• Asian-Australasian Journal of Animal Sciences
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• v.12 no.1
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• pp.84-92
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• 1999

The rumen microbial ecosystem is coming to be recognized as a rich alternative source of genes for industrially useful enzymes. Recent advances in biotechnology are enabling development of novel strategies for effective delivery and enhancement of these gene products. One particularly promising avenue for industrial application of rumen enzymes is as feed supplements for nonruminant and ruminant animal diets. Increasing competition in the livestock industry has forced producers to cut costs by adopting new technologies aimed at increasing production efficiency. Cellulases, xylanases, ${\beta}$-glucanases, pectinases, and phytases have been shown to increase the efficiency of feedstuff utilization (e.g., degradation of cellulose, xylan and ${\beta}$-glucan) and to decrease pollutants (e.g., phytic acid). These enzymes enhance the availability of feed components to the animal and eliminate some of their naturally occurring antinutritional effects. In the past, the cost and inconvenience of enzyme production and delivery has hampered widespread application of this promising technology. Over the last decade, however, advances in recombinant DNA technology have significantly improved microbial production systems. Novel strategies for delivery and enhancement of genes and gene products from the rumen include expression of seed proteins, oleosin proteins in canola and transgenic animals secreting digestive enzymes from the pancreas. Thus, the biotechnological framework is in place to achieve substantial improvements in animal production through enzyme supplementation. On the other hand, the rumen ecosystem provides ongoing enrichment and natural selection of microbes adapted to specific conditions, and represents a virtually untapped resource of novel products such as enzymes, detoxificants and antibiotics.

• Journal of the Korean Wood Science and Technology
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• v.43 no.5
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• pp.628-640
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• 2015

Cellulase is the key enzyme in the use of cellulose-based biomaterials. Because of its structure, cellulose is difficult to be degraded by enzymes. In order to utilize cellulose-based biomaterials efficiently, evolutionary wisdom of how to use enzymes accurately and harmoniously in a biological system is needed, such as the cellulose digestive system in animals. In this study, the symbiotic bacteria from snails, Achatina fulica, were identified and their cellulase activity was evaluated. The 16S rRNA sequence analysis of 100 aerobic bacteria showed that they belonged to 9 genus and almost half of the bacteria were Lactococcus spp. Among 100 identified strains, only two Aeromonas sp. strains showed cellulase activity. Aeromonas sp. KMBS020 had both endo-${\beta}$-glucanase and ${\beta}$-glucosidase activities but Aeromonas sp. KMBS018 had ${\beta}$-glucosidase activity only. None of the 100 bacterial colonies had any cellobiohydrolase activity.

• Proceedings of the KSCN Conference
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• 2001.05a
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• pp.459.2-460
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• 2001

• Journal of the Korean Wood Science and Technology
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• v.38 no.2
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• pp.140-148
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• 2010

This study was to investigate the enzymatic hydrolysis of cellulose using the cellulase from whole body of the native termite collected in Milyang-si, Kyungsangnamdo, Korea. In the results, optimal temperature and pH for the enzyme of native termites were $45^{\circ}C$ and pH 5.5 for both endo-${\beta}$-1, 4-glucanase and ${\beta}$-glucosidase. Enzyme activity of the termite enzyme was shown $8.8{\times}10^{-2}\;FPU/m{\ell}$. And the highest glucose hydrolysis rate of cellulose by the digestive enzyme from test termites was 24.5% based on the glucan, comparing 59.7% by commercial enzyme (only celluclast 1.5 L) at 1% (w/v) substrate and 36 hours in hydrolysis time. This hydrolysis rate by the digestive enzyme from test termites was comparatively high value in 41% level of the commercial enzyme. When cellulose was hydrolyzed by the digestive enzyme of the native termite, glucose hydrolysis was almost completed in 12 hours which was the considerably reduced time for cellulose hydrolysis. It was suggested that the quiet short reaction time for cellulose hydrolysis by the enzyme from native termite could be a very high advantage for development of hydrolysis cellulase for lignocellulosic biomass.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.12
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• pp.1784-1789
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• 2002

One hundred and twenty-eight growing barrows (Jiaxing Black${\times}$Duroc${\times}$Landrace) at an average BW of 20.8 kg were allocated to four treatments for 42 days, each of which was replicated four times with eight pigs per replicate and used to investigate the effects of fructooligosaccharide (FOS) on digestive enzyme activities, intestinal microflora and morphology of growing pigs. The pigs received the same basal corn-soybean meal diet and FOS was added to the basal diet at 0, 2, 4, 6 g/kg diet at the expense of corn, respectively. As compared to control, supplementation with 4 and 6 g/kg FOS significantly improved average daily gain and feed efficiency. Addition of FOS enhanced the growth of Bifidobacterium and Lactobacillus, but inhibited Clostridium and Escherichia coli in the small intestinal and proximal colonic contents. Supplementation with 4 and 6 g/kg FOS significantly improved the activities of total protease, trypsin and amylase in the small intestinal contents. However, FOS had no significant effect on the activity of lipase in the small intestinal contents as well as the digestive enzymes in pancreas. Morphological measurement of jejunal mucosa did show response to consumption of FOS. Villus height and the villus height to crypt depth ratio at the jejunal mucosa were significantly higher with 4 and 6 g/kg FOS supplementation as compared to control.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.6
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• pp.577-583
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• 2001

