• KSBB Journal
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• v.5 no.4
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• pp.383-390
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• 1990

Alcoholic distillery waste was utilized as dual purposes to produce citric acid and to reduce the amount of waste to be treated. Enzyme and acid hydrolysis of this waste were studied to suggest effective way of present purpose. Enzymatic hydrolysis of this naked barley alcoholic distillery waste by $\alpha$-and $\beta$-amylase gave glucose as 8g/l concentration at $55^{\circ}C$ for 6 hours, which produced 1g/l citric acid and 5.33g/l mycelial. This waste material hydrolyzed with 25% HCl at $120^{\circ}C$ showed 21.5g/l glucose and produced 1.75g/l citric acid with 4.9g/1 mycelial. The glucose concentration was decreased to 3.44g/l by further 2nd acid hydrolysis because the monosugars were decomposed at prolonged hydrolysis conditions. The addition of 3g/l $NH_4NO_3$ increased the mycelial growth but reduced the amount of citric acid formed. The formation of citric acid was increased at low concentration of manganese ion.

• Journal of Microbiology and Biotechnology
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• v.18 no.8
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• pp.1401-1407
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• 2008

The roles of conserved amino acid residues (Va1329-Ala330-Asn331-Glu332), constituting an extra sugar-binding space (ESBS) of Thermus maltogenic amylase (ThMA), were investigated by combinatorial saturation mutagenesis. Various ThMA mutants were firstly screened on the basis of starch hydrolyzing activity and their enzymatic properties were characterized in detail. Most of the ThMA variants showed remarkable decreases in their hydrolyzing activity, but their specificity against various substrates could be altered by mutagenesis. Unexpectedly, mutant H-16 (Gly-Leu-Val-Tyr) showed almost identical hydrolyzing and transglycosylation activities to wild type, whereas K-33 (Ser-Gly-Asp-Glu) showed an extremely low transglycosylation activity. Interestingly, K-33 produced glucose, maltose, and acarviosine from acarbose, whereas ThMA hydrolyzed acarbose to only glucose and acarviosine-glucose. These results propose that the substrate specificity, hydrolysis pattern, and transglycosylation activity of ThMA can be modulated by combinatorial mutations near the ESBS.

• Proceedings of the Korean Vacuum Society Conference
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• 2012.02a
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• pp.557-557
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• 2012

Silicatein-${\alpha}$, the enzyme extracted from silica spicules in glass sponges, has been studied extensively in the way of chemistry from 1999, in which the pioneering work by Morse, D. E. - the discovery of the enzymatic hydrolysis in Silicatein-${\alpha}$ - was published. Since its reaction conditions are physiologically favored, synthesis of various materials, such as gallium oxide, zirconium oxide, and silicon oxide, was achieved without any hazardous wastes. Although some groups synthesized oxide films and particles, they have not achieved yet controlled morphogenesis in the reaction conditions mentioned above. With the knowledge of catalytic triad involved in hydrolysis of silicone alkoxide and oligomerization of silicic acid, we designed the novel peptide amphiphiles to not only form self-assembled structure, but also display similar activities to silicatein-${\alpha}$. Designed templates were able to self-assemble into left-handed helices for the peptide amphiphiles with L-form amino acid, catalyzing polycondensation of silicic acids onto the surface of them. It led to the formation of silica helices with 30-50 nm diameters. These results were characterized by various techniques, including SEM, TEM, and STEM. Given the situation that nano-bio-technology, the bio-applicable technology in nanometer scale, has been attracting considerable attention; this result could be applied to the latest applications in biotechnology, such as biosensors, lab-on-a-chip, biocompatible nanodevices.

• Journal of the Korean Applied Science and Technology
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• v.33 no.1
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• pp.176-185
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• 2016

Yeonsan Ogae has been known as supporting health and high efficacy of treatment. In recent days, as the efficacy of functional peptides has known, the optimization of oligo peptides production and its characteristics from Ogae legs has been performed. Response surface method was used to perform the optimizaion of enzyme hydrolysis. The range of processes was temperature ( 40, 50 and $60^{\circ}C$), pH( pH 6.0, 7.0 and 8.0 ), and enzyme( 1, 2 and 3% ). The degree of hydrolysis, amino acids, molecular weight of products were analyzed. The optimum process of enzyme hydrolysis were determined as temperature $58^{\circ}C$, pH 7.5, and enzyme concentration 3%. At optimum conditions, the degree of hydrolysis after 2 h reaction was 75-80%. The amino acid and were 168.131 mg/100 g, respectively. The molecular weight of products by using MALDI-TOF was ranged from 300 to 1,000 Da.

• Food Engineering Progress
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• v.15 no.1
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• pp.41-47
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• 2011

The defatted rice bran (DRB) was enzymatically hydrolyzed using eight commercial proteases for 4hr at optimum pH and temperature. Proteolytic hydrolysates were examined in supernatant and precipitate using lowry, semimicro kjeldahl and gravimetric method using weight difference before and after enzymatic hydrolysis. In lowry and kjeldahl protein assay method, two proteases (Alcalase and Protease N) were found to be the most effective enzymes. In gravimetric method, 60.6~118.3 mg protein/g DRB was hydrolyzed after eight commercial proteases treatments. Similar to lowry and kjeldahl method, 118.3 and 107.1 mg protein/g DRB were hydrolyzed after Alcalase and Protease N treatments, respectively. When two or three effective proteases (Protamex, Alcalase and Protease N) were applied at one time to obtain synergistic effect, significant increase (P<0.05) was observed when three proteases were applied at one time (63.4 mg protein/g DRB in lowry method and 204.5 mg protein/g DRB in gravimetric method). This result suggests that Alcalase and Protease N were the most effective enzymes for proteolysis of DRB and three commercial enzymes (Protamex, Alcalase and Protease N) showed the synergistic effect on the hydrolysis of DRB.

