• 제목/요약/키워드: Heat inactivation

검색결과 127건 처리시간 0.028초

도토리박 추출물과 푸마르산 및 중온 열 병합처리에 의한 적근대의 미생물 제어 효과 (Combined Treatment of Acorn Pomace Extract, Fumaric Acid, and Mild Heat for Inactivation of Microorganisms on Red Chard)

  • 박신민;송경빈
    • 한국식품영양과학회지
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    • 제45권11호
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    • pp.1696-1700
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    • 2016
  • 본 연구에서는 차아염소산 나트륨 같은 염소계 살균세척제를 대체하기 위한 천연 살균세척제로서 도토리박 추출물(APE)을 개발하기 위해 적근대에 Listeria monocytogenes를 접종한 후 APE의 항균 효과를 측정하였다. 그리고 최적 세척처리 조건을 수립하고자 APE, FA, $50^{\circ}C$에서의 mild heat를 병합처리하였다. 모든 처리구 중 0.5% APE/$50^{\circ}C$ mild heat/0.5% fumaric acid(FA) 병합 세척처리가 가장 효과적이었는데, L. monocytogenes 수를 대조구에 비해 3.36 log CFU/g 감소시켰다. 병합처리된 적근대 시료의 저장 8일 후 총 호기성균은 대조구와 비교하였을 때 2.89 log CFU/g 감소하였고, 색도 측정 결과 처리구 간 유의적인 차이가 나타나지 않았다. 따라서 본 연구 결과 APE/mild heat/FA 병합처리 방법은 수확 후 적근대의 품질에 영향을 미치지 않고 미생물학적 안전성을 높일 수 있는 효과적인 기술이라고 판단된다.

엽록체 Small Heat Shock Protein의 도입에 따른 형질전환 식물체의 광합성 활성 및 고온내성의 증가 (Introduction of Chloroplast Small Heat Shock Protein Increases Photosynthesis and Thermotolerance in Transgenic Plants)

  • 이병현;조진기
    • Current Research on Agriculture and Life Sciences
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    • 제17권
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    • pp.15-20
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    • 1999
  • 엽록제 small HSP의 기능을 조사하기 위하여 항상적으로 발현하는 형질전환 식물체를 작성하였다. 고온 스트레스 하에서의 형질전환 식물체의 고온내성을 chlorophyll 형광으로 측정하였다. Leaf disc를 고온조건에서 5분간 처리한 후, 광화학계 II의 불활성화를 나타내는 Fo 값의 증가 또는 Fv 값의 감소치를 조사하였다. 형질전환 식물체는 고온 스트레스 하에서의 이들 값의 증감율이 현격히 감소하였다. 또한 유식물체를 $52^{\circ}C$에서 45분간 처리한 후, $25^{\circ}C$에서 계속적으로 배양하였을 때, 비형질전환 식물체는 전부 고사하였으나, 형질전환 식물체의 약 80%는 생존하였다. 이러한 결과는 엽록체 small HSP가 고온 스트레스 하에서 광합성기구를 보호하는데 있어서 중요한 기능을 담당하고 있음을 나타낸다.

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전염성기관지염(傳染性氣管支炎) 바이러스에 대한 가토혈청억제물질(家兎血淸抑制物質)에 관한 연구(硏究) (Studies on Rabbit Serum Inhibitor of Avian Infectious Bronchitis Virus)

  • 유태석
    • 대한수의학회지
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    • 제5권1호
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    • pp.43-57
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    • 1965
  • It has been-reported that rabbit serum exhibit an inhibitory action on avian infectious bronchitis virus in embryonating chicken embryo. In this thesis, the biological, serological, physical and chemical properties of normal rabbit serum on the effect of the virus propagation were studied. Throughout the studies, the following experimental results 'were obtained and summarized here. 1. An inhibitory action of rabbit serum on avian infectious bronchitis vrius is due to the normal serum constituents. 2. The nature of the neutralization between normal rabbit serum and the virus is similar to that of the specific antiserum and the virus. 3. Rabbit serum, heat inactivated at $56^{\circ}C$, for 30 minutes, showed its average $log_{10}El,D_{50}Nl$ of 3.7. 4. The inhibitory compound present in the normal rabbit serum is inactivated by means of 5 per cent trypsin, 0.01 M potassium periodate, and absorbed to zymosan. 5. The inhibitory compound was not affected by 0.05 M trichloroacetic acid and 0.005M $KH_2PO_4$. 6. The higher the temperature of heat inactivation of rabbit serum caused the lesser the neutralizing effect on the virus. Heating the serum at $66^{\circ}C$, for 30 minutes brought about a complete loss of the neutralizing index of the serum. 7. No ions, as a cofactor, was incorporated to the inhibitory action of rabbit serum on the virus. 8. The inhibitory compound amays be found in a fraction of serum globulin.

