• Microbiology and Biotechnology Letters
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• v.23 no.3
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• pp.304-310
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• 1995

A thermophilic bacterium producing the extracellular cellulase-free xylanase was isolated from soil and has been identified as Bacillus sp. The optimal growth temperature was 50$\circ$C and the optimal pH, 7.0. Under the optimal growth condition, maximal xylanase production was 2.2 units/ml in the flask culture. The enzyme production was induced by xylan and xylose, but was repressed by sucrose or trehalose. The partially purified xylanase was most active at 70$\circ$C. It was found that the enzyme was stable at 65$\circ$C for 10 hours with over 75% of the activity. The enzyme was most active at pH 7.0 and retained 90% of its maximum activity between pH 5.0 and pH 9.0 though Bacillus sp. was not grown on alkaline conditions (>pH 8.0). In addition, the activity of xylanase was over 60% at pH 10.0. At the ambient temperature, the enzyme was stable over a pH range of 5.0 to 9.0 for 10 h, indicating that the enzyme is thermostable and alkalotolerant. The activity of xylanase was completely inhibited by metal ions including Hg$^{2+}$ and Fe$^{2+}$, while EDTA, phenylmethylsulfonyl fluoride (PMSF), $\beta$-mercaptoethanol and SDS didn't affect its activity. The enzyme was also identified to exert no activity on carboxymethylcellulose, laminarin, galactomannan, and soluble starch.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.567-570
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• 2000

The condition of immobilization of the partially purified levan fructotransferase and the properties of the immobilized enzyme was investigated. Levan fructotransferase was immobilized on ${\kappa}\;-carrageenan$ beads by entrapment method. The optimal ${\kappa}\;-carrageenan$ concentration was obtained 2%(w/v) (or the matrix. At that time, immobilized enzymes(0.81 units) have relative low activity compare with soluble enzyme(7.7 units). To immobilized and soluble enzyme, optimal activity temperature and pH were measured $55^{\circ}C$, 6.0 in sodium phosphate buffer 20mM solution. If crosslinking agent was added, proper concentration was 0.5%(v/v). At $37^{\circ}C$, immobilized and soluble enzyme converted levan to oligofructose and DFA IV, and the conversion ratio was 32% and 61% at 60 hr.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.2
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• pp.417-422
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• 1999

Algin and chitosan are known as biodegradable natural polymers. PVA is useful for the production of water soluble packaging, paper, textile sizes. PVA/Algin and PVA/chitosan films were prepared by solution blends method in the weight ratio of chitosan, algin for the purpose of useful biodegradable films. Thermal and mechanical properties of blend films such as DSC, impact strength, tensile strength and morphology by SEM were determined. As a result, The ratio of 10.0wt% PVA/chitosan films were similar to PVA at thermal and mechanical properties. PVA/Algin films were found that phase separation was occured as more than 25wt% increasing the blend ratio of algin. PVA/Algin films were observed to be less partially compatibility than 10wt% increasing the blend ratio of algin by DSC, mechanical properties and SEM. Blend films were completely degraded pH 4.0 better than 7.0, 10.0 in the buffer solution. Also, they were rapidly degraded in the enzyme( glucosidase) solution better than pH solution by enzymolysis.

• Journal of Nutrition and Health
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• v.14 no.3
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• pp.146-150
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• 1981

Some enzymatic properties of the lipase extracted from rice bran were studied. The rate of free fatty acid formation as a function of incubation time was maximum after 30 min. at $35^{\circ}C$. The activation energy of the enzyme was 1.83 Kcal/mol and using a olive oil emulsion as substrate, the Km value was $0.8{\times}10^{-3}M$. The enzyme activity was more stimulated by calcium ion. Application of these enzymatic properties onto the effective utilization of rice bran and preservation of rice were discussed.

• Journal of the Korean Society of Clothing and Textiles
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• v.23 no.8
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• pp.1139-1148
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• 1999

This paper discussed the assessment of hand of denim fabrics finished by enzymatic hydrolysis. The semantic differential scale established using the database collected from university students. Analyzing the subjective rating by common factor analysis with oblimin rotation five factors expressing the hand were induced. Factor one was the surface property related to the surface roughness or softness Factor two was the durability which was related to the compactness and bearing strength Factor three was the sense of weight which was related to the thickness and weight. The moisture related properties and the sense of shape recovery were the forth and fifth factors respectively. the evaluations on the surface property weight and moisture related properties were similar by men and women However the shape recovery and the durability were evaluated differently. Surface and weight related properties were important factors judging the hand of fabrics by both group.