• Korean Journal of Food Science and Technology
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• v.43 no.6
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• pp.729-734
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• 2011

With the goal of transforming rice protein from an insoluble to a soluble form to increase the industrial utilization of rice wine meal (RWM), RWM was derivatized using commercial proteases and the RWM hydrolysates were characterized. Eight commercial proteases were used individually or in combination for hydrolysis of RWM. The degree of hydrolysis was assessed by determining the soluble protein in supernatant using the Lowry assay, protein in precipitates using a semimicro Kjeldahl procedure, and gravimetrically by the weight difference before and after hydrolysis. Protamex, Alcalase and Protease N proteases were most effective for hydrolysis of RWM. Although these assessment methodologies displayed some variation, they generally showed a similar pattern. When the aforementioned three proteases were simultaneously used to treat RWM, no significant difference was observed between the three assays (p<0.05) indicating an absence of enzymatic synergy.

• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.720-725
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• 2000

To reduce the antigenicity of egg white (EW), EW was treated with several proteolytic enzymes, trifluoromethanesulfonic acid (TFMS), heat, and NaOH. Competitive indirect enzyme-linked immunosorbent assay (ciELISA), using rabbit anti-EW antibody, was performed to examine the antigenicity of the treated EW's. Enzymatic hydrolysis gave no good effect on the reduction of the antigenicity of EW. Neither did the pretreatment with ${\gamma}-irradiation$ before the hydrolysis reduce the antigenicity. TFMS treatment removed the antigenicity of EW. The antigenicity of EW heated at $120^{\circ}C$ for 30 min or treated with NaOH at 0.3% (w/v) and more, decreased to less than 1/10,000 as compared with that of native EW. The combinatory treatment with NaOH, followed by heat at $70^{\circ}C$ for 15 min had a synergic effect on the reduction of the antigenicity of EW.

• Applied Biological Chemistry
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• v.48 no.3
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• pp.292-295
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• 2005

Synthesis of methyl 3-methyloctanoate, a perfume component isolated from African orchid Aerangis confusa (or Aerangis kirkii) was achieved starting from itaconic acid in 9 steps. Itaconic acid is one of the cheapest organic compounds which is the fermentation product of microorganism Asp. terreus. As the key intermediate, 2-methyl-1,4-butanediol 4-acetate was obtained through the enzymatic regioselective hydrolysis of 2-methyl-1,4-butanediol diacetate with lipase. After Grignard reaction and oxidation, 3-methyloctanoic acid was obtained and converted to the various corresponding scented esters with a variety of alkyl alcohols, and the resulting fragrancy esters are expected to be utilized as the aroma additive materials in cosmetics, drinks and foods.

• Food Science and Preservation
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• v.31 no.3
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• pp.444-451
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• 2024

This study aimed to investigate the characteristics of protein hydrolysates derived from defatted egg yolk using various proteolytic enzymes and compare the antioxidant activity of the resulting hydrolysates. The defatted egg yolk powder was subjected to enzymatic hydrolysis using four different proteases (alcalase, bromelain, flavourzyme and neutrase), and the resulting hydrolysates were evaluated for their antioxidant properties. Through analysis of available amino group contents and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it was observed that the defatted egg yolk powder treated with alcalase, flavourzyme, and neutrase for 12 h exhibited a high degree of hydrolysis value. Based on the RC₅₀ values obtained from two different antioxidant analyses, all hydrolysates showed comparable antioxidant activity, except for the alcalase hydrolysate, which demonstrated notably higher scavenging activity against hydrogen peroxide than the other hydrolysates. These findings suggest the potential of protein hydrolysates from defatted egg yolk, a by-product of lecithin extraction, as natural antioxidants.

• Journal of the Korean Wood Science and Technology
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• v.15 no.4
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• pp.18-25
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• 1987

The cellulolytic activities of Aspergillus fumigatus KC-1 was investigated, which showed the most active producer of cellulase among the 256 strains of cellulose-decomposing microorganisms screened in our laboratory. All the examined cellulolytic activities (filter paper-, Avicel-, cotton-, CMC-, salicin- and xylansaccharifying activity) in a culture of A. fumigatus KC-1 grown on 1% popular sawdust pretreated with peroxide alkaline reached a maximum within 4-5 days. The optimum pH and temperature for the enzymatic activity was found to be pH 4.5 and $60^{\circ}C$ respectively. The sawdust of poplar wood delignified with 1% NaOH and 20% peracetic acid succesively recorded the highest hydrolysis rate in the tests of enzymatic saccharification. The major end product of hydrolysis of poplar wood with the cellulolytic enzymes obtained from A. fumigatus KC-1 was glucose with small amount of cellobiose and xylose. It can be concluded from these results that A. fumigatus KC-1 is an advantagous source of a cellulase that is capable of hydrolyzing cellulose to glucose rapidly. The influence of degree of delignification, substrate size and its concentration on the rate of hydrolysis of poplar wood was also discussed.