• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.217-221
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• 1996

Various treatments of naked barley with commercial liquefying enzymes have been emploved to reduce high viscosity of naked barley in cooking as a raw material for alcohol production and to increase alcohol yield. The enzyme BAN used for cooking and liquefaction of naked barley was able to make a reduction of one third of viscosity and to enhance alcohol yield of 4 l/Ton of raw material than the T120L was. Of course, alcohol yield depended in part on the applied saccharifying enzymes. The low temperature cooking of naked barley with BAN was favorable compared with high temperature cooking for both of reducing viscosity (210 vs. 237 cp) and final alcohol yield (Yp/so: 0.397 vs. 0.395 g/g) in industrial scale.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1976.04a
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• pp.184.5-184
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• 1976

In the course of studies on thermostable liquefying amylase from thermostable Bacillus spp., we have isolated a strain which produces amylase activity. This strain was identified to be Bacillus stearothermophlus. The amylase of this strain demonstrated a maximum activity at 65$^{\circ}C$ and Ca$\^$＋＋/ did not improve thermostability of the enzyme although the erzyme was capable of hydrolyzing starch at temperature of 80$^{\circ}C$ and above. The maximum amount of the enzyme was product at pH 7.0, 50$^{\circ}C$.

• The Korean Journal of Food And Nutrition
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• v.1 no.2
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• pp.43-49
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• 1988

Fermented barley food was produced by the combining action of an enzyme and a lactobacillus. When Lactobacillus sp. L-5 and commercial liquefying amylase from Tae Pyeong Yang Chemical Co. were selected, inoculated on steamed barley and cultivated at 37$^{\circ}C$ for 48hrs, the fermented product of good quality was obtained. In batch cultivation using rotary drum fermentor, viable cell count reached 1.1$\times$10CFU/g after 12hrs' cultivation, and specific growth rate in logarithmic phase was 0.6hr-1. Viable cell count, acidity, pH, concentration of reducing sugar and viscosity of the 48hrs' fermentation product from rotary drum fermentor was 4.3$\times$108CFU/g, 1.17%, 3.1, 10.7% and 1430cp.

• Microbiology and Biotechnology Letters
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• v.14 no.3
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• pp.225-232
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• 1986

This study was to improve the quality of Kochuzang and utilize red pepper seed. Kochuzang were prepared with the addition of red pepper seed and garlic (2％), compared the changes in the various chemical components and enzyme activity during the aging period of Kochuzang, and also organoleptic values of the products. Enzyme activities of liquefying and saccharogenic amylase, protease and lipase were increased by addition of garlic pulp and the suvival activities of enzyme except liquefying amylase were lasted high the late period of aging. Also the addition of red pepper seed was effective in maintaining the enzyme activities Change of titration acidity and pH of kochuzang were little when red pepper seed was added, but in case of a garlic additive it showed no difference at the late period of aging. Total nitrogen and amino nitrogen were increased by the addition of red pepper seed or garlic until the late period of aging, and ammonia nitrogen also increased during the middle period of againg, but showed no difference at the late period. Alcohol content was decreased by the addition of garlic or red pepper seed. but crude lipid was increased by the audition of red pepper seed. but crude lipid was increased by the addition of red pepper seed. Generally, taste, flavor and color of garlic added group were superior to the non-garlic added group for the products which aged for 10 weeks. Therefore, The quality of Barley Kochuazng may be improved by adding 2％ garlic to the whole red pepper.

• Applied Biological Chemistry
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• v.12
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• pp.33-41
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• 1969

1. Crude cellulase extracted from wheat bran media of Chaetomium globosum with pH 7.0 McIlvaine buffer was fractionated by precipitation with ammonium sulfate and by treatment with the cellulose powder, DEAE-Sephadex A-25 and Amberite XE-65 (IRC-50) column chromatography. 2. Consquently two cellulases C-1 and C-2 were obtained by cellulose column chromatography. Cellulose C-1 was a powerful CMC-saccharifying and CMC-liquefying activity but cellulose C-2 was stronger CMC-liquefying activity compared to CMC-saccharifying activity and cellulase C-2 had smaller protein than that of cellulose C-1. And cellulose C-2 was fractionated by DEAE-Sephadex A-25 column chromatography into cellulase C-1-1 and cellulose C-1-2. 3. It can be obtained, therefore, that cellulose produced Chaelomium globosum consisted, at least, of three cellulases C-2, C-1-1 and C-1-2. 4. Cellulose C-1-1 was homogenous in the ultraviolet and the ultracentrifuge pattern. And cellulose C-1-1 had enzyme for CMC-saccharifying activity. 5. The optimum pH for the enzyme activity of cellulose C-1-1 was 4.0 in any methods of meas urement reducing sugar and viscosity. The optimum temperature was $40^{\circ}C$ in any methods. 6. The pH stability of cellulase C-1-1 was within pH 5.0 to pH 6.0 at $40^{\circ}C$ and fairly stable in acidic solution. 7. The heat stability was below $50^{\circ}C$ at pH 4.0 and complete heat inactivation of this cellulase occurred at $70^{\circ}C$.

