• KSBB Journal
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• v.5 no.2
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• pp.107-112
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• 1990

The kinetic characteristics of an invertase immobilized covalently on porous silica have been appraised for the applicability of porous silica to immobilization supports of enzymes. The invertase was covalently bound with glutaraldehyde on 3-aminopropyltriethoxy-silane-activated porous silica to give a maximum loading of 120mg invertase per 1 gram of dry silica and 26.9 to 70.2% retention of original activity. The porous structure of silica seems to be suitable for enzyme immobilization, judging from the observed results of high immobilization capacity and comparably satisfactory retention of enzyme activity.

• Korean Journal of Food Science and Technology
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• v.12 no.3
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• pp.176-181
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• 1980

Yeast invertase was immobilized on the 2 kinds of matrices : one is an indirectly coupled enzyme to the cyanogen bromide activated Sepharose by using ${\omega}-aminohexyl$ group as an extension arm, and the other is a tightly adsorbed enzyme on the modified hydrophobic cellulose derivative which has a phenoxyacetyl group as a linkage. The enzyme preparation coupled on Sepharose retained 26.0% of the original activity against sucrose as a substrate, while the preparation immobilized on phenoxyacetyl cellulose retained 72.9% . The immobilized invertase preparation on ${\omega}-aminohexyl$ Sepharose showed the optimal pH 4.5, optimal temperature $60^{\circ}C$, activation energy $5,941\;cal/mole{\cdot}deg$ and Km' 22.2 mM against sucrose, while the preparation adsorbed on phenoxyacetyl cellulose showed the optimal pH 4.0, optimal temperature $60^{\circ}C$, activation energy $7,769\;cal/mole{\cdot}deg$ and Km' 69.9 mM.

• Korean Journal of Food Science and Technology
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• v.14 no.1
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• pp.1-5
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• 1982

An invertase from Korean ginseng (Panax ginseng C. A. Mayer) was purified by means of DEAE-cellulose column chromatography and gel-filtration through Sephadex G-75. The homogeneity of the purified invertase was proved by polyacrylamide gel disc electrophoresis. The enzyme was separated into two subunits by SDS-polyacrylamide gel electrophoresis, showing its molecular weights as 48,000. The enzyme preparation showed a characteristic protein UV-spectra.

• Journal of Applied Biological Chemistry
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• v.50 no.4
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• pp.196-201
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• 2007

An intracellular invertase was purified to homogeneity from the cell extract of an alkalophilic and thermophilic Bacillus sp. TA-11, which was classified as a new species belonging to Bacillus cereus based on chemotaxanomic and phylogenetic analyses. The purified enzyme with a recovery of 26.6% was determined to be a monomeric protein with a molecular weight of 23 kDa by SDS-PAGE and 26 kDa by gel filtration. The maximum enzyme activity was observed at pH 7.0 and $50^{\circ}C$, and the purified enzyme was stable at the pH range of 5.0 to 8.0 and below $60^{\circ}C$. $K_m$ and $V_{max}$ values of the enzyme for sucrose were 370 mM and 3.0 ${\mu}M$ per min, respectively. The enzyme activity was significantly inhibited by bivalent metal ions ($Hg^{2+}$, $Cd^{2+}$ and $Cu^{2+}$) and sugars (glucose and fructose).

• Journal of the Korea Safety Management & Science
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• v.1 no.1
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• pp.259-272
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• 1999

In order to enhance the selectivity, productivity and yield of methyl fructoside, which was synthesized by enzymatic glycosylation of sucrose and methanol solution, controlling of surface property of solid support using different immobilization procedures optimized microenvironment of immobilized invertase. Silanization and polyethylene imine coating methods were adopted to give a hydrophobic and hydrophilic environment of immobilized invertase. As a result, polyethyleneimine coating method gave higher loading of enzyme, effective activity, and relative activity than silanization method, because it brought on increasing the functional density of amino group and enhancing the conservation of activity by regulating of hydrophilicity. And then, hydrophilic environment was possible to restraint the assessing of methyl fructoside molecule, which was more hydrophobic than sucrose, fructose, and glucose molecule in the reaction mixture, into .the active site of immobilizedinvertase. Consequently, hydrophilic microenvironment of immobilized invertase by polyethyleneimine coating obtained higher yield and productivity with increasing conversion than silanized and native invertase. Thus, this procedure optimized the microenvironment of immobilized invertase suitable for the enzymatic synthesis of methyl fructoside.

• Korean Journal of Environmental Biology
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• v.27 no.4
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• pp.406-413
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• 2009

The enzyme invertase contributes to sugar unloading, pathogen defense, differentiation and development in plants. We cloned the complete cDNA of a soluble acid invertase from pea seedlings (Pisum sativum) via RT-PCR and the rapid amplification of the cDNA end (RACE) technique. The full-length cDNA of the soluble pea invertase comprised 2237 bp and contained a complete open reading frame encoding 647 amino acids. The deduced amino acid sequence showed high homology to soluble acid invertases from various plants. Northern blot analysis demonstrated the soluble acid invertase gene of P. sativum was strongly expressed in sink organs such as shoot tips and root tips, and induced by abscisic acid, gibberellic acid and jasmonic acid in shoots. Especially, gibberellic acid enhanced the gene expression of the soluble acid invertase in a time-dependent manner. This study presents that the gene expression patterns of a soluble acid invertase from pea are strongly consistent with the suggestion that individual invertase gene product has different functions in the growing plant.

• 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.

• Applied Biological Chemistry
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• v.30 no.2
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• pp.169-178
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• 1987

The extracellular and intracellular inulases from Kluyveromyces marxianus were purified and characterized. The maximum production of both inulases was achieved at stationary phase in a pH-controlled medium at pH 5 with yeast nitrogen base as organic nitrogen source. Each enzyme was concentrated by tannic acid precipitation and separated into two fractions by DEAF-cellulose chromatography. Electrophoretic analysis showed that the four fractions had three glycoprotein bards each. Only main glycoprotein band, however, had both inulase and invertase activities. There were no significant differences between two enzymes in the optimum pH and temperature. But the intracellular inulases had higher heat stability and less affinity toward inulin than the extracellular enzymes do. All the purified enzymes were considered to be exo-inulases using hydrolyzate analysis with TLC.

• Journal of Plant Biology
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• v.35 no.1
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• pp.91-95
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• 1992

Changes of contents of reducing sugar and sucrose and activities of sucrose-phosphate synthase, sucrose synthease and invertase from the leaves of barley (Hordeum vulgare L. cv. Chalssal) seedlings grown at $4^{\circ}C$ were investigated, and the property of acid invertase were also examined. In the seedlings grown at $4^{\circ}C$ for 3 days, the contents of reducing sugar and sucrose were increased to 1.3 and 2.4 times, respectively. Activity of acid invertase was decreased markedly by cold treatment while the activities of sucrosephosphate synthase, sucrose synthase, and alkaline invertase were not changed. In acid phosphatase purified partially by ammonium sulfate fractionation and DEAE-Sephacel column chromatography, the $K_m$ value for sucrose was 9.5 mM and the optimum pH and temperature was 5.5 and $35^{\circ}C$ respectively. This enzyme was supposed to be ${\beta}-fructosidase$ by studies on the substrate specificity and the molecular weight was estimated to be 63 Kd by Sephadex G-200 gel chromatography.graphy.

• 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.