• Journal of Life Science
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• v.20 no.12
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• pp.1906-1909
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• 2010

Acid and halide ion catalyses for the hydrolysis of benzenesulfinamides were kinetically investigated. The rates of hydrolysis increased with increasing concentration of both acid and halide ions and also showed to speed up as the electron donating ability of the benzenesulfinyl moiety and the electron withdrawing ability in the leaving group increased. The reactivity of halide ions was in the order of $Br^-$ > $Cl^-$. The reaction mechanism may be accommodated by including a hypervalent intermediate and sulfonium cation.

• Korean Chemical Engineering Research
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• v.45 no.3
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• pp.291-297
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• 2007

The hydrolysis reaction of sulfur mustard(HD, bis 2-chloroethylsulfide), one type of the blister agents was studied in water to find the operation conditions which can convert HD into less toxic compounds. The reaction was proceeded into two steps. First, 10~20 wt% of HD was hydrolyzed in water at $90^{\circ}C$ for 2 hr and aqueous sodium hydroxide solution(2.1 eq) was subsequently added to the reaction mixture at room temperature. The efficiency of HD hydrolysis at this experimental conditions was greater than 99.99% and the final degradation products of HD were 68 wt% of thiodiglycol, 8 wt% of 1,2-bis(2-hydroxyethylthio)ethane and 24 wt% of bis(2-hydroxyethylthioethyl)ether.

• Korean Journal of Food Science and Technology
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• v.47 no.6
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• pp.772-778
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• 2015

Hydrolysis of isolate soybean protein (ISP) using subcritical water (SCW) was conducted to study the feasibility for producing protein hydrolyzate. SCW hydrolysis of SPI suspension (5-15%) was conducted in an electrically heated batch reactor (2 L). The effects of temperature (230 to $270^{\circ}C$) and holding time (10 to 50 min) on the degree of hydrolysis (DH) and the production of amino acids were studied by surface response method. The DH was determined by derivatizing the hydrolyzates with ortho-phthalaldehyde (OPA) solution. It was confirmed that reaction temperature and holding time affected the hydrothermolysis of soybean protein. However, the holding time was less effective on amino acid yield when the temperature was higher than $230^{\circ}C$. In order to achieve optimal yields of amino acids exceeding 43%, the temperature should be within the range between 256 and $268^{\circ}C$ with holding time from 29 to 41 min, respectively. A maximum estimated amino acid yield of 43.5% was obtained at $268^{\circ}C$ for 35 min.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.26 no.2
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• pp.120-132
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• 1993

A continuous hollow fiber membrane reactor(CHFMR) was developed and optimized for the production of yellowfin sole(Limanda aspera) skin gelatin hydrolysates using trypsin. The results were summerized as follows: The $K_m$ value of the CHFMR was 2.4 times higher than that of the batch reactor, indicating reduced enzyme affinity for the substrate. The $K_2$ value of the CHFMR was 8.5 times lower than that of the batch process, showing a significant reduction in trypsin activity in the CHFMR. The optimum operating conditions for the CHFMR process were $55^{\circ}C$, pH 9.0, flux 7.79 ml/min, residence time 77min, and trypsin to substrate ratio, 0.01(w/w) After operating for 60min under the above conditions, $79\%$ of the total amount of initial gelatin was hydrolysed. Enzyme leakage was observed through the 10,000 MWCO membrane after the 20min of reactor operation, while none occurred after 5hr. Total enzyme leakage was about $12.95\%$ at $55^{\circ}C$ for 5hrs. However, there was no apparent correlation between enzyme leakage and substrate hydrolysis. The membrane has a significant effect on trypsin activity loss for 60min of the CHFMR operation. The CHFMR operating with the membrane lost $34\%$ of the initial activity versus a $23\%$ loss of activity after 3hr in the continuous reactor lacking the hollow fiber membrane. The measurement of fouling property showed that relative flux reduction was $91\%$ and flux recover rate was $92\%$ at $10\%$ substrate solution. The productivity(378.85mg product/mg enzyme) of the CHFMR was more than 4 times higher than that of the batch reactor at $55^{\circ}C$.

• Proceedings of the Korean Society of Tribologists and Lubrication Engineers Conference
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• 2001.06a
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• pp.162-177
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• 2001

The hydrolysis rates of seven kinds of polyol ester base oils 〔POEs〕 of different branch shape were investigated by using a simple apparatus under mild acidic condition. Seven polyol ester base oils were made of poly hydric alcohols of two-four valence, normal or branched fatty acids of different carbon number. p-Toluene sulfonic acid was used as acid catalyst to accelerate the rate of hydrolysis. Partial esters and fatty acid produced by sequential hydrolysis of POEs were identified and their concentrations were determined by calibrated-internal standard method using Gas Chromatography. The rate constants of each step in sequential hydrolysis were determined by the least square method from rate equation and the concentration of each component, were compared with one another. It was shown that the rate of hydrolysis of POEs was strongly affected by whether molecular structure of fatty acid was straight chain or branch chain and which position was branched. The hydrolysis stability for all the POEs can be reasonably explained by using a steric hindrance effect anticipated fi:om their molecular structures affecting as water molecule makes an attack on the carbonyl carbon of POEs.

