• 제목/요약/키워드: Temperature-dependent Hydrolysis

검색결과 32건 처리시간 0.024초

만니톨의 효소 가수분해 반응 조건 최적화 (Optimization for Enzymatic Hydrolysis of Mannitol)

  • 박은영;김용진;정승미;이동훈
    • KSBB Journal
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    • 제28권2호
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    • pp.65-73
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    • 2013
  • This study aimed to investigate the enzymatic hydrolysis of mannitol using Viscozyme$^{(R)}$ L, Celluclast$^{(R)}$ 1.5 L, Saczyme$^{(R)}$, Novozym$^{(R)}$, Fungamyl$^{(R)}$ 800 L, Driselase$^{(R)}$ Basidiomycetes sp., and Alginate Lyase, and to optimize of reaction conditions for production of reducing sugar. Response surface methodology (RSM) based on central composite rotatable design was used to study effects of the independent variables such as enzyme (1-9% v/w), reaction time (10-30 h), pH (3.0-7.0) and reaction temperature ($30-70^{\circ}C$) on production of reducing sugar from mannitol. The coefficient of determination ($R^2$) of $Y_1$ (yield of reducing sugar by Viscozyme$^{(R)}$ L) and $Y_3$ (yield of reducing sugar by Saczyme$^{(R)}$) for the dependent variable regression equation was analyzed as 0.985 and 0.814. And the p-value of $Y_1$ and $Y_3$ showing 0.000 and 0.001 within 1% (p < 0.01), respectively, was very significant. The optimum conditions for production of reducing sugar with Viscozyme$^{(R)}$ L were 9.0 % (v/w) amount of enzyme, 30.0 hours of reaction time, pH 4.5 and $30.0^{\circ}C$ of reaction temperature, and those with Saczyme$^{(R)}$ were 9.0% (v/w) of amount of enzyme dosage, 30.0 h of reaction time, pH 7.0 and $30.0^{\circ}C$ of reaction temperature, consequently, the predicted reducing sugar yields were 22.5 and 27.9 mg/g-mannitol, respectively.

고온, 고압 가수분해반응에 의한 우지 분해공정: 반응표면분석법을 이용한 반응조건의 최적화

  • 김원호;김용민;김호중;허병기
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2001년도 추계학술발표대회
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    • pp.303-307
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    • 2001
  • 반응표면분석법을 이용하여 우지의 고온, 고압가수분해 공정조건을 최적화 시키고자 하였다. 이때 선정된 공정의 독립변수로는 반응온도, 반응압력 그리고 fat/water ratio이었으며 이에 대한 중속변수로는 TG, FFA, 1,3-DG, 2,3-DG 그리고 MG을 선정하였다. 반응압력을 이산화탄소를 이용하여 가수분해반응속도를 증가시키고자 하였지만 지방산 생성농도에는 커다란 영향을 미치지는 않았다. 지방산 생성농도에 대해서는 다른 공정변수들에 비해 반응온도에 크게 의존하였고, Derringer-Suich 방법을 이용한 지방산 생성농도를 최적화 시킬 수 있는 조건으로는 반응온도 $271^{\circ}C$ 반응압력 86 bar 그리고 far/water ratio 106.08g/133.92g를 얻었으며 이 조건에서 3시간동안 가수분해하여 얻은 FFA생성농도는 96.49%로 얻었다. 통계적 분석에 이용된 자료들은 유의성 검증, 적합결여, 그리고 잔차분석 등을 해석한 결과 모든 자료가 95%이상의 신뢰도를 가지므로 매우 유익한 것으로 사료된다.

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역미셀계내에서 인지질분해효소 $A_2$에 의한 레시친의 가수분해 (Hydrolysis of Phosphatidylcholine in Aerosol-OT/Isooctane Reversed Micelles by Phospholipase $A_2$)

