• YAKHAK HOEJI
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• v.5 no.1
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• pp.51-55
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• 1960

Some enzymatic properties of Cynthia roretzi V. Drasche (Korean:U-Rung-Shei) was studied by author and obtained the following results; 1. The optimum pH of the digestive gland proteinase ws 7.4-7.6 2. Activity of metallic ion on the Proteinase showed following order; 10$^{-3}$ M. M $n^{++}$>1-$^{-3}$ M. $Co^{++}$>10$^{-4}$ M. $Mg^{++}$\ulcorner10$^{-2}$ M.S $r^{++}$. Inhibition of metallic ion on the Proteinase showed following order: 10$^{-3}$ M. A $g^{+}$>10$^{-3}$ M. c $d^{++}$>10$^{-3}$ M. P $b^{++}$>10$^{-3}$ M. Z $n^{++}$ 3. The digestive gland enzyme inactivated at 70.deg. C, but no influence at 50.deg. C. 4. When the enzyme concentration increase 2 times, and 3 times, the enzymatic activity also increase, but not proportionally 5. The digestive gland Proteinase showed remarkably higher enzymatic activity than the intestinal Proteinase. 6. The digestive gland amylase brom the ascidion showed remarkably higher enzymatic activity than the heptaponcreatic amylase from shell fish (Turbo (Batillus) Cornutus Solander).).er).).).er).).

• Journal of Microbiology and Biotechnology
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• v.1 no.1
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• pp.54-62
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• 1991

Cyclodextrin glucanotransferase(CGTase) derived from Bacillus macerans was immobilized by (1) covalent linkage on chitosan and chitin with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA 900 after succinylation, and (3) entrapment on alginate and polyacrylamide by cross linking. Adsorption on Amberite IRA 900 and covalent linking on chitosan were identified to be the most suitable immobilization methods considering the yield of activity and stability of immobilized CGTase. The enzymatic properties of immobilized CGTase were investigated and compared with those of the soluble CGTase. Thermal stability of CGTase immobilized on chitosan was increased from 50 to $55^{\circ}C$, and the optimum temperature of CGTase immobilized on Amberite IRA 900 was shifted from 55 to $50^{\circ}C$. The effect of molecular size of soluble starch (substrate) on immobilized CGTase investigated using partially liquefied substrates with different dextrose equivalent(DE). Cyclodextrin(CD) conversion yield augmented according to the increase of DE level for immobilized CGTase on Amberite IRA 900. CD conversion yield of partially cyclized starch with soluble CGTase was higher compared with liquefied one with ${\alpha}-amylase$.

• YAKHAK HOEJI
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• v.4 no.1
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• pp.35-38
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• 1959

The enzymatic activity of amylase which was isolated from a shell fish Veneridae Soxidmnus purpuratus Sowerby(Korean name :Gai-jo-gai") was studied and the obtained results were as follows: (1) The optimum pH of the enzyme was Ca. 6.2-6.4. (2) Prohibiting activity of metalic ions for the enzymatic activity was the order of 1/1000M-$Mg^{++}$>1/1000M-$Sr^{++}$>1/1000M-$Na^{+}$, and $Ca^{++}$ ion's prohibiting action was hardly showed. (3) Of 3 specimens of amyiase from Heptapancreas, Gastro-intestine and crystalline style, the highest activity was shown by amylase from crystlline style, and the other two showed almost same degree of activity. (4) Heptapancreas Amylase from the shell fish showed remarkably higher enzymatic activity than the pancreas amylase from a pig.

• Journal of the Korean Society of Clothing and Textiles
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• v.30 no.9_10 s.157
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• pp.1485-1493
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• 2006

This study was to investigate the effect of different scouring methods on mechanical properties and appearance of lyocell. Two different scouring methods were adopted for the study; one was the traditional scouring with alkali and the other was enzymatic scouring. Enzymatic scouring was carried with four different enzymes; C1 : Cellusoft L, C2 : Cellusoft UL, D1 : Denimax 992L, D2 : Denimax Acid XCL. The mechanical properties of scoured lyocell were measured using KES-FB. The appearance of scoured samples was analyzed by 3D CAD SYSTEM of i-Designer. While the untreated fabric showed the best linearity because it is stiff, alkali treated samples showed the worst dimensional stability and distorted easily. Enzyme treated samples, especially C1 treated samples showed the best dimensional stability. In addition, enzyme treated samples showed low bending rigidity compared to the alkali treated samples. It means that the enzyme treated samples are more flexible than alkali treated samples. However, the smoothness of the sample's surface treated by either of methods did not show much difference. From the study, it was suggested that the enzymatic scouring for lyocell could help to gain natural silhouette.