• Applied Chemistry for Engineering
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• v.3 no.1
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• pp.119-129
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• 1992

The rates of mass transfer with the alkaline hydrolysis of ethyl acetate and n-butyl acetate were measured by using a modified Lewis cell. The rates of mass transfer with chemical reaction were independent of the speed of agitation, and the reaction enhancement factors were independent of the ionic strength. The second order reaction rate constants of ethyl acetate and n-butyl acetate could be obtained from an approximate solution of a diffusion equation by film theory, and their values were $0.041m^3/kg\;mol{\cdot}s$ and $0.338m^3/kgmol{\cdot}s$, respectively.

• Proceedings of the Korean Fiber Society Conference
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• 2002.04a
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• pp.191-194
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• 2002

완전히 가수분해 된 폴리비닐알콜(PVA)는 쉽게 결정화되기 때문에 일부 가수분해된 PVA보다 에멜전 안정화와 계면활성이 약하다$^{1)}$ . 이러한 성질을 개선하려면 폴리비닐알콜분자에 hydrophobic한 알킬기를 도입하는 것이 주요한 방법이다. 폴리비닐알콜 분자에 긴 알킬기를 도입하는 방법에는 chain transfer 반응을 통하여 폴리비닐아세테이트(PVAc)분자의 말단에 긴 알킬기를 도입한 후 가수분해하는 방법$^{1)}$ ; 비닐아세테이트 (VAc)가 긴 알킬리를 가진 비닐 단량체와 copolymerization 한 후 가수분해하는 방법 $^{2),3)}$ ; 합성된 PVA가 긴 알킬리를 긴 알킬리를 가진 acyl chloride와 직접 반응하여 얻는 방법$^{4)}$ 등이 있다. (중략)

• Journal of the Korean Applied Science and Technology
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• v.34 no.2
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• pp.338-348
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• 2017

Protein hydrolysates derived from plants and animals having antioxidant, suppression of hypertension, immunodulatory, alleviation of pain, and antimicrobial activity has been known as playing important role like hormone. This study was performed to optimize the hydrolysis of protein of sea of cucumber by a flavourzyme. The ranges of processes were the reaction temperature of 40 to $60^{\circ}C$, pH 6 to 8, and enzyme concentration 0.5 to 1.5%(w/v). As a result, the optimization of process was determined at temperature of $48-50^{\circ}C$, pH of 7.0-7.2, and enzyme concentration of 1.0-1.1%(w/v), and degree of hydrolysis was 43-45 at above conditions. The molecular weight of hydrolysate was distributed to 500-3,500 Da and showed typical peptides. Inhibition concentration ($IC_{50}$) of peptides of DPPH radical scavenging activity, Superoxide anion radical scavenging activity, Hydroxy radical scavenging activity, $Fe^{2+}$ cheating activity was 1.25, 3.40, 10.3, and 22.11 mg/mL, respectively. Therefore, we expect that those products are useful as functional food ingredients.

• Journal of the Korean Applied Science and Technology
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• v.33 no.2
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• pp.293-303
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• 2016

Protein hydrolysate that shows physiological function such as antioxidant, suppression of hypertension, immunodulatory, alleviation of pain, and antimicrobial activity has been known as playing important role like hormone. This study was performed to optimize the hydrolysis of the wing's meat of Yosan-Ogae by a commercial protease. The ranges of processes were the reaction temperature of 40 to $60^{\circ}C$, pH 6 to 8, and enzyme concentration 1 to 3%(w/v). As a result, the optimization of process was determined at temperature of $48-50^{\circ}C$, pH of 7.0-7.2, and enzyme concentration of 3%(w/v), and degree of hydrolysis was 68 to 69% at above conditions. The molecular weight of hydrolysate was distributed to 500-1,200 Da and showed typical peptides. The amino acids of peptides showing presumably antioxidant activity such as histidine, proline, methionine, cystein, tyrosine, tryptophan, phenylalanine comprised about 43.07%. The glutamic acid was 13.6%. Therefore, we expect that those products are useful as functional food ingredients.

• Journal of the Korean Chemical Society
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• v.18 no.6
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• pp.430-436
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• 1974

The rate constants of hydrolysis of 1,1-dicyano-2-p-dimethylaminophenyl-2-chloroethylene(DPC) were determined at various pH and the rate equation which can be applied over wide pH range is obtained. From the rate equation the mechanism of the hydrolysis of a DPC over wide pH range is fully explained; below pH 3 and above pH 7.5, the rate constant is proportional to the concentration of hydronium ion and hydroxide ion, respectively. However, in the range of pH 3 to 7.5, water, hydronium ion and hydroxide ion catalyze the hydrolysis of DPC.