• Food Science of Animal Resources
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• v.36 no.1
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• pp.114-121
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• 2016

This study was performed to improve the techniques used for tenderizing red meat as elderly food. Beef meat was immersed in liposome encapsulated enzyme solution and the effect of protease encapsulation on the beef properties was analyzed. The protease encapsulation properties were analyzed according to the size distribution and enzymatic activity. After enzyme reaction on the beef, the chemical properties of the meat such as pH, water holding capacity, shear rate, lipid oxidation and total volatile basic nitrogen (TVB-N) were analyzed. The pH of the beef increased during the reaction and coating protease (CP) was higher than non-coating protease (NCP). Total color differences were increased remarkably after 36 h and generally, the difference in CP was relatively lower than in NCP. WHC was significantly decreased within 24 h, and no effect from the protease coating was observed. Protease activity was significantly increased within 48 h and no differences in the enzyme coating were observed. The TVB-N value of NCP was increased within 24 h while CP was sustained for up to 36 h. The TVB-N value of protease treated meat increased after 36 h and no effect from the protease coating was detected. Consequently, liposome encapsulated protease was found to have similar properties as non-coated protease. Application of liposome seems to be an interesting option for injecting various functional materials without changing the properties of meat.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.9
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• pp.1300-1306
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• 2011

This study investigated the physicochemical characteristics of wet-milled rice flour treated with pectinase and cellulase in a steeping process. Enzyme treatments were used as follows: pectinase 0.05%, cellulase 0.05%, and mixed enzyme treatments 0.05~0.2%. For particle distribution, rice flour E-treated with mixed enzymes (pectinase 0.05% and cellulase 0.05%) was the finest at 48.3% particle distribution less than $53\;{\mu}m$. Protein contents and damaged starch were reduced by enzyme treatments. Damaged starch was the lowest (12.1%) in rice flour E compared with non-enzyme treatment (18.1%). Amylose content, water binding capacity, solubility, and swelling power all increased upon enzyme treatments, and their effects increased upon mixed enzyme treatment. For gelatinization characteristics of RVA, peak viscosity, final viscosity, breakdown, and total setback viscosity increased in rice flours treated with mixed enzymes. Especially, in steeping method with mixed enzyme treatment, pectinase 0.05% and cellulase 0.05% treatment was suitable for minimizing damaged starch and high fine particle distribution of rice flours compared with single enzyme treatment.

• Journal of Microbiology and Biotechnology
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• v.26 no.10
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• pp.1701-1707
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• 2016

Lipoxygenase (LOX) is an industrial enzyme with wide applications in food and pharmaceutical industries. The available structure information indicates that eukaryotic LOXs consist of N terminus β-barrel and C terminus catalytic domains. However, the latest crystal structure of Pseudomonas aeruginosa LOX shows it is significantly different from those of eukaryotic LOXs, including the N-terminal helix domain. In this paper, the functions of this N-terminal helix domain in the soluble expression and catalysis of P. aeruginosa LOX were analyzed. Genetic truncation of this helix domain resulted in an insoluble P. aeruginosa LOX mutant. The active C-terminal domain was obtained by dispase digestion of the P. aeruginosa LOX derivative containing the genetically introduced dispase recognition sites. This functional C-terminal domain showed raised substrate affinity but reduced catalytic activity and thermostability. Crystal structure analyses demonstrate that the broken polar contacts connecting the two domains and the exposed hydrophobic substrate binding pocket may contribute to the insoluble expression of the C terminus domain and the changes in the enzyme properties. Our data suggest that the N terminus domain of P. aeruginosa LOX is required for its soluble expression in E. coli, which is different from that of the eukaryotic LOXs. Besides this, this N-terminal domain is not necessary for catalysis but shows positive effects on the enzyme properties. The results presented here provide new and valuable information on the functions of the N terminus helix domain of P. aeruginosa LOX and further improvement of its enzyme properties by molecular modification.

• Food Science of Animal Resources
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• v.43 no.1
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• pp.46-60
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• 2023

Slaughterhouse blood is a by-product of animal slaughter that can be a good source of animal protein. This research purposed to examine the functional qualities of the blood plasma from Hanwoo cattle, black goat, and their hydrolysates. Part of the plasma was hydrolyzed with proteolytic enzymes (Bacillus protease, papain, thermolysin, elastase, and α-chymotrypsin) to yield bioactive peptides under optimum conditions. The levels of hydrolysates were evaluated by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis. The antioxidant, metal-chelating, and angiotensin I-converting enzyme (ACE) inhibitory properties of intact blood plasma and selected hydrolysates were investigated. Accordingly, two plasma hydrolysates by protease (pH 6.5/55℃/3 h) and thermolysin (pH 7.5/37℃/3-6 h) were selected for analysis of their functional properties. In the oil model system, only goat blood plasma had lower levels of thiobarbituric acid reactive substances than the control. The diphenyl picrylhydrazyl radical scavenging activity was higher in cattle and goat plasma than in proteolytic hydrolysates. Ironchelating activities increased after proteolytic degradation except for protease-treated cattle blood. Copper-chelating activity was excellent in all test samples except for the original bovine plasma. As for ACE inhibition, only non-hydrolyzed goat plasma and its hydrolysates by thermolysin showed ACE inhibitory activity (9.86±5.03% and 21.77±3.74%). In conclusion, goat plasma without hydrolyzation and its hydrolysates can be a good source of bioactive compounds with functional characteristics, whereas cattle plasma has a relatively low value. Further studies on the molecular structure of these compounds are needed with more suitable enzyme combinations.

• 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.