• Korean Journal of Food Science and Technology
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• v.28 no.2
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• pp.273-278
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• 1996

The research was undertaken to characterize the reaction mode of transglucosidase (TG) from Aspergillus niger for the production of isomaltooligosaccharides such as isomaltose, panose and isomaltotriose. TG hydrolyzed maltose to glucose units and produced panose and glucose by transglucosylation. TG hydrolyzed panose to maltose and glucose when panose was used as an initial substrate. The reaction patterns of products when isomaltose, isomaltotriose or isomaltotetraose were used as substrates were different from the case when maltose was used as a substrate. Maltotriose and maltose showed the same formation pattern of products. TG also produced isomaltooligosaccharides from maltooligosaccharides. The production of panote by TG from maltose was mathematically described by Michaelis-Menten kinetics. The kinetic constants, $V_{max}$ (the maximum velocity) and $K_m$ (Michaelis constant), were estimated by Lineweaver-Burk plot to be 400 M/min and 21.4 mM, respectively.

• Korean Journal of Food Science and Technology
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• v.29 no.2
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• pp.320-325
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• 1997

Transglucosidase (TG) from Aspergillus niger was immobilized on various carriers by several immobilization methods such as ionic binding, adsorption, entrapment, covalent linkage and metal chelation to improve the process performance. The covalent linkage with CNBr-activated sepharose 4B was found as the best method for immobilization of TG based on the immobilization yield which was 61.3%. The immobilization through ionic binding and adsorption gave 33.1% and 22.5% yield respectively but both methods were not selected due to lower yield than covalent linkage using CNBr-Sepharose 4B. Internal diffusion resistance in beads developed by entrapment were not suitable factor in producing final target products. Covalent linkage of TG on magnesium silicate, silica gel and glass bead and metal chelation method didn't result in higher yield than the selected one, either.

• Journal of Ginseng Research
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• v.23 no.2 s.54
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• pp.93-98
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• 1999

In order to evalulate the qualities of red ginseng extract and decrease precipitate fonnation in ginseng drink, red ginseng extract was hydrolized with ${\beta}-amylase$ and transglucosidase. $5.2\%$ isomaltose was produced as isomaltooligosaccharides and glucose content was increased in the enzyme treated ginseng extract. Contents of ginsenoside $R-b_1\;and\;R-b_2$ were decreased, whereas ginsenoside-Rd was increased by the enzyme treatments. The growth of 3 strains of bifidus spp. and 4 strains of lactobacillus spp., beneficial intestinal bacteria, were enhanced by adding of the enzymatically hydrolized ginseng extract. Sweetness and sourness were increased, however, bitterness and astringency were decreased in the hydrolized ginseng extract. The fonnation of precipitates in hydrolized red ginseng extract of $pH\;3.0\~4.5$ were significantly decreased in the storage condition of $40^{\circ}C$ for 1 month compared to that of control.

• Korean Journal of Food Science and Technology
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• v.30 no.1
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• pp.110-117
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• 1998

A packed-bed reactor with immobilized transglucosidase (TG) was operated to test the possibility of continuous production of isomaltooligosaccharides (IMO) and the effect of concentration and feed rate of substrate solution on the production pattern as well as operational stability The pattern of formation of IMO was the same to the one of soluble TG. The concentrations of glucose and isomaltose produced by the packed-bed reactor were gradually decreased as the flow rates were increased regardless of the concentrations and kinds of maltose solution as substrate. Isomaltotriose showed the same tendency except 10% maltose solution. But the concentration of panose was increased and then decreased as the flow rates were increased. The maximum yield of IMO was 52.1% when 10% (w/v) solution was fed to the reactor at 2 mL./min feed rate. When each 20% and 30% (w/v) solution was respectively used at $0.5{\sim}1.0\;mL/min$, the maximum yield were $39.0{\sim}38.0%\;and\;12.1{\sim}14.2%$. The maximum yield was 36.3% at $0.5{\sim}1.0\;mL/min$ when a commercial maltose product containing 20% maltose was used. The reactor was stably operated at $55^{\circ}C$. 85% and 65% of initial activity was maintained for 144 hours and 288 hours of operation, respectively. A reactor analysis strongly an immobilized TG system could apply to continuous production of IMO.

• Journal of Life Science
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• v.28 no.8
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• pp.969-976
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• 2018

In this study, transglucosidase (TG), an enzyme produced by Aspergillus niger, synthesized isomaltooligosaccharide from ${\alpha}-(1{\rightarrow}4)$ linked substrates. The highest TG-producing A. niger KCTC6913 was selected from six kinds of species, and optimized TG producing conditions were established. Five different carbon sources (potato starch, sweet potato starch, corn starch, wheat starch, and dextrin) and three different nitrogen sources (yeast extract, malt extract, and beef extract) were tested to establish the carbon and nitrogen sources favorable for TG production. Measurements of TG activity after an initial culture at pH 5.0 for 15 days revealed that potato starch and yeast extract, which are basic culture media, resulted in the highest TG activity. In addition, A. niger KCTC6913 increased TG production under aerobic conditions and a controlled carbon/nitrogen ratio. In conclusion, to evaluate TG activity in the established optimal medium, it is confirmed that the basal and potato dextrose broth medium were used as a control, and the highest TG production was measured, which was highlighted in the established optimal medium.