The digestive enzyme activities such as $\alpha-amylase$, trypsin and pepsin from the laboratory-reared river puffer Takifugu obscurus were measured from the time course of 1 day until the 65 day after hatching. In the case of $\alpha-amylase$, it was showed minimum activity of 0.0493 U/mg at the total length (TL) 10 mm, and showed maximum activity of 0.1480 U/mg at 19 mmTL. Trypsin and pepsin were showed their maximum activities of 0.0264, 0.0258 U/mg and 0.0178, 0.0201 U/mg when the total length of 16 and 24 mm, and represented remarkable correlations between the changes of enzyme activity and growth rate. The ontogenetic variations of digestive enzymes were represented clearly different patterns; i.e, the pepsin showed higher activity when the periods of larva ($4\~5\;mmTL$) and juvenile II ($19\~24\;mmTL$), however, the trypsin represented maximum activity at the stages of juvenile I ($11\~16\;mmTL$) and young fish (27 mmTL), respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.16 no.2
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• pp.147-153
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• 1983

To check the differences of the digestive enzymes by the bait habits and the proteolytic activities of the fissile extracts from the fish, omnivorous filefish (Navodon modestus), carnivorous cat shark (Scilliorhinus tarazame) and bloodsucking hag fish (Eptatretus burgeri) were sampled for this experiment. The activity of crude alkaline protease extracted from the muscle and the internal organs of the samples was determined with casein as substrate. The activity of the proteolytic enzymes showed remarkable differences by the organs of the fish. The optimum condition of the pretenses from the muscle revealed in range of pH 7.8-8.3, at $60-65^{\circ}C$, while those of the enzymes from the internal organs were at about pH 8.2, $45-55^{\circ}C$, but those of hag fish were at about pH 6.7, $45-55^{\circ}C$. The proteolytic activity of the enzyme of alimentary canal in filefish and in hag fish was 57 and 11 times stronger than that of muscle, respectively. The crude enzyme from the alimentary canal of file fish showed the strongest proteolytic activity in samples submitted and that of cat shark was the lowest. The activity of pancreatic alkaline protease in cat shark was 50 fold higher than that of muscle alkaline protease in the fish.

• Journal of Ginseng Research
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• v.48 no.3
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• pp.253-265
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• 2024

Orally administered ginsenosides, the major active components of ginseng, have been shown to be biotransformed into a number of metabolites by gastric juice, digestive and bacterial enzymes in the gastrointestinal tract and also in the liver. Attention is brought to pharmacokinetic studies of ginseng that need further clarification to better understand the safety and possible active mechanism for clinical application. Experimental results demonstrated that ginsenoside metabolites play an important role in the pharmacokinetic properties such as drug metabolizing enzymes and drug transporters, thereby can be applied as a metabolic modulator. Very few are known on the possibility of the consistency of detected ginsenosides with real active metabolites if taken the recommended dose of ginseng, but they have been found to act on the pharmacokinetic key factors in any clinical trial, affecting oral bioavailability. Since ginseng is increasingly being taken in a manner more often associated with prescription medicines, ginseng and drug interactions have been also reviewed. Considering the extensive oral administration of ginseng, the aim of this review is to provide a comprehensive overview and perspectives of recent studies on the pharmacokinetic properties of ginsenosides such as deglycosylation, absorption, metabolizing enzymes and transporters, together with ginsenoside and drug interactions.

• Korean Journal of Food Science and Technology
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• v.13 no.3
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• pp.241-246
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• 1981

A fungal strain which produced high levels of acid protease and amylase was isolated from the atmosphere for application to the manufacture of digestive enzme preparation. This study was carried out to elucidate its microbiological characteristics, environmental conditions for production of the enzymes, and relationships between the enzyme activity and acidity. 1. The isolate was identified as a fungal strain which belonged to Aspergillus niger by the manual of Rafer and Fennel, and was found to be a strain producing high levels of acid protease and amylase. 2. The optimal pH of tile enzymes produced by the strain were: protease, 2.0;, ${\alpha}-amylase$, 4 to 5; and glucoamylase, 3 to 5. 3. The optimal culture conditions for production of the enzymes were: protease (at pH 2.5), 2 to 3 days incubation on wheat bran at $30^{\circ}C$; ${\alpha}-amylase$ and glucoamylase(at pH 3.0), 3 days incubation at $30^{\circ}C$. 4. The production of acid protease and glucoamylase was increased approximately by 20 percent when 2 percent of corn starch was added to the wheat bran medium. 5. The addition of 0.3 percent ammonium sulfate to the wheat bran medium resulted in enhancing the enzyme production, especially of acid prctease.

• Journal of Life Science
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• v.23 no.4
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• pp.554-559
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• 2013

Brown rice (Oryza sativa) is rich in nutrients, including dietary fiber, vitamins, minerals, and other unmeasured constituents, as well as carbohydrates. Brown rice is an applicable staple for chronic diseases, such as diabetes and hyperlipidemia, but it is not commonly used in dietary management due to several reasons. In this study, we investigated the possibility of using digestive enzymes to process brown rice. When the weight of the brown rice was measured after packing in the same volume of water, it was increased in pectinase-treated brown rice compared to control or collagenase-treated brown rice. Using SEM analysis, we observed huge scratches and nanopores on the surface of the brown rice after the pectinase treatment, but the nutritional components were preserved. We also analyzed the water adsorption rate and performed a starch reaction assay to examine the physical changes after the pectinase treatment. The pectinase-treated brown rice showed a higher water adsorption rate and a faster starch reaction than the nontreated brown rice. These results suggest that digestive enzymes like pectinase can aid the nutritional preservation of brown rice and improve its taste.