  • 장판식
    • 한국식품과학회지
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    • 제29권1호
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    • pp.26-31
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    • 1997
  • 물을 극미량 함유하는 미수계 효소반응계인 aerosol-OT/이소옥탄으로 구성된 역미셀계내에서 레시친의 일종인 DPPC (dipalmitoyl phosphatidylcholine)의 가수분해반응을 phospholipase $A_2$가 촉매할 수 있었다. 또한 phospholipase $A_2$에 의한 가수분해반응을 정량분석하기 위한 고성능 액체 크로마토그래피에 의한 예민하고 간편한 방법을 고안하였는 바, 이에 의하여 aerosol-OT/이소옥탄 역미셀계내에서 phospholipase $A_2$에 의한 가수분해반응의 동력학적인 분석이 가능하였다. 한편, 여러가지 유화제와 유기용매 중 aerosol-OT와 이소옥탄일 때 효소반응이 가장 효과적이었으며, 반응 적정온도는 $35{\sim}40^{\circ}C$, 적정 pH는 7.0이었다. 또한 역미셀계내에서의 가수분해반응은 수분 함량변화에 민감하였으며, R-값(=[water]/[aerosol-OT])이 10.0일 때 가장 높은 효소활성을 나타내었다. 효소반응을 위한 최적조건하에서의 $K_{m,app.}$$V_{max.,app.}$는 각각 8.73 mM, 2.83 units/㎎ protein이었으며, 역미셀계내에서 phospholipase $A_2$에 의한 DPPC가수분해반응의 활성화에너지는 12.31 kcal/mole로 산출되었다.

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폴리아크릴로니트릴의 가수분해와 아미드화에 의한 열감응성 폴리(N-이소프로필아크릴아미드)의 합성과 특성분석 (Synthesis and Characterization of Thermo-responsive Poly(N-isopropylacrylamide) via Hydrolysis and Amidation of Poly(acrylonitrile))

  • 이희동;김영호
    • 폴리머
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    • 제37권6호
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    • pp.784-793
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    • 2013
  • 폴리아크릴로니트릴(PAN) 섬유로 된 제품에 열감응 특성을 부여하기 위하여, PAN을 가수분해하여 카복실기를 생성시키고 이를 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride(EDC)와 N-히드록시석신이미드(NHS)를 촉매로 하여 이소프로필아민(IPA)과 반응시켜 열감응성 고분자인 폴리(N-이소프로필아크릴아미드) (PNIPAAm)로 전환시키는 방법에 대해 연구하였다. PAN을 알칼리 가수분해시킨 후 산 가수분해를 추가하여 카복실기 함량을 늘릴 수 있었다. 폴리아크릴산(PAA)과 IPA와의 아미드화 반응은 촉매인 EDC와 NHS의 양에 의존하며, PAA 단위가 약 53% 이상 PNIPAAm으로 전환되어야 하한임계용액온도(LCST) 거동을 나타냈다.

결합제의 종류와 양에 따라 분무건조된 페라이트 분말의 성형특성 (Dependence of Compaction Behavior of Spray-Dried Ferrite Powders on the Kinds and Concentrations of Binder Systems)

  • 홍대영;변순천;제해준;홍국선
    • 한국세라믹학회지
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    • 제32권9호
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    • pp.1047-1055
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    • 1995
  • Mn-Zn ferrite granules were formed by a spray-drying method of the slurry containing different kinds and concentrations of binders at various temperatures. The slurry was made by conventional ceramic processing method, that is, by mixing Fe2O3, MnO, ZnO powders (52 : 24 : 24 mol%), calcining and milling. Typical shape of the spray dried granules was spherical. The compaction behavior of these granules was dependent on the spray-drying temperature and the kind and concentration of binders. At lower pressure the granules were displaced and at higher pressure the granules were deformed and fractured to fill pores among the granules. The optimum concentration of the binder was 0.5wt%. The granules containing 0.5wt% PVA 205 were deformed and fractured well and the green density was higher than others. At higher concentrations of the binder the granules were deformed rather than fractured, therefore the green density was lowered because of the remaining unfilled pores. The decomposition temperature and the heat released were increased with increasing the concentration of the binders. The compaction response of the granules containing PVA 205 was more efficient than those containing PVA 217 and PVA 117. Green density was not dependent on the degree of hydrolysis of the binders. The compaction response of the granules spray-dried at 15$0^{\circ}C$ was most efficient.

