• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.2
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• pp.106-111
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• 2003

A novel carbohydrolase, which is a DXAMase, containing both dextranase and amylase equivalent activities, was purified from Lipomyces starkeyi KSM22. The purified DXAMase was also found to hydrolyze cellobiose, gentiobiose, trehalose and melezitose, while disproportionation reactions were exhibited with various di- and tri-saccharides, such as maltose, isomaltose, gentiobiose, kojibiose, sophorose, panose, maltotriose, and isomaltotriose with various kinds of oligosaccharides produced as acceptor reaction products. Furthermore, the purified DXAMase hydrolyzed raw waxy rice Starch and produced maltodextrin to the extent of 50% as a glucose equivalent.

• KSBB Journal
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• v.26 no.3
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• pp.206-210
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• 2011

The growth effect of Nannochloropsis oculata (N.oculata), unicellular microalgae, by alginate was investigated. Alginate was depolymerized with sulfuric acid ($H_2SO_4$) and heat ($121^{\circ}C$), simultaneously. Addition of 0.75% alginate oligomer depolymerized with 0.2 N $H_2SO_4$ showed the maximum yield and the growth rate of N. oculata. Chlorophyll content and reducing sugar was increased by alginate oligomer in a dose-dependent manner. Alginate oligomer promoted the growth of N. oculata, whereas the original alginate polysaccharides had no significant effect. Laminaria japonica (L. japonica) extract containing high level of alginate was also increased growth rate and chlorophyll content. $CO_2$ supply addition to L. japonica extract showed no change the growth rate, although addition to alginate oligomer showed prominently increased. N. oculata could use more saccharides in presence of $CO_2$ according to reducing sugar determination. From these results, it is useful to establish optimal condition for high cell density cultivation of N. oculata.

• Journal of Microbiology and Biotechnology
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• v.22 no.8
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• pp.1118-1126
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• 2012

Four putative GH12 genes were found in the Fusarium graminearum genome. The corresponding proteins were expressed in Escherichia coli, purified, and evaluated. FGSG_05851 and FGSG_11037 displayed high activities towards xyloglucan ($V_{max}$ of 4 and $11{\mu}mol/min$, respectively), whereas FGSG_07892 and FGSG_16349 were much less active with this substrate (0.081 and $0.004{\mu}mol/min$, respectively). However, all four of these enzymes had a similar binding affinity for xyloglucan. Xyloglucan was the substrate preferred by FGSG_05851, in contrast to the three other enzymes, which preferred ${\beta}$-glucan or lichenan. Therefore, FGSG_05851 is a xyloglucan-specific glucanase (E.C. 3.2.1.151) rather than an endoglucanase (E.C. 3.2.1.4) with broad substrate specificity. FGSG_11037 displayed a peculiar behavior in that the xyloglucan binding was highly cooperative, with a Hill coefficient of 2.5. Finally, FGSG_05851 essentially degraded xyloglucan into hepta-, octa-, and nonasaccharides, whereas the three other enzymes yielded hepta- and octa-saccharides as well as larger molecules.

• Journal of Dairy Science and Biotechnology
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• v.24 no.1
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• pp.65-73
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• 2006

This study was to review recent reports in effects of various starter cultures on the viscosity in stirred yogurt. The rheological properties of yogurt have received considerable attention in the literature. Most yogurts are typically made by mixed cultures of Lactobacillus bulgaricus and Streptococcus thermophilus. The viscosity of yogurt made by mixed cultures was much higher than that of yogurt by single cultures. Since texture of stirred yogurt is the result of both acid aggregation of casein micelles and production of exopoly-saccharides, it is suggested that yogurt be made by the exopolysaccharide-producing cultures in order to increase viscosity, Both types of exopolysaccharides are capsule and loose slime(ropy). But it is desirable to use encapsulated nonropy strains. And Bifidobacteria affects adversely to the viscosity of yogurt. Therefore, starter cultures which have an effect on yogurt viscosity have been widely demonstrated. This review is the search for the development of viscosity in stirred yogurt.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.5
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• pp.461-467
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• 2009

A bacterial strain was screened and identified from sea sediments in Tongyeong coastal area in order to obtain proteases or peptidase cleaving C-terminal of glutamic acid. Strain TS0611, which showed the highest activity from 5 isolated protease producing strains, was selected and its properties investigated. Strain TS0611 was a gram-positive rod, $1.2\;{\mu}m$ in cell length, catalase positive, motility-positive, melanin-negative and grew at 15~$50^{\circ}C$, and hydrolyzed gelatin and casein. This strain was identified as Bacillus thuringiensis or Bacillus cereus based on results from the API system(API 50 CHB) which examined saccharides properties, fatty acid composition of cell wall, and 16S rRNA gene sequence.

