• Title/Summary/Keyword: thermal inactivation

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고정익 항공기 저온 시동 성능의 품질 신뢰성 향상에 관한 실증적 연구 (An Empirical Study on the Quality Reliability of the Start-up performance of the Fixed Wing Aircraft at low temperature)

  • 김대운;정수헌
    • 품질경영학회지
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    • 제46권1호
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    • pp.169-188
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    • 2018
  • Purpose: The purpose of this study is to analyze low-temperature starting performance of the light attacker and to search and improve the aircraft system including battery and Battery Charge and Control Unit(BCCU). Methods: In order to improve the starting up performance of the light attacker at low-temp, various deficiency cause were derived and analyzed using Fault Tree Analysis method. As a result, it was confirmed there were drawbacks in the charging and discharging mechanism of the battery. The inactivation of the battery's electrolyte at low-temp and the premature termination of the battery charge were the main cause. After long error and trial, we improved these problems by improving performance of battery and optimizing the charging algorithm of BCCU. Results: It was confirmed that the problems of starting up failures were solved through the combined performance test of the battery and BCCU, the ground test using the aircraft system and the operation test conducted by Korea Airforce operating unit for 3 months in winter. Conclusion: This study showed that the improvement of quality reliability was achieved and thus the start-up performance issue of the light attacker has been resolved at low temperature. And it is expected that the design methodologies of temperature-affected electrical system of aircraft will contribute to the development of the aircraft industry in the future.

Application of Saccharomyces rouxii for the Production of Non-alcoholic Beer

  • Sohrabvandi, Sarah;Razavi, Seyed Hadi;Mousavi, Seyed Mohammad;Mortazavian, Amir;Rezaei, Karamathollah
    • Food Science and Biotechnology
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    • 제18권5호
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    • pp.1132-1137
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    • 2009
  • Successive application of Saccharomyces cerevisiae DSM 70424 and Saccharomyces rouxii DSM 2535 or DSM 2531 in the production of non-alcoholic beer was investigated. The aim of the study was to consider the impact of the 2 mentioned strains of S. rouxii on the reduction of alcohol content in wort fermented at 12 or $24^{\circ}C$ for 96 hr, applying periodic aeration. The 2 S. rouxii strains were added at the $48^{th}$ hr of fermentation after thermal inactivation of S. cerevisiae cells. The greatest alcohol decrease rate was observed for the treatment containing S. rouxii DSM 2535-fermented at $24^{\circ}C$ (from 1.56 to 0.36%). The concentration of acetaldehyde, diacetyl, and 2,3-pentandione, that have a key role in appearance of 'wort' and 'buttery' off flavors, were significantly lower in S. rouxii-containing treatments fermented at $24^{\circ}C$. S. rouxii-containing treatment fermented at $24^{\circ}C$ showed slightly lower overall flavor acceptability compared to S. cerevisiae-containing treatment fermented at the same temperature. Such score was improved for the products obtained at $12^{\circ}C$.

Aspergillus niger가 생산(生産)하는 Endo-Polygalacturonase의 분리(分離)와 특성(特性) (Separation and Characterization of Endo-Polygalacturonase from Aspergillus niger)

  • 박경빈;박관화
    • 한국식품과학회지
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    • 제16권1호
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    • pp.41-46
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    • 1984
  • Aspergillus niger sherumanni IAM 2059가 분비하는 펙틴질분해효소 중에서 endo-polygalacturonase 를 Sephadex G-100, DEAE-Sephadex A-50을 이용하여 분리하고 점도감소와 분해산물분석을 통해 효소의 특성을 조사하였다. Chromatography를 통해 얻은 3 개의 역가 fraction (F-A, F-I 및 F-II) 은 각각 exo형 효소, eodo-polygalacturonase, endo-polymethylgalacturonase 이었다. endo-polygalacturonase의 역가 최적 pH는 환원당 생성으로는 pH4.2 근방이었고 점도감도로는 pH4.7 근방이었다. 이 효소의 Z-value는 $7.5^{\circ}C$이고 $D40^{\circ}C$는 240sec 이며 $40^{\circ}C$에서 활성화엔트로피(Enthalphy of activation) 217.3KJ/mol, 활성화엔트로피(Entropy of activation) 409.2J/mol.K, 활성화자유에너지(Free energy activation) 89.2KJ/mol 이었다.