• Journal of Food Hygiene and Safety
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• v.35 no.1
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• pp.83-92
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• 2020

This study investigated the optimal conditions of enzymatic reaction for production of isomaltooligosaccharides (IMO) using rice flour. To manufacture IMO, commercial enzymes (Termamyl 2X, Maltogenase L, Promozyme D2, Fungamyl 800L and Transglucosidase L) were used. The sugar composition and amount of IMO were examined by HPLC with charged aerosol detector (HPLC-CAD) in each manufacturing process. Liquefaction reaction was performed according to different Termamyl 2X concentrations (0.025%, 0.05%, 0.075%, 0.1%) and reaction times (1 h, 2 h). As a result, the reducing sugar content was the highest at 138.26 g/L when 0.075% Termamyl 2X was added for 2 hours. In order to optimize simultaneous saccharification and transglucosylation, experiments on enzyme selection, enzyme concentration and enzyme reaction time were conducted. Reaction with 0.0015% Maltogenase L, 0.05-0.1% Promozyme D2 and 0.1% Tansglucosidase L was effective in decreasing glucose content and increasing content of IMO with a high degree of polymerization. A change in sugar content was observed every 6 hours to determine the optimal reaction time, and the highest IMO was produced after 36 hours of reaction (75.36 g/L). The IMO prepared under optimal conditions showed isomaltose, 35.11 g/L; panose, 11.97 g/L; isomaltotriose, 19.95 g/L; isomaltotetraose, 7.46 g/L; isomaltopentaose, 1.05 g/L at 18 brix and the ratio of IMO in the total sugar was 56.37%.

• Korean Journal of Food Science and Technology
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• v.30 no.3
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• pp.630-637
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• 1998

Enzymatic properties of immobilized transglucosidase (TG) from Aspergillus niger was characterized and compared with soluble TG. Michaelis-Menten constant $(K_m)$ and maximum velocity $(V_{max})$ of immobilized TG were $122\;mM,\;3.9{\times}10^{-2}\;mM/min$ and in case of soluble TG, 21 mM, 0.4 mM/min. The optimum pH of immobilized TG was pH 5.0 like soluble TG but immobilized TG showed 16% and 45% higher activity than soluble TG at pH 5.0 and pH 6.0. Both of immobilized TG and soluble TG were stable from pH 2.0 to pH 9.0, and therefore their activities in these pH ranges were remained more than 90%. The temperature was optimal at $60{\sim}70^{\circ}C\;and\;70{\sim}80^{\circ}C$ for soluble TG and immobilized TG, respectively. The thermal stability of immobilized TG was significantly improved than that of soluble TG, and immobilized TG retained $32{\sim}40%$ higher activity than soluble TG. D-values from thermal inactivation of immobilized TG were 7690 sec at $65^{\circ}C$, 83 sec at $75^{\circ}C$, 7.2 sec at $80^{\circ}C$. Z-values of soluble and immobilized TG were $6.4^{\circ}C\;and\;5.3^{\circ}C$, respectively. The little difference of activation energies of soluble TG and immobilized TG supposed that there was little difference in mass transfer limitation during the reaction of soluble TG and immobilized TG.

• Microbiology and Biotechnology Letters
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• v.19 no.2
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• pp.140-146
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• 1991

Mutation experiments were performed to select the mutant of Aspergillus niger 55, which had lost almost all the ability to produce transglucosidases but retained that of high productivity of raw meal saccharifying enzyme, by means of successive induction with N-methyl-N'-nitro-N-nitrosoguanidine(MNNG), ultraviolet(UV) light, and ${\gamma}$-rays. Also, we used the mutant enrichment techniques, such as liquid culture-filtration procedure and differential heat sensitivity of conidia, in order to increase the possibility of obtaining a mutant. The glucoamylase productivity of mutant PFST-38 was 11 times higher than that of the parent strain. The mutant PFST-38 was morphologically identical to the parent strain, except for the size of conidia, the tendency to form conidia and the lenght of conidiophore. Asp. niger mutant PFST-38 apeared to be useful for the submerged production of the raw corn meal saccharifying enzyme.

• Applied Biological Chemistry
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• v.3
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• pp.9-15
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• 1962

1) Among 8 strains of Rhizopus and 7 of Aspergillus species investigated for their producibility of saccharifying amylase, Rhizopus delemar ND 1 and Aspergillus usamii mut. shirousamii were selected as having high saccharifying activity. 2). Since Rh. delemar ND 1 shows high saccharifying activity and slight transglucosidase activity, it likely seems suitable for the production of starch-sugar by enzymic saccharification. Asp. usamii mut. shirousamii exerts low saccharifying but moderate transglucesidase activity and is considered to be usable in producing sugar-syrup with particular flavor and taste. 3). Using the saccharogenic enzyme from Rh. delemar ND 1, a prelimimary trial was done to obtain purified glucose powders.