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Structure and Function of HtrA Family Proteins, the Key Players in Protein Quality Control

  • Kim, Dong-Young;Kim, Kyeong-Kyu
    • BMB Reports
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    • 제38권3호
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    • pp.266-274
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    • 2005
  • High temperature requirement A (HtrA) and its homologues constitute the HtrA familiy proteins, a group of heat shock-induced serine proteases. Bacterial HtrA proteins perform crucial functions with regard to protein quality control in the periplasmic space, functioning as both molecular chaperones and proteases. In contrast to other bacterial quality control proteins, including ClpXP, ClpAP, and HslUV, HtrA proteins contain no regulatory components or ATP binding domains. Thus, they are commonly referred to as ATP-independent chaperone proteases. Whereas the function of ATP-dependent chaperone-proteases is regulated by ATP hydrolysis, HtrA exhibits a PDZ domain and a temperature-dependent switch mechanism, which effects the change in its function from molecular chaperone to protease. This mechanism is also related to substrate recognition and the fine control of its function. Structural and biochemical analyses of the three HtrA proteins, DegP, DegQ, and DegS, have provided us with clues as to the functional regulation of HtrA proteins, as well as their roles in protein quality control at atomic scales. The objective of this brief review is to discuss some of the recent studies which have been conducted regarding the structure and function of these HtrA proteins, and to compare their roles in the context of protein quality control.

Ammonia Volatilization from Rice Paddy Soils Fertilized with 15N-Urea Under Elevated CO2 and Temperature

  • Lim, Sang-Sun;Kwak, Jin-Hyeob;Lee, Dong-Suk;Lee, Sun-Il;Park, Hyun-Jung;Kim, Han-Yong;Nam, Hong-Shik;Cho, Kyeong-Min;Choi, Woo-Jung
    • 한국환경농학회지
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    • 제28권3호
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    • pp.233-237
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    • 2009
  • It has widely been observed that the effect of elevating atmospheric $CO_2$ concentrations on rice productivity depends largely on soil N availabilities. However, the responses of ammonia volatilization from flooded paddy soil that is an important pathway of N loss and thus affecting fertilizer N availability to concomitant increases in atmospheric $CO_2$ and temperature has rarely been studied. In this paper, we first report the interactive effect of elevated $CO_2$ and temperature on ammonia volatilization from rice paddy soils applied with urea. Urea labeled with $^{15}N$ was used to quantitatively estimate the contribution of applied urea-N to total ammonia volatilization. This study was conducted using Temperature Gradient Chambers (TGCs) with two $CO_2$ levels [ambient $CO_2$ (AC), 383 ppmv and elevated $CO_2$ (EC), 645 ppmv] as whole-plot treatment (main treatment) and two temperature levels [ambient temperature (AT), $25.7^{\circ}C$ and elevated temperature (ET), $27.8^{\circ}C$] as split-plot treatments (sub-treatment) with triplicates. Elevated temperature increased ammonia volatilization probably due to a shift of chemical equilibrium toward $NH_3$ production via enhanced hydrolysis of urea to $NH_3$ of which rate is dependent on temperature. Meanwhile, elevated $CO_2$ decreased ammonia volatilization and that could be attributed to increased rhizosphere biomass that assimilates $NH_4^+$ otherwise being lost via volatilization. Such opposite effects of elevated temperature and $CO_2$ resulted in the accumulated amount of ammonia volatilization in the order of ACET>ACAT>ECET>ECAT. The pattern of ammonia volatilization from applied urea-$^{15}N$ as affected by treatments was very similar to that of total ammonia volatilization. Our results suggest that elevated $CO_2$ has the potential to decrease ammonia volatilization from paddy soils applied with urea, but the effect could partially be offset when air temperature rises concomitantly.

유효충돌빈도를 고려한 암모니아 생성 증대기법 연구 (Study on Enhancement of Ammonia Generation for Effective Collision Frequency)