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Amplicilin biosynthesis by immobilized enzyme

  • Kim, Young-Sik;Ryu, Dewy-D.Y.
    • Archives of Pharmacal Research
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    • 제3권1호
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    • pp.7-12
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    • 1980
  • Ampliciline was synthesized from 6-amino-pencillanic acid (6-APA) and D-.alpha. phenylglycine methyl ester by using amplicilin synthesizing enzyme from Peudomonas melanogenum (IAM 1655). The whole cell enzyme was immobilized by entrapping it in the polyacrylamide gel lattices. The polymer used in the enzyme entrapment was made from 150 mg per ml of acrylamide monomer and 8 mg per ml of N, N'-methylenebisacrylamide. About 200 mg/whole cell enzyme was mixed in the polymer for entrapment. The maximal activity retention after immobilization was 56%. The optimal pH values for the whole cell enzyme and the immobilized whole cell enzyme were 6.0 and 5.9, respectively. The optimal temperature for the enzyme activity were the same for both type of preparations. The enzyme stabilities against pH and heat increased for immobilized whole cell enzyme. Immobilized cell was more stable especially in the acidic condition while both type were found to be very suceptible to thermal inactivation at a temperature above 4.deg.C. The kinetic constants obtained from Lineweaver-Burk plot based on two substate reaction mechanism showed somewhat higher value for immobilized whole cell enzyme as compared to the whole cell enzyme : the Km value for 6-APA were 7.0 mM and 12.5 mM while Km values for phenylglycine methyl ester were 4.5 mM and 8.2 mM, respectively. Using the immobilized whole cell enzyme packed in a column reactor, the productivity of ampiciline was studied by varying the flow rate of substrate solution. At the space velocity, SV, 0.14 hr$^{-1}$ the conversion was 45%. Operational stability found in terms of half life was 30 hr at SV = 0.2 hr.

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Aspergillus fumigatus이 생산하는 Alkaline protease의 특성과 작용양상 (Characteristics and Action Pattern of Alkaline Protease produced from Aspergillus fumigatus)

  • 차원섭;최청
    • 한국식품영양과학회지
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    • 제18권3호
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    • pp.348-355
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    • 1989
  • Alkaline protease 생성능이 강한 Aspergillus fumigatus 균주를 토양에서 분리하고, 생성효소를 정제하여 특성을 조사한 결과 최적 pH는 9.0, pH안정성은 $pH\;8.0{\sim}10.0$, 최적온도는 $50^{\circ}C$였으며, $50^{\circ}C$이하의 온도에서 안정하나 그 이상의 온도에서는 급격한 효소 불활성화를 보였고, 금속염 $Mn^{++},\;Cu^{++},\;Ba^{++},\;Mg^{++}$ 등에 의해서 활성이 다소 증대되나 $K^+,\;Fe^{+++},\;Ag^{++},\;Pb^{++},\;Na^+,\;Ca^{++},\;Hg^+,\;Zn^{++}$에 의해 저해를 받았다. 활성저해제인 EDTA, 2,4-DNP, ${\varepsilon}-amino$ caproic acid에는 큰 저해를 받지 않으나, PCMB에 많은 저해를 받는 것으로 미루어 활성 부위가 SH기인 cystein protease로 추정되었다. Km값은 $8.33{\times}10^{-4}mole/{\ell}$, Vmax는 $47.62{\mu}g/min$였으며, casein과 hemoglobin을 trypsin보다 더 잘 분해하고, casein을 hemoglobin보다 잘 분해하였다.

