied in thermophilic and alkalophilic Bacillus sp. TA-11. Biosynthesis of the invertase was effectively induced in the presence of 10 mM sucrose for 180 min. Glucose repressed the invertase induction by sucrose and as late as addition time of glucose, the invertase formation was increased, indicating that glucose repression was occurred by inducer exclusion. Catabolite repression was reduced a little by the addition of cAMP for 180 min of induction.

• Microbiology and Biotechnology Letters
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• v.20 no.6
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• pp.625-629
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• 1992

This work was carried out to study physiological characteristics of Rhodosporidium toru[oides cells having two different mating types. The mating type A produces internal. cell wall-bound, and external invertases while type a produces only two invertases except external invertase. Comparing their characteristics after partial purification of internal invertases from both mating type cells, invertase from type a has decreased 15% of invertase activity only by $Mn^{2+}$ I while invertase from type A has been increased 11% of invertase activity by $Zn^{2+}$ and decreased 15% of invertase activity by $Mn^{2+}$ On the effect of enzyme inhibitor, invertase of type a was inhibited from 12% to 57% by 2-mercaptoethanol, sodium dodecyl sulfate, phenol. but invertase of type A was slightly inhibited only by phenol. The thermal stability of both invertases has showed steep inactivation at above $80^{\circ}C$ and their optimal temperatures were similar at $60^{\circ}C$ . Invertase from type A showed stability only on condition of acid from pH 3 to 6 and its opimal pH was 5.0, while invertase from type a showed stability at the wide range of pH 3-10 and its optimal pH was 4.0. And the $K_m$ values of invertases from type A and type a were $2.5{\times}10^3$M and$3.4{\times}10^3$M, respectively.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.313-320
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• 1989

Rhodotorula glutinis K-24 was found to produce internal, cell wall bound, and external invertase. Internal invertase was purified by column chromatographies on DEAE-Sephadex A-50, Sp-sephadex C-50, gel filtration on Sephadex G-200 and isoelectric focusing. Cell wall bound invertase was partially purified by the following procedures; column chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. Optimum pH and temperature for enzymatic activities of internal and cell wall bound invertase were pH 3.0 and 6$0^{\circ}C$, respectively. Both enzymes were inhibited by HgC1$_2$, AgNO$_3$, MnSO$_4$, and sodium dodecylsulfate. The molecular weights of internal and cell wall bound invertases were estimated to be 310,000 and 61,000, respectively. Other physicochemical properties of the both enzymes were similar.

• Journal of Life Science
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• v.15 no.3 s.70
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• pp.499-504
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• 2005

This experiment was conducted to identify the effect of several plant growth retardants on growth of Sedirea japonica seedlings cultured in vitro and their changes of invertase activities. When seedlings of Sedirea japonica were treated with ancymidol and paclobutrazol, as the concentrations were increased, leaf length was gradually shortened and leaf width became wider than that of control. On the other hand, root length was shorter, but the number of root and the root's diameters were greatly increased, compared with control. In 0.05mg/L uniconazole, growth of leaf and root were enhanced, compared with the control and higher concentrations of uniconazole. As concentration of each growth retardants was increased, leaf shape became round and smaller. Both soluble acid invertase activity and soluble alkaline invertase activity in leaf were decreased in higher concentrations of each growth retardant, but those of the root were contrary to those of the leaf. To confirm the estimated invertase activities, starch content of leaf was higher in low concentration treatments in each growth retardant, but in the root was contrary to content that of the leaf.

• The Journal of Natural Sciences
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• v.17 no.1
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• pp.103-111
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• 2006

Regulation of invertase biosynthesis was studied with the E. coil harboring recombinant plasmid, pYC17. Biosynthesis of invertase in the recombinant E. coil was effectively induced in the presence of 30mM of sucrose for 3h. Glucose also repressed the invertase induction in the recombinant E. coil at 10 mM, lower than that of parent strain (30 mM).

• The Journal of Natural Sciences
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• v.18 no.1
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• pp.29-38
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• 2007

Regulation of invertase biosynthesis was studied with alkalophilic and thermophilic Bacillus cereus TA-11. Biosynthesis of invertase in Bacillus cereus TA-11 was effectively induced in the presence of 10 mM of sucrose for 180 min and 25 mM of raffinose for 90 min, respectively. Glucose repressed the invertase induction by sucrose and as late addition time of glucose, invertase formation was increased, indicating that glucose repression was occurred by inducer exclusion. Catabolite repression was not reduced by the addition of cAMP for 180 min of induction.

• Microbiology and Biotechnology Letters
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• v.20 no.3
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• pp.348-354
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• 1992

In order to improve the productivity of invertase by recombinant Saccharomyces cerevisiae containing SUC2 gene, the effect of amino acids and dissolved oxygen concentration on the gene expression was investigated. Optimal concentrations of leucine and histidine for cell growth and cloned gene expression were 0.03 gig and 0.04 gig, respectively, expressed as the ratio of amino acid/glucose. The lack or excess of leucine and histidine has inhibitory effect on cell growth and invertase expression. In batch culture, the less aeration was, the higher invertase activity was. In continuous culture at a dilution rate of 0.09 h 1 with controlled dissolved oxygen tension, invertase activity increased dramatically at DOT levels below 5% air saturation, and a maximum activity of 215.54 KUlg cell was obtained under unaerated condition.

• KSBB Journal
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• v.13 no.3
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• pp.308-311
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• 1998

A novel process was developed to simultaneously produce invertase and yeast extract from baker's yeast using ultrafiltration (UF) and microfiltration (MF) membrane processing. After the extraction of invertase under the optimal condition obtained in this study, invertase was separated from yeast cells using a hollow fiber membrane with a pore size of 0.1 $\mu\textrm{m}$. The resulting permeate containing invertase was concentrated using a hollow fiber membrane with a nominal molecular weight cut-off of 30 kDa. The yeast cell and permeate solutions, which were obtained after MF and UF membrane processing, respectively, were mixed together, and the autolysis was performed at 50$^{\circ}C$ in the presence of 5% (w/v) ethanol and 1% (w/v) NaCl. As a result, the yeast extract and invertase could be simultaneously produced from baker's yeast by this novel process.