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Increased Thermotolerance of Transgenic Rice Plant by Introduction of Thermotolerant Gene

  • Lee, Byung-Hyun;Won, Sung-Hye;Kim, Ki-Yong;Lee, Hyoshin;Jinki Jo
    • 한국초지조사료학회지
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    • 제20권2호
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    • pp.97-102
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    • 2000
  • To increase thennotolerance of forage crops, transgenic rice plants as a model for transformation of monocots were generated. A cDNA encoding the chloroplast-localized small heat shock protein (small HSP) of rice, Oshsp21, was introduced into rice plants via Agrobacterium-mediated gene transfer system. Calli induced from scutella were co-cultivated with a A. tumefaciens strain EHAlOl canying a plasmid, pIGhsp21. A large number of transgenic plants were regenerated on a medium containing hygromycin. Integration of Oshsp2l gene was confirmed by PCR and Southern blot analyses with genomic DNA. Northern blot and immunoblot analyses revealed that the Oshsp21 gene was constitutively expressed and accumulated as mature protein in transgenic plants. Effects of constitutive expression of the OshspZl on thermotolerance were first probed with the chlorophyll fluorescence. Results indicate that inactivation of electron transport reactions in photosystem I1 (PSII), were mitigated by constitutive expression of the Oshsp21. These results suggest that the chloroplast small HSP plays an important role in protecting photosynthetic machinery during heat stress. (Key words : Thermotolerance, Rice, Transgenic, cDNA)

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디프테리아 백신의 진화와 물리화학적, 분자생물학적, 면역학적 지식의 진보에 따른 새로운 백신의 개발에 관한 고찰연구 (The Evolution and Value of Diphtheria Vaccine)

  • 배경동
    • KSBB Journal
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    • 제26권6호
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    • pp.491-504
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    • 2011
  • This review article provides an overview of the evolution of diphtheria vaccine, its value and its future. Diphtheria is an infectious illness caused by diphtheria toxin produced by pathogenic strains of Corynebacterium diphtheriae. It is characterized by a sore throat with membrane formation due to local tissue necrosis, which can lead to fatal airway obstruction; neural and cardiac damage are other common complications. Diphtheria vaccine was first brought to market in the 1920s, following the discovery that diphtheria toxin can be detoxified using formalin. However, conventional formalin-inactivated toxoid vaccines have some fundamental limitations. Innovative technologies and approaches with the potential to overcome these limitations are discussed in this paper. These include genetic inactivation of diphtheria toxoid, innovative vaccine delivery systems, new adjuvants (both TLR-independent and TLR-dependent adjuvants), and heat- and freeze-stable agents, as well as novel platforms for producing improved conventional vaccine, DNA vaccine, transcutaneous (microneedle-mediated) vaccine, oral vaccine and edible vaccine expressed in transgenic plants. These innovations target improvements in vaccine quality (efficacy, safety, stability and consistency), ease of use and/or thermal stability. Their successful development and use should help to increase global diphtheria vaccine coverage.

Increasing Sulforaphane Formation in Broccoli Sprouts by Radish Sprouts Additions