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The Biochemical Characterization of D-Hydroxyisovalerate Dehydrogenase, a Key Enzyme in the Biosynthesis of Enniatins

  • Lee, Chan; Zocher, Rainer
    • BMB Reports
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    • 제29권6호
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    • pp.493-499
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    • 1996
  • The biochemical properties of purified D-hydruxyisovalerate dehydrogenase from Fusarium sambucinum was elucidated. D-Hydroxyisovalerate dehydrogenase produced solely D-hydroxyisovalerate from 2-ketoisovalerate. The isoelectric point of the purified enzyme was 7.0. The enzyme was highly specific with 2-ketoisovalerate ($K_{m}=0.188$ mM, $V_{max}=8.814$ mmol/min mg) and 2-keto-3-methyl-n-valerate ($K_{m}=0.4$ mM, $V_{max}=1.851$ mmol/min mg) for the reductive reaction. This was also seen by comparing D-hydroxyisovalerate ($K_{m}=1.667$ mM, $V_{max}=0.407$ mmol/min mg) and D-hydroxy-3-methyl-n-valerate ($K_{m}=6.7$ mM, $V_{max}=0.648$ mmol/min mg) for the oxidative reaction. Thiol blocking reagents, such as iodoacetamide, N-ethylmaleimide and p-chloromecuribenzoate inhibited about 80% of enzyme activity at 0.02 mM, 50 mM and 50 mM, respectively. The enzyme activity was also inhibited by the addition of 0.1 mM of various metal ions, such as $Fe^{2+}$ (67%), $Cu^{2+}$ (88%), $Zn^{2+}$ t (76%) and $Mg^{2+}$ (9%). The enzyme was stable over three months in 50 mM potassium phosphate buffer (pH 5~7) at $-80^{\circ}C$. However the purified enzyme lost 30% of its activity in the same buffer after 24 h at $4^{\circ}C$. The studies about thermal inactivation of D-hydroxyisovalerate dehydrogenase exhibit 209.2 kJ/M of activation enthalpy and 0.35 kJ/mol K of activation entropy.

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충진층 반응기에서 고정화 cellulase에 의한 셀룰로스 가수 분해 (Hydrolysis of Cellulose by Immobilized Cellulase in a Packed Bed Reactor)

  • 강병철;이종백
    • 생명과학회지
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    • 제23권11호
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    • pp.1365-1370
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    • 2013
  • 약 염기성 이온교환 수지에 cellulase를 고정화하였고 고정화 cellulase는 흡착 특성이 Langmuir 흡착 등온선을 잘 따랐다. pH와 온도에 대한 효소 활성은 고정화 효소가 우수한 특성을 보였다. 열에 대한 효소 활성은 1차식으로 감소하였고 고정화 효소가 자유 효소에 비해 열 안정성이 우수하였다. 초기 속도법을 통해서 자유 효소와 고정화 효소의 Michaelis-Menten 속도 상수를 결정하였고 속도상수 Km은 고정화 효소가 큰 값을 나타내었다. 충진층 반응기에서 셀룰로스의 전환 공정을 재순환에 의해 측정하였다. 투입되는 셀룰로스의 유량 변화에 대한 셀룰로스의 변환을 연속 공정에서 조사하였다. 장기 운전의 성능을 평가하기 위해 7일 통한 연속공정을 실시하였고 고정화 효소는 48%의 활성을 유지하였다.

전자선 조사에 의한 신선굴(Crassostrea gigas) 중 휴먼노로바이러스 GII. 4의 저감화 (Inactivation of Human Norovirus GII. 4 on Oyster Crassostrea gigas by Electron Beam Irradiation)

