• 한국세라믹학회지
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• 제40권6호
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• pp.608-614
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• 2003

pH 9.1, 9$0^{\circ}C$, 6시간의 조건에서 $\alpha$-tricalcium phosphate ($\alpha$-Ca$_3$(PO$_4$)$_2$)의 가수분해반응에 의해서 잘 발달된 수산화아파타이트 휘스커상 (길이 5$mu extrm{m}$,지름 0.5$\mu\textrm{m}$)이 합성되었다 수산화아파타이트로 $\alpha$-Ca$_3$(PO$_4$)$_2$의 전환에 미치는 반응조건(온도, 시간, pH)의 영향이 조사되었다. 아울러 XRD, SEM, ICP, TGA와 같은 분석기기를 사용하여 수산화아파트의 미세구조, 조성, 열적 안정성을 검토하였다.

• 자원리싸이클링
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• 제11권2호
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• pp.14-19
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• 2002

PVC(polyvinyl chloride)sheet를 NaOH수용액 중에서 반응온도 $80~150^{\circ}C$, 반응시간 0~7시간으로 처리하여 가소제의 침출에 관해서 검토하였다. DOP의 가수분해에 의해서 생성된 프탈산 수율은 알카리촉매로써 NaOH농도의 증가와 온도의 상승으로 인해 증가하고, $150^{\circ}C$, 10M NaOH, 3시간이상에서 프탈산 수율은 거의 100%,에 달했다. 따라서 PVC sheet에 30% 포함되어져 있는 가소제는 알카리수용액 중에서 탈염화수소가 일어나기 이전에 가수분해되어졌다. 또한, PVC필름의 수열처리에서는 DOP의 가수분해로 인해 세공이 생성되었다.

• 한국세라믹학회지
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• 제36권7호
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• pp.691-697
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• 1999

TiO2 powder was adsorbed on the surface of mica using the heterocoagulation method in water TiO2 powder was prepared from hydrolysis of titanium-iso propoxide in a mixed solvent of anhydrous ethanol and water. When the molar ratio of water to titanium iso-propoxide was 0.25 monodispersed spherical TiO2 particles were obtained. The prepared TiO2 powder showed anatase phase after heat treatment at 50$0^{\circ}C$ for 2 h and then transformed to rutile phase after heat treatment at 100$0^{\circ}C$ for 2h. The iso-electric points of TiO2 and Mica were pH 3.9 and pH 3.25 respectively which were measured by the Z-potential analysis in water base. The maximum Z-potential difference between two powders was observed in the range of pH 3.6~3.7 TiO2 powder was adsorbed on the surface of mica by heterocoagulation method in pH 3.6~3,7 The properties of prepared TiO2 powder was haracterized by TG-DTA, XRD and SEM The morphology and thermal properties of TiO2-adsorbed mica were examined.

• Bulletin of the Korean Chemical Society
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• 제22권8호
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• pp.872-876
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• 2001

Topological changes caused by the alkaline and enzymatic attacks of solution-grown, chain-folded lamellar crystals (SGCs) of poly[(R)-3-hydroxybutyrate] P(3HB) have been studied in order to investigate the chain-folding structure in P(3HB) crystal regions. NaOH and an extracellular PHB depolymerase purified from Alcaligenes faecalis T1 were used for alkaline and enzymatic hydrolysis, respectively. The measurements were performed on crystals attached to a substrate which is inactive to degradation mediums. Both alkaline and enzymatic attacks lead to a breakup of the lamellar crystals along the crystallographic b-axis during initial erosion. Since hydrolysis preferentially occurs in amorphous regions, this morphological result reflects relatively loosely packed chains in core parts of lamellar crystals. Additionally, it was supported by the ridge formation along the b-axis in the lamellar crystals after thermal treatment at a low temperature because of the thermally sensitive nature of the loosely packed chains in lamellar crystals. However, the alkaline hydrolysis accompanied the chain erosions or scissions in quasi-regular folded lamellar surfaces due to smaller size of alkaline ions in comparison to the enzyme, resulting in the decrease of molecular weight.

• Bulletin of the Korean Chemical Society
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• 제10권6호
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• pp.600-604
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• 1989

In order to find the rational methods for improving the thermal stability of subtilisin Carlsberg, the mechanisms of irreversible thermoinactivation of the enzyme were studied at $90^{\circ}C.$ At pH 4, the main process was hydrolysis of peptide bond. This process followed first order kinetics, yielding a rate constant of $1.26\;{\times}\;10^{-1}h^{-1}$. Hydrolysis of peptide bond of PMS-subtilisin occurred at various sites, which produced new distinct fragments of molecular weights of 27.2 KD, 25.9 KD, 25.0 KD, 22.3 KD, 19.0 KD, 17.6 KD, 16.5 KD, 15.7 KD, 15.0 KD, 13.7 KD, and 12.7 KD. Most of the new fragments originated from the acidic hydrolysis at the C-side of aspartic acid residues. However 25.0 KD, 15.7 KD, and 13.7 KD which could not be removed in purification steps stemmed from the autolytic cleavage of subtilisin. The minor process at pH 4 was deamidation at asparagine and/or glutamine residues and some extend of aggregation was also observed. However, the aggregation was main process at pH 7 with a first order kinetic constant of $16 h^{-1}.$ At pH 9, the main process seemed to be combination of deamidation and cleavage of peptide bond.