• Korean journal of food and cookery science
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• v.28 no.1
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• pp.51-55
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• 2012

This study was conducted to investigate the physicochemical properties of citrus peel extracts with different hot water extraction and enzymatic hydrolysis conditions. Enzymatic hydrolysis was also employed using Viscozyme L and results were compared with that of optimized hot water extract. Hot water extraction was performed under different parameters; the sample to solvent ratio(1:20, 1:15, 1:10), extraction time(2, 4 hrs), extraction temperature(85, $95^{\circ}C$) and enzymatic hydrolysis(0, 1%) and the subsequent extracts were used for determining their physicochemical properties, such as total yield, total phenolics, total flavonoids, and electron donating ability (EDA). With the increase in the sample to solvent ratio and extraction time, total yield, total phenolics, total flavonoids and EDA increased. But extraction temperature did not significantly affect the hot water extract. As hot water extract was hydrolyzed by the enzyme, total yield and active ingredients increased rapidly. In the result of total yield, total phenolics, total flavonoids and EDA, the activity of enzyme-treated extract was higher than those of enzyme-untreated extract. Based upon the overall hot water extraction efficiency, it was found that 20 times volume or 120 min at a time at $95^{\circ}C$ after enzyme treatment was optimal.

• The Korean Journal of Food And Nutrition
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• v.9 no.1
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• pp.85-91
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• 1996

B-amylase(EC 3.2.1.2) was isolated from the root of arrowroot(Peuria thunbergiana Bentham) with distilled water and then fractionated with ammonium sulfate. Crude extract was partially purified by ion exchange chromatography and gel filtration. The enzymatic properties of partially purified $\beta$-amylase were as follows, the enzyme was fractionated with ammonium sulfate between 0.2 and 0.4 saturation, and showed the typical reaction properties of B-amylase producing only maltose from starch. Optinum pH and temperature were pH 6.5, $50^{\circ}C$ respectively. The activity of the enzyme had proportional relations with enzyme protein concentration below 4mg, and had Michaelis constant of 66.7mg% for soluble starch. The enzyme was inhibited by some metal louts such as silver, cadmium, mercury, aluminum, iron and copper.

• Journal of Life Science
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• v.9 no.1
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• pp.64-68
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• 1999

The properties of purified intracellular adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) of Nocardioides sp. J-326TK isolated from soil have been studied. The enzyme deaminated adenosine and 2`-deoxyadenosine and the respective {TEX}$K_{M}${/TEX} values were 4.0×{TEX}$10^{-4}${/TEX} M and 5.0× {TEX}$10^{-4}${/TEX} M, but the enzyme was not active on 8-bromoadenosine, 6-methylaminopurine riboside, ATP, ADP, 2`-AMP, 3`-AMP, 5`-AMP, dAMP, cAMP, NAD, FAD, NADP and adenine. The enzyme activity was strongly inhibited by the addition of {TEX}$Hg^{2+}${/TEX} and {TEX}$Ag^{+}${/TEX}, {TEX}$Cu^{2+}${/TEX}, {TEX}$Co^{2+}${/TEX} and {TEX}$Mn^{2+}${/TEX} also inhibited the activity but much less extent. The effect of alkyl reagents, metal chelating reagents and certain other compounds on the enzyme activity were also examined. No reagent activated the enzyme. On the contrary, the enzyme reaction was slightly inhibited by o-phenanthroline and 6-benzyladenosine.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 1998.06a
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• pp.264.2-265
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• 1998

• Journal of Microbiology and Biotechnology
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• v.10 no.3
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• pp.307-311
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• 2000

Abstract Extracellular chitinase was purified from the culture liquid of the marine bacterium, Bacillus sp. LJ-25 , and its enzymatic properties were examined. The purified chitinase exhibited a single band on SDS-PAGE and the molecular weight was estimated to be approximately 50 kDa. The optimum pH and temperature for the enzymatic activity were 7.0 and $35^{\circ}C$, respectively. The activity of the chitinase was strongly inhibited by $Zn^{2+}$ and slightly inhibited by $Ba^{2+},{\;}Co^{2+},{\;}Mn^{2+},{\;}and{\;}Cu^{2+}$. The purified chitinase did not hydrolyze $p-nitrophenolN-acetyl-{\bata}-D-glucosaminide{\;}(GlcNAc)_2$ and Micrococcus lysodeikticus cells, which are known to be the substrates for exo-type chitinase. Among the hydrolyzates of colloidal chitin, $(GlcNAc)_2$ was in the highest concentration with small amounts of GlcNAc and $(GlcNAc)_3$..

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.4
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• pp.585-590
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• 2002

The effects of a high level of sucrose on the moisture content, water activity, protein denaturation and sensory properties in Chinese-style pork jerky were investigated. The pork jerky with different levels (0, 12, 15, 18 and 21%) of sucrose was prepared. Fifteen frozen boneless pork legs from different animals were used in this trial. Sucrose is a non-reducing disaccharides and would not undergo non-enzymatic browning. Some studies pointed out that sucrose might be hydrolyzed during freezing, dehydration and storage into glucose and fructose, and cause non-enzymatic browning in meat products. The results showed that moisture content and water activity of pork jerky decreased with increase of the level of sucrose. At the same time, shear value was increased due to the reduced moisture content and water activity by osmotic dehydration. However, a higher level of sucrose had a significantly negative effect on protein solubility and extractability of myosin heavy chain of pork jerky due to non-enzymatic browning. From the results of sensory panel tests, the pork jerky with 21% of sucrose seems to be more acceptable by the panelists in hardness, sweetness and overall acceptability.