  • Gi-Chang Kim;Mi Jang;Hab-Hwa Beak;In-Guk Hwang;Hae-Ju Kang;Byung-Soon Hwang;Ji-Young Kim;Chan-Mi Park
    • 한국자원식물학회:학술대회논문집
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    • 한국자원식물학회 2020년도 추계국제학술대회
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    • pp.78-78
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    • 2020
  • Cruciferous plants such as broccoli and radish contain glucosinolate, which is a bioactive precursor that is most often used in Korean foods and is unique as a food ingredient. In addition, it contains various other phytochemicals and is promising as a health-oriented food material. In particular, Sulforaphane is a hydrolyzate of the glucosinolate, which has a more beneficial effect on the human body. Glucosinolate may be hydrolyzed by enzymes called myrosinase, which is voluntarily possessed by cruciferous plants. However, the ESP(Epithiospecifier protein) in broccoli sprouts could acts competitively with myrosinase, and convert to the less bioactive sulforaphane nitrile form. Therefore, we improved the yielding of sulforaphane in broccoli sprouts with a new method. We induce inactivation of the ESP protein by heat treatment. At this time, a myrosinase was introduced from the radish sprout because myrosinase in broccoli sprouts is also denatured by heat treatment. According to the results, we have confirmed by GC / MS that formation of sulforaphane increases more than 7 fold using set heating and mixing conditions.

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건열처리를 이용한 알팔파의 주요 식중독균 저감화 (Effects of Dry Heat Treatment on the Reduction of Main Food-Borne Bacteria on Alfalfa Seeds)

  • 홍순영;김수진;방우석
    • 한국식품위생안전성학회지
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    • 제37권4호
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    • pp.225-231
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    • 2022
  • 본 연구에서는 건열처리를 통해 알팔파 종자에 접종된 Bacillus cereus ATCC 12480, Listeria monocytogenes ATCC SSA81, Staphylococcus aureus ATCC 6538, Escherichia coli O157:H7 ATCC 43894, Salmonella Typhimurium ATCC 14028을 발아율에 영향 없이 불활성화 시키는 조건(65℃에서 21일, 70℃에서 16일, 75℃에서 10일, 80℃에서 7일)을 조사하였다. 알팔파 종자를 6-7 log CFU/g 수준으로 접종하고 65, 70, 75, 80℃로 건열처리 한 후, 발아율을 확인하였다. 알팔파 종자의 발아율은 시장에 유통되고 있는 알팔파 새싹의 발아율 기준인 70%로 설정하였다. 알팔파 종자에서 B. cereus는 65℃에서 21일, 70℃에서 18일, 75℃에서 14일, 80℃에서 4일, Listeria monocytogenes는 65℃에서 21일, 70℃에서 18일, 75℃에서 12일, 80℃에서 7일, S. aureus는 65℃에서 18일, 70℃에서 18일, 75℃에서 11일, 80℃에서 4일, E. coli O157:H7은 65℃에서 21일, 70℃에서 18일, 75℃에서 12일, 80℃에서 6일, Sal. Typhimurium은 65℃에서 24일, 70℃에서 22일, 75℃에서 14일, 80℃에서 7일 이상 건열처리 하였을 때 완전히 불활성화 되었다. 모든 균주는 65℃에서 80℃로 온도가 상승할 때 특정 온도에서 세균의 90%를 죽이는 데 필요한 시간인 D-값(R2=0.5656-0.7957)이 유의미하게 감소하였다(P<0.05). 80℃에서 7일간 건열처리 하였을 때 발아율이 70% 미만으로 감소하였기 때문에 75℃에서 14일간 건열처리 하는 것이 알팔파 종자의 안전성을 확보하는데 있어 가장 효과적인 방법이다. 이 연구는 알팔파 종자의 안전성을 확보하고 일정한 품질의 새싹을 생산하는데 기초자료로 이용될 것으로 기대된다.

후지 사과 Polyphenol Oxidase의 특성 및 활성억제 (Characteristics and Inhibition of Polyphenol Oxidase from Fuji Apples)

  • 최언호;정동선;조남숙;심영현
    • Applied Biological Chemistry
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    • 제30권3호
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    • pp.278-284
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    • 1987
  • 사과의 건조, 가공 중의 갈변을 방지하기 위한 기초 조사로서 후지 사과로부터 추출한 crude polyphenol oxidase의 특성과 열에 대한 저항성, 갈변 저해제의 저해 효과 등을 조사하였다. Catechol을 기질로 사용하였을 때 polyphenol oxidase의 최적 pH는 5.5, 최적온도는 $20^{\circ}C$, $K_m$ 값은 0.14M이었고, 열불활성화는 유사일차반응을 보였으며 이때 활성화에너지$(E_a)$와 Z값은 각각 23.0cal/kmol, $19.7^{\circ}C$였다. 기질에 따른 친화력은 o-diphenol, 특히 chlorogenic acid에 대하여 높았고, monophenol과 m-diphenol, p-diphenol에 대해서는 나타나지 않았다. Polyphenol oxidase에 의한 갈변은 thiourea와 potassium metabisulfite는 10mM에서, L-cysteine과 ascorbic acid, sodium diethyldithiocarbamate는 1mM에서 현저하게 저해되었다.