• The Korean Journal of Food And Nutrition
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• v.27 no.3
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• pp.414-420
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• 2014

This study was performed to increase the yield and to reduce the processing times for the preparation to improve the productivity and quality of rice jochung, a traditional food in Korea. In order to evaluate the quality characteristics and yield of jochung, the viscosity, color value, mineral contents and the sensory evaluation were measured. Jochung is prepared from steamed rice (STR), wet-milled rice flour (WRF) and dry-milled rice flour (DRF) by processing methods of rice and reacting times (6 hours or 13 hours) of liquefaction and saccharification. There is commonly added liquefying enzyme for rice liquefaction (0.4%/10 kg rice, at $85{\sim}90^{\circ}C$ for 1 hour or 4 hours) and saccharogenic enzyme with malt (2.5% or 4.5%/10 kg rice, at $56{\sim}60^{\circ}C$ for 5 hours or 9 hours). The inner structural properties of WRF showed the more distinct shape regular structure of uncombined starch particles but the DRF closely maintained particles of rice flour observed by SEM. If processing times for liquefation and saccharification were reduced from 13 hours to 6 hours, the yield of jochungs prepared with WRF increased 8%, the DRF 7%, and the STR 3% respectively and the sensory evaluation as well as color values and overall desirability received high scores. The viscosity, color a and b values of jochung processed with WRF for 6 hours were lower than that processed for 13 hours. The viscosity and color a, b value and Ca content were decreased in the jochung processed with WRF or DRF for 6 hours, but Mg, P and K were increased than that of STR. Jochung processed by 0.4% liquefying enzyme and 2.5% malt with WRF for 6 hours will increase the yield, save manufacturing times and costs and will thereby enable cost-effective techniques.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1242-1248
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• 2007

Genomic analysis of a hyperthermophilic archaeon, Thermococcus onnurineus NA1 [1], revealed the presence of an open reading frame consisting of 1,377 bp similar to ${\alpha}$-amylases from Thermococcales, encoding a 458-residue polypeptide containing a putative 25-residue signal peptide. The mature form of the ${\alpha}$-amylase was cloned and the recombinant enzyme was characterized. The optimum activity of the enzyme occurred at $80^{\circ}C$ and pH 5.5. The enzyme showed a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7), but not pullulan and cyclodextrin. Surprisingly, the enzyme was not highly thermostable, with half-life ($t_{1/2}$) values of 10 min at $90^{\circ}C$, despite the high similarity to ${\alpha}$-amylases from Pyrococcus. Factors affecting the thermostability were considered to enhance the thermo stability. The presence of $Ca^{2+}$ seemed to be critical, significantly changing $t_{1/2}$ at $90^{\circ}C$ to 153 min by the addition of 0.5 mM $Ca^{2+}$. On the other hand, the thermostability was not enhanced by the addition of $Zn^{2+}$ or other divalent metals, irrespective of the concentration. The mutagenetic study showed that the recovery of zinc-binding residues (His175 and Cys189) enhanced the thermo stability, indicating that the residues involved in metal binding is very critical for the thermostability.

• Microbiology and Biotechnology Letters
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• v.14 no.5
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• pp.399-405
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• 1986

Corn starch was saccharified without cooking in an agitated bead reaction system. Uncooked corn starch was effectively hydrolyzed even at the concentration as high as 39%(w/v). After 24 hours. the extent of saccharification reached at 92%, which corresponds glucose concentration of 425g/L. Fed-batch feeding of starch was more effective than batch feeding for saccharification of uncooked corn starch. The composition of hydrolysated of uncooked starch was analyzed. which was composed of 95% glucose, 0.7% of maltose, and 4.5% of high saccharide, similar with that of cooked starch. The hydrolysate can be successfully utilized for HFCS manufacture. The starch liquefying and saccharifying enzyme was relatively stable even be the physical impact of the attrition-milling media. The enzyme stabilizer, $Ca^{++}$, played an essential role in preventing the enzyme deactivation caused by the physical impact.

• Journal of Microbiology and Biotechnology
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• v.11 no.4
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• pp.636-643
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• 2001

Bacillus sp. AIR-5, a strain from soil, produced an extracellular maltopentaose-forming amylase from amylose and soluble starch. This bacterium produced 8.9 g/l of maltopentaose from 40 g/l of soluble starch in a batch fermentation and the maltopentaose made up 90 % of the maltooligosaccharides produced (from maltose to maltoheptaose). The culture supernatant was concentrated using a 30 K molecular weight cut-off membrane and purified by DEAE-Cellulose and Sephadex G-150 column chromatographies. The purified protein showed one band on a native-PAGE and its molecular mass was estimated as 250 kDa. The 250-kDa protein was composed of tetramers of a 63-kDa protein. the isoelectric point of the purified protein was pH 6.9, and the optimum temperature for the enzyme activity was $45^{\circ}C$. The enzyme was quickly inactivated above $55^{\circ}C$, and showed a maximum activity at pH 8.5 and over 90% stability between a pH of 6 to 10. The putative N-terminal amino acid sequence of AIR-5 amylase, ATINNGTLMQYFEWYVPNDG, showed a 96% sequence similarity with that of BLA, a general liquefying amylase.

• Microbiology and Biotechnology Letters
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• v.19 no.3
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• pp.290-295
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• 1991

Direct conversion of raw starch without liquefaction to maltose using maltose-forming fungal a-amylase (Fungamyl) was carried out in an agitated bead enzyme reactor (bioattritor). The reaction rate in bioattritor was comparable with conventional method which utilized liquefied soluble starch. Moreover the extent of maltose formation increased substantially compared with conventional method; from 150 g / I of raw starch, around 95 g/l of maltose was formed and 72% of maltose content in sugar mixture was achieved. Especially, pH influenced greatly not only on total sugar formation from raw starch in bioattritor but also on maltose content in sugar mixture. The optimal pH for maltose formation from raw starch was shifted into the weak alkaline pH, the optimal pH of 8.0~9.0 in bioattritor contrast to pH of 5.0~5.5 for liquefied starch. The maltose formation and content were also affected by the amounts of Fungamyl added and raw starch concentration. Consumption of maltose-forming Fungamyl can be substantially reduced by supplementary addition of starch liquefying a-amylase (Termamyl).