  • 김지윤;전은비;최만석;박신영
    • 한국수산과학회지
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    • 제54권1호
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    • pp.16-22
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    • 2021
  • This study investigated the reduction in human norovirus (HNV) GII. 4 count in pacific oyster Crassostrea gigas using electron beam irradiation. Infectious HNV GII. 4 was detected using RT-qPCR (real time reverse transcription-quantitative polymerase chain reaction) with PMA (propidium monoazide)/sarkosyl. At electron beam doses 1, 5, 7, and 10 kGy, the count of HNV GII. 4 was 2.74, 2.37, 2.06, and 1.55 log copies/μL (control, 3.01 log copy/μL), respectively, confirming that as the irradiation dose increased, norovirus count reduced significantly (P<0.05). After PMA/sarkosyl treatment, the counts further reduced at the same irradiation dose, and 10 kGy showed significant differences between the non-treated and PMA/sarkosyl-treated samples (P<0.05). The Ed (decimal reduction dose of electron beam) value based on the first-order kinetic model was 7.33 kGy (R2=0.98). No significant difference was observed in the pH values of the control (6.2) and electron beam-irradiated samples at all doses (6.1). For sensory evaluation, the non-treated sample scored the highest in all categories (5.25-6.17), while the samples treated with 10 kGy showed the lowest score (4.67-5.33), although without statistical significance (P>0.05). Overall, our results suggest that 7 kGy electron beam is sufficient for the non-thermal sterilization of oysters without causing significant changes in quality.

감태나무 에틸아세테이트 분획의 항염증 및 진통 효과 (Anti-inflammatory and Anti-nociceptive Effects of Ethyl Acetate Fraction of Lindera glauca)

  • 김종수;강보혜;박승주;양우인;김명수;이병수;차동석;이세연;권진;전훈
    • 생약학회지
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    • 제53권1호
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    • pp.49-56
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    • 2022
  • The present study was designed to evaluate the anti-inflammatory and anti-nociceptive potential of the ethyl acetate fraction of Lindera glauca (ELG). We found that ELG significantly suppressed NO production through decreased enzyme activity and expression of iNOS in the IFN-γ/LPS-activated murine peritoneal macrophages. The treatment of ELG also down-regulated the expression of COX-2. Our western blot data revealed that inhibitory effects of ELG on these pro-inflammatory mediators were attributed to inactivation of NF-κB. In addition, ELG-fed mice showed a marked decrease in paw edema induced by subplantar injection of trypsin, suggesting in vivo anti-inflammatory potential of ELG. We further investigated the anti-nociceptive properties of ELG using thermal and chemical nociception model. We found that ELG has a strong anti-nociceptive activities in both central and peripheral mechanism. An additional combination test with naloxone revealed that opioid receptor was not involved in the ELG-mediated anti-nociception. In conclusion, ELG may possibly be used as valuable anti-inflammatory and anti-nociceptive agent for the treatment of inflammatory diseases and pains.

고온성 방선균에 의한 순소생산에 관한 연구 (제2보) $\alpha$-Amylase의 효소학적 성질 (Studies on the Production of Enzymes by Thermophilic Actinomycetes (PART II) Some Properties of $\alpha$-Amylase from Thermophilic Actinomycetes)

  • Yang, Han-Chul;Park, Yong-Jin;Cho, Hong-Yeon
    • 한국미생물·생명공학회지
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    • 제4권3호
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    • pp.91-97
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    • 1976
  • 고온성 방선균으로부터 내열성 $\alpha$-Amylase의 생산과 그 이용 가능성을 검토하기 위하여 토양시료로부터 $\alpha$-Amylase 생산능력이 극히 우수한 구주를 분리하여 분리균의 몇가지 균학적 성질내지는 효소생산을 위한 배양조건을 조사하여 전보에 발표하였으며 본보에서는 공시방선균이 생산하는 $\alpha$-Amylase의 효소학적 일반성질을 검토하여 다음과 같은 결과를 얻었다. 1) 본효소의 최적활성 pH는 6.5이었으며 최적변성온도는 55$^{\circ}C$~$65^{\circ}C$이었다. 2) 본효소의 안정 pH범위는 7.0~8.0에 위치 하였으며 3) 활성에 대한 금속 ion의 영향은 $Ca^{++}$$Na^{++}$ ion에 의하여 촉진되었으나 중금속 ion인 Fe$^{++}$ Cu$^{++}$ ion등은 현저히 조해함을 보였으며 열안정성에 대한 금속 ion의 효과는 $Ca^{++}$ ion에 의해 증가했다. 4) 본 순소의 Km value는 2.17$\times$$10^{-4}$g per $m\ell$이었으며 5) Activation energy는 12,000$\pm$580 ㎈ per mole 이었다.

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