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Removal and Inactivation of Human Immunodeficiency Virus(HIV-1) by Cold Ethanol Fractionation and Pasteurization during the Manufacturing of Albumin and Immunoglobulins from Human Plasma

  • Kim, In-Seop;Eo, Ho-Gueon;Park, Chan-Woo;Chong E. Chang;Lee, Soungmin
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제6권1호
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    • pp.25-30
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    • 2001
  • Viral safety is a prerequisite for manufacturing clinical albumin and immunoglobulins from human plasma pools. This study was designed to evaluate the efficacy of cold ethanol fractionation and pasteurization (60$\^{C}$ heat treatment for 10h) for the removal/inactivation of human immunodeficiency virus type 1 (HIV-1) during the manufacturing of albumin and immunoglobulins. Samples from the relevant stages of the production process were spiked with HIV-1, and the amount of virus in each fraction was quantified by the 50% tissue culture infectious dose(TCID(sub)50). Both fraction IV fractionation and pasteurization steps during albumin processing were robust and effective in inactivating HIV-1, titers of which were reduced from an initial 8.5 log(sub)10 TCID(sub)50 to undetectable levels. The log reduction factors achieved were $\geq$ 4.5 and $\geq$ 6.5, respectively. In addition, fraction III fractionation and pasteurization during immunoglobulins processing were robust and effective in eliminating HIV-1. HIV-1 titers were reduced from an initial 7.3 log(sub)10 TCID(sub)50 to undetectable levels. The log reduction factors achieved in this case were $\geq$ 4.9 and $\geq$ 5.3, respectively. These results indicate that the process investigated for the production of albumin and immunoglobulins have sufficient HIV-1 reducing capacity to achieve a high margin of safety.

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Overproduction of the Escherichia coli Chaperones GroEL-GroES in Rhodococcus ruber Improves the Activity and Stability of Cell Catalysts Harboring a Nitrile Hydratase

  • Tian, Yuxuan;Yu, Chen, Huimin;Shen, Zhongyao
    • Journal of Microbiology and Biotechnology
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    • 제26권2호
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    • pp.337-346
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    • 2016
  • Three combinations of molecular chaperones from Escherichia coli (i.e., DnaK-DnaJ-GrpE-GroEL-GroES, GroEL-GroES, and DnaK-DnaJ-GrpE) were overproduced in E. coli BL21, and their in vitro stabilizing effects on a nitrile hydratase (NHase) were assessed. The optimal gene combination, E. coli groEL-groES (ecgroEL-ES), was introduced into Rhodococcus ruber TH3. A novel engineered strain, R. ruber TH3G was constructed with the native NHase gene on its chromosome and the heterologous ecgroEL-ES genes in a shuttle plasmid. In R. ruber TH3G, NHase activity was enhanced 37.3% compared with the control, TH3. The in vivo stabilizing effect of ecGroEL-ES on the NHase was assessed using both acrylamide immersion and heat shock experiments. The inactivation behavior of the in vivo NHase after immersion in a solution of dynamically increased concentrations of acrylamide was particularly evident. When the acrylamide concentration was increased to 500 g/l (50%), the remaining NHase activity in TH3G was 38%, but in TH3, activity was reduced to 10%. Reactivation of the in vivo NHases after varying degrees of inactivation was further assessed. The activity of the reactivated NHase was more than 2-fold greater in TH3G than in TH3. The hydration synthesis of acrylamide catalyzed by the in vivo NHase was performed with continuous acrylonitrile feeding. The final concentration of acrylamide was 640 g/l when catalyzed by TH3G, compared with 490 g/l acrylamide by TH3. This study is the first to show that the chaperones ecGroEL-ES work well in Rhodococcus and simultaneously possess protein-folding assistance functions and the ability to stabilize and reactivate the native NHases.