  • 김세진;최용석;박현철
    • 항공우주시스템공학회지
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    • 제17권6호
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    • pp.1-8
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    • 2023
  • 기후변화 대응을 위하여, 항공 분야를 포함한 운송 분야에서 국제온실가스 감축제도 도입 추진 및 대체 에너지 개발 등 환경문제에 대한 연구개발이 활발하다. 그 중 무탄소 에너지원으로 주목받는 암모니아 연료에 대한 관심이 증대되고 있다. 암모니아는 액화 및 운반이 용이하며, 메탄올과 비슷한 에너지 밀도 등의 장점이 있다. 그러나 폭발성 및 독성으로 취급성이 어렵다. 본 연구에서는 암모니아에 비해 취급이 용이한 요소수에 고온의 수분으로 열분해와 가수분해 반응을 유도하여 안정적인 암모니아 발생을 시도하고자 하였다. 암모니아 가수분해 촉진을 위해 고온의 증기를 이용하였고 이론 당량비 미만의 암모니아 발생원인 규명을 하고자 했다. 기체분자운동론에 기인하여 가수분해 촉진을 위한 충분한 충돌빈도가 이루어지지 않았다는 가설을 수립했다. 수분 공급량 변화를 통해 미반응 이소시안산의 가수분해 여부를 실험하였고 암모니아 발생량이 증가함을 확인하였다. 일정 구간동안 암모니아 발생량 증가는 증기 온도, 수분공급유량에 종속됨을 알 수 있었다.

알루미나에 담지된 플라티늄을 이용한 $NO_X$의 전환반응에 미치는 요인 분석 (Analysis of $NO_X$ Conversion Reaction using Platinum supported on Alumina)

  • 안범수
    • 한국응용과학기술학회지
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    • 제22권2호
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    • pp.168-174
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    • 2005
  • Aluminum tri-butoxide was mixed with the water/ethanol solution and then chloroplatinic acid was added to the solution. The solution was dried at $100^{\circ}C$ for 15hrs to remove the solvent and water then it was calcined at $500^{\circ}C$. The catalyst was activated with a gas mixture. During the activation, the temperature was increased from $150^{\circ}C$ to $500^{\circ}C$. The necessary amount of urea was dissolved in 50mL water and injected. Aqueous urea solution was then mixed with the feed gas stream. At low temperatures, nitrogen containing compounds of urea decomposition are used as reductants in the reducton of $NO_X$. However at high temperatures the nitrogen containing compounds are oxidized to NO and $NO_2$ by oxygen instead of being used in the reduction. The activity of the catalyst was dependent on urea concentration in the feed stream when there was not adequate water vapor in the feed. The maximum conversion was shifted from $250^{\circ}C$ to $150^{\circ}C$ when water concentration was increased from 2 to 17%. It seems that the maximum temperature shifts to lower temperatures because the hydrolysis rate of HNCO increases with water, resulting in higher amounts of $NH_3$.

Substitution of Glycine 275 by Glutamate (G275E) in Lipase of Bacillus stearothermophilus Affects Its Catalytic Activity and Enantio- and Chain Length Specificity

  • Kim, Myung-Hee;Kim, Hyung-Kwoun;Oh, Byung-Chul;Oh, Tae-Kwang
    • Journal of Microbiology and Biotechnology
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    • 제10권6호
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    • pp.764-769
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    • 2000
  • The lipase gene(lip) from Bacillus stearothermophilus was recombined in vitro by utilizing the DNA shuffling technique. After four rounds of shuffling, transformation, and screening based on the initial rate of clear zone formation on a tricaprylin plate, a clone (M10) was isolated, the cell extract of which showed about 2.8-fold increased lipase activity. The DNA sequence of the mutant lipase gene (m10) showed 3 base changes, resulting in two cryptic mutations and one amino acid substitution: S113($AGC{\rightarrow}AGT$), L252 ($TTG{\rightarrow}TTA$), and G275E ($GGA{\rightarrow}GAA$). SDS-PAGE analysis revealed that the increased enzyme activity observed in M10 was partly caused by high expression of the m10 lipase gene. The amount of the expressed G275E lipase was estimated to comprise as much as 41% of the total soluble proteins of the cell. The maximum velocity ($V_{max}$) of the purified mutant enzyme for the hydrolysis of olive oil was measured to be 3,200 U/mg, which was 10% higher than that of the parental (WT) lipase (2,900 U/mg). Its optimum temperature for the hydrolysis of olive oil was $68^{\circ}C$ and it showed a typical $Ca^{2+}$-dependent thermostability, properties fo which were the same as those of the WT lipase. However, the mutant enzyme exhibited a high enantiospecificity towards (S)-naproxen compared with the WT lipase. In addition, it showed increased hydrolytic activity towards triolein, tricaprin, tricaprylin, and tricaproin.

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