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Microwave 조사에 의한 Listeria monocytogenes의 불활성에 관한 연구
이조윤,김종우,이강욱,배형철,Lee, J.Y.,Kim, J.W.,Lee, K.W.,Bae, H.C. 충남대학교 농업과학연구소 1999 Korean Journal of Agricultural Science Vol.26 No.1
The purpose of this study was to determine the thermal inactivation of L. monocytogenes KCTC3443 in liquid culture heated in the controlled microwave system and in the conventional heating method. Furthermore, we have carried out a comparative study on the thermal and nonthermal microwave effects on microorganisms, pasteurized using a controlled microwave energy specially designed apparatuses and a water bath. For the automatic temperature control during microwave heating, the real time data acquisition and computation system is designed with BASIC routine. The automatic temperature control system used in the experiments perform relatively stable control at the experiment temperature of 55, 65, $75^{\circ}C$ and $85^{\circ}C$ for 30 minutes. The effects of microwave heating on liquid cultures was compared with that of conventional heating. The results show that microwave radiation, while being slightly quicker than conventional heating, still reduces effectively the number of pathogenic bacteria during heating for a limit time in liquid cultures. While no particular differences between microwave heating and conventional heating was not observed in the thermal inactivation of L. monocytogenes at 55, 65, $75^{\circ}C$ and $85^{\circ}C$ for 30 min., respectively. Microwave heating is, therefore, substantially not effective in inactivating L. monocytogenes in liquid culture than conventional heating method.
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남명수,배형철,박창식 충남대학교 형질전환복제돼지연구센터 2004 논문집 Vol. No.8
This study was carried out to establish the purification protocol of angiogenin(ANG) from bovine milk. The purification of ANG from bovine milk was performed by using cation chromatography, high-performance liquid chromatography and gel-filtration. We obtained the ANG protein have the molecular weight of about 14 kD by SDS-PAGE analysis. This protein was confirmed as ANG by NH₂-terminal sequence analysis of the first 15 amino acids. Identified amino acids revealed the protein to be identical to that previously reported for bovine ANG.
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