• 대한환경공학회지
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• 제38권3호
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• pp.110-116
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• 2016

최근 다양한 형태의 슬러지 최종처리 기술들이 제안되고, 기존 혐기성 소화공정에서 바이오가스 생산효율을 증가시키기 위한 전처리 기술들이 개발되어왔다. 이들 기술 중 열적전처리(Thermal pretreatment) 기술은 기존 슬러지 처리방법과 다르게 입자의 유기성 성분을 용해시킴으로써 슬러지 특성을 변화시켜 감량과 재이용이 가능한 전처리 기술이다. 그러나 대부분의 연구들은 높은 온도에서 입자의 가수분해, COD 가용화부분에 중점을 두고 연구 되어졌으며, 소수의 결과들만이 물리, 화학적 특성변화에 대해서 보고되었다. 본 연구는 열적전처리 효율에 영향을 미칠 수 있는 온도, 약품이 탄소원 형성과 분율에 미치는 영향을 알아보고자 하였다. 그 결과 반응온도가 증가함에 따라 입자의 가수분해 속도가 증가하였으며, 산화제의 주입량이 증가 할수록 고분자 유기성 물질은 감소하고 저분자 유기성 물질(분자량 350 g/mol 이하)의 분율이 증가하는 것을 확인할 수 있었다. 이번 실험결과는 슬러지 감량화 및 재이용를 위한 열적 전처리에 의한 분자의 특성을 파악하는데 기여할 수 있을 것이라 판단한다.

• 한국미생물생명공학회:학술대회논문집
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• 한국미생물생명공학회 1986년도 추계학술대회
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• pp.523.2-523
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• 1986

The hydrolysis of olive oil was attempted with immobilized C. rugosa lipase in the reverse phase solvent system. (i.e. immobilized wet particles is dispersed in continuous phase olive oil or organic solvents containing olive oil). Sephadex LH-20 and LH-60 were used as the supports that can be used in organic solvents. The water content of wet particles of sephadex LH-20 and LH-60 were about 72% (w/w) and 85% (w/w), respectively Both swollen gels with 0.05M buffers adsorbed about 18% of lipase dissolved. They were easily dispersed in liquid olive oil or in organic solvents. The effects of organic solvents on the stability and catalytic activity of the lipase have been examined. The results revealed that isooctane is superior to the other solvents examined for enzymatic fat spliting in reverse phase system. Kinetics of enzymatic hydrolys of olive oil by immobilized lipase has been investigated in a batch reactor. Effects of pH and temperature on the lipase were studied. The substrate concentration was influenced positively on the thermal stability.

• 한국식품영양학회지
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• 제34권1호
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• pp.26-35
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• 2021

Myrosinases (thioglucosidases) catalyze the hydrolysis of a class of compounds called glucosinolates, of which the aglycones show various biological functions. It is often necessary to minimize the loss of myrosinase activity during thermal processing of cruciferous vegetables. Myrosinase was isolated from a popular spice, white mustard (Sinapis alba), and its thermal inactivation kinetics was investigated. The enzyme was extracted from white mustard seeds and purified by a sequential processes of ammonium sulfate fractionation, Concanavalin A-Sepharose column chromatography, and gel permeation chromatography. At least three isozymes were revealed by Concanavalin A-Sepharose column chromatography. The purity of the major myrosinase was examined by native polyacrylamide gel electrophoresis and on-gel activity staining with methyl red. The molecular weight of the major enzyme was estimated to be 171 kDa. When the consecutive step model was used for the thermal inactivation of the major myrosinase, its inactivation energy was 44.388 kJ/mol for the early stage of destruction and 32.019 kJ/mol for the late stage of destruction. When the distinct two enzymes model was used, the inactivation energy was 77.772 kJ/mol for the labile enzyme and 95.145 kJ/mol for the stable enzyme. The thermal inactivation energies lie within energy range causing nutrient destruction on heating.

• The Korean Journal of Ceramics
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• 제1권1호
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• pp.1-6
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• 1995

Submicrometer, monosized ceramic powder of $Al_2TiO_5$$Al_2O_3$ ethanolic solutions. All particles produced by sol-gel-process were amprphous, monodispersed and with a narrow particle-size distribution. Compacts fired above $1300^{\circ}C$ formed aluminium titanate. Mullite formed first at $1480^{\circ}C$. After decomposition test at $1100^{\circ}C$, and cyclic thermal decomposition test at 750-1400-$750^{\circ}C$ for 100hrs., aluminium titanate was well stablized by composition with mullite.

• 한국작물학회지
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• 제51권2호
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• pp.148-153
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• 2006

Effects of ${\alpha}$-chymotrypsin modification on degree of hydrolysis (DH), solubility, emulsifying capacity and thermal aggregation of laboratory-purified soy protein isolate (SPI) using a lipoxygenase-defected soybean (Jinpum-kong) and commercial soy protein isolate (Supro 500E) were compared. SPIs were hydrolyzed by ${\alpha}$-chymotrypsin at pH 7.8 and $37^{\circ}C$ for 30 min. DHs of Supro 500E and Jinpum-kong SPI were increased by ${\alpha}$-chymotrypsin modification, and DH of Supro 500E was higher than that of Jinpum-kong SPI. DH of ${\alpha}$-chymotrypsin treated Jinpum-kong SPI was similar with untreated Supro 500E and DH of treated Supro 500E was the highest. Solubility, emulsifying capacity and thermal aggregation of SPIs were increased by ${\alpha}$-chymotrypsin modification, and these changes were highly related to changes in DH. Functional properties of Supro 500E were higher than Jinpum-kong SPI in both of untreated and ${\alpha}$-chymotrypsin treated SPIs.