• Journal of Microbiology and Biotechnology
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• v.7 no.3
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• pp.174-179
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• 1997

In order to investigate effect of glucooligosaccharide (GOS) prepared by extrusion process as a bifidogenic factor, cultivation of Bifidobacterium sp., Bacteroides fragilis and Clostridium perfringens was done and analyzed. B. fragilis and C. perfringens were able to utilize only 16% and 11% of the oligosaccharides in GOS, respectively, whilst Bifidobacterium sp. FBD-22 could utilize 38%. Especially, many kinds of oligo saccharides in GOS were able to be utilized selectively only by Bifidobacterium sp.. In case that GOS, as a carbon source, was used in the co-cultivation by Bifidobacterium sp., B. fragilis and C. perfringens, growth of Bifidobacterium sp. was not influenced by the existence of B. fragilis and C. perfringens. Bifidobacterium sp. showed advantage on carbon source competition for GOS with B. fragilis. Acetic acid, antimicrobial agent in the intestine, was produced two times more from GOS than glucose in co-cultures of three strains. Therefore, it is suggested that GOS can be a potent bifidogenic factor which proliferates the population of Bifidobacterium sp. and may finally improve the intestinal environments of human.

• Journal of Microbiology and Biotechnology
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• v.17 no.9
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• pp.1430-1436
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• 2007

[ ${\alpha}$ ]-Galactosidase was immobilized in a mixture of k-carrageenan and locust bean gum. The properties of the free and immobilized enzyme were then determined. The optimum pH for both the soluble and immobilized enzyme was 4.8. The optimum temperature for the soluble enzymes was $50^{\circ}C$, whereas that for the immobilized enzyme was $55^{\circ}C$. The immobilized enzyme was used in batch, repeated batch, and continuous modes to degrade the raffinose-family sugars present in soymilk. Two hours of incubation with the free and immobilized ${\alpha}$-galactosidases resulted in an 80% and 68% reduction in the raffinose oligo saccharides in the soymilk, respectively. In the repeated batch, a 73% reduction was obtained in the fourth cycle. A fluidized bed reactor was also designed to treat soymilk continuously and the performance of the immobilized ${\alpha}$-galactosidase tested at different flow rates, resulting in a 90% reduction of raffinose-family oligosaccharides in the soymilk at a flow rate 40 ml/h. Therefore, the present study demonstrated that immobilized ${\alpha}$-galactosidase in a continuous mode is efficient for reducing the oligosaccharides present in soymilk, which may be of considerable interest for industrial application.

• Microbiology and Biotechnology Letters
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• v.32 no.4
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• pp.347-351
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• 2004

Hydrolysis of manno-oligosaccharides and galactomannan was studied with the purified Bacillus subtilis WL-7 mannanase from recombinant Eschericoli. The predominant products of hydrolysis were mannose, mannobiose and mannotriose. The enzyme could hydrolyze $\beta$-1 A-linked manno-oligosaccharides larger than mannobiose, but was not active on mannobiose. When the mannanase hydrolyzed manno-oligo saccharides of degree of polymerization(DP) 4-6, it was more active on the substrate of higher DP. Based on analysis of transient reaction products by TLC, the enzyme was found to have a preference for internal $\beta$-IA-mannosidic linkages, which are the central mannosidic bond of mannotetraose and the two middle mannosidic bonds of mannopentaose. The $\beta$-l A-mannosidic bonds situated at the second and fourth positions from the nonreducing end of mannohexaose were preferenhydrolyzed by the mannanase. Locust bean gum(LBG) was enzymatically hydrolyzed with higher efficiency than guar gum, resulting that amount of reducing sugars was liberated more efficiently from LBG than guar gum with same activity of mannanase.

• The Korean Journal of Food And Nutrition
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• v.6 no.3
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• pp.189-198
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• 1993

This study was carried out to investigate the effect of medium-cooked rice on brewing of yakju which was a traditional rice wine in Korea. The influences of cooking temperature of rice on hydrolysis of rice starch and rice protein were tested, and experimental brewings were done according to the traditional brewing method of Bangmunju in which some medium-cooked rice was used. The results obtained were as follows The hydrolysis of starch and protein in medium-cooked rice at 60~$65^{\circ}C$ was easier than that of full-cooked rice at 80~10$0^{\circ}C$. The amounts of saccharides, total amino acids and extracts In Yakju brewed with the combined use of medium-cooked rice and full-cooked rice were twice as much as those brewed with full-cooked rice only. The results of sensory test of Yakju brewed with the combined use of medium-cooked rice and full-cooked rice were better in taste, color and flavor than those brewed with full-cooked rice only. It was thought that our ancestor's traditional brewing method of Yakju in which medium cooked rice and full-cooked rice were used combinedly was excellent Judging from zymological point of views.

• The Korean Journal of Food And Nutrition
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• v.10 no.1
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• pp.87-91
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• 1997

Isomaltooligosaccharides in Sikhye were digested with enzyme (30unit/ml) of $\alpha$-amylase, $\alpha$-glucosidase and glucoamylase from Aspergillus awamori, sweet potato $\beta$-amylase and human salivary $\alpha$-amylase at 37$^{\circ}C$ for 1 hour, respectively. These amylases acted on these saccharides to give hydrolysis products with less than 20% of degree of hydrolysis, except the case of glucoamylase with 62% of high degree of hydrolysis. $\alpha$-Glucosidase plus human salivary $\alpha$-amylase hydrolyzed it to attain the hydrolysis value up to 25%, but further increment of hydrolysis was not observed. Rice residue in Sikhye has similar sugar composition and structure, judging from sugar analyses by the enzymatic hydrolysis. These results suggest that isomaltooligosaccharides and rice residue in Sikhye can be a growth factor for Bifidobacterium and dietary fiber which is useful for human health.