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RISS 인기검색어
- 검색키워드
- 학과정보 : 酪農學科 (검색결과 16 건)
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더러브렛말의 체중변화와 경주로 상태가 경주속도에 미치는 영향에 관한 연구
This study was undertaken to estimate effects of change of body weight and racetrack conditions on racing time in Thoroughbreds, using a total of 3,966 horses and 71,452 racing records that collected from KRA(Korea Racing Association) from 1994 to 1999. Results obtained were as follows. 1. Based on moisture contents, conditions of racetrack were classified into Heavy(less than 6%), Good(6 to less than 10%), Soft(10 to less than 15%), Yield(15 to less than 20%), and Sloppy(equal or more than 20%). Frequencies of racetrack conditions were 31.9, 42.1, 13.1, 6.1, and 6.8% for Heavy, Good, Soft, Yield and Sloppy, respectively. Thus, the frequency of Good racetrack was the highest and these of Yielding and Sloppy were relatively low. Overall, the frequency of Heavy was increased in spring and winter, whereas frequencies of Yield and Sloppy were increased in summer. The frequency of Good was the highest in autumn. 2. The regression coefficients of moisture contents of racetrack for racing time separated by racing distance ranged from -0.064 to -0.128 sec and the racing time was the faster in Yield and Sloppy than other track conditions. The time differences between Heavy and Sloppy ranged from 0.74 to 1.86 sec. 3. The average body weight of domestic racehorses was 446.5㎏ and the average body weights of stallion, gelding, and mare were 456.5, 452.7 and 440.5㎏, respectively. Body weight of stallion was the highest. 4. The high loss of body weight observed in March, April and May for mare and in May, June and July for stallion and gelding. Overall, the body weight of racehorses was decreased in spring and summer, and increased in autumn and winter. 5. The heritability and repeatability for racing time were 0.275 and 0.520, respectively. The heritability and repeatability for body weight estimated from total records were 0.473 and 0.916, respectively. Heritabilities and repeatabilities for body weight estimated by sex were 0.649 and 0.927, 0.652 and 0.922, 0.422 and 0.913 for gelding, stallion and mare, respectively. 6. When the change of body weight was higher than ±10㎏, the racing time increased significantly. If body weight decreased more than -20㎏ compared to 0㎏, the racing time was increased more than 0.1 sec, but if increased more than +20㎏, the racing time increased more than 0.2 sec. 7. When the change of body weight was ±0.5 percent of body weight, the racing time was the best(shortest). When the change of body weight was more than ±2.5%, racing performance decreased considerably.
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Bacillus subtilis β-galactosidase의 固定化에 關한 硏究
본 연구는 Bacillus subtilis를 밀기울로 고체 배양하여 추출한 β-galactosidase를 정제하여 Ca-alginate bead법으로 고정화하기 위한 조건검토 및 고정화 효소의 특성을 조사한 것으로 그 결과를 요약하면 다음과 같다. 1. Acetone으로 침전시킨 조효소는 일차로 DEAE-cellulose Ion exchange, 이차로 Septhadex G-100 gel filtration에 의하여 약 42배 정제되었고 이때 수율은 28.1%이었다. 2. 본 고정화 효소는 Sodium alginate 농도 2%, 효소액농도 15% 및 bead 제조시 CaCl₂ 용액 2%에서 120분 교반시켰을 때 가장 활성이 좋았으며 고정화 효소의 최적반응을 위한 50℃에서의 진탕 최적속도는 120 spm, 4cm이었다. 3. 조제된 고정화 효소의 최적온도와 pH는 55℃와 6.5이고 65℃에서 1시간 처리시 25%의 잔존활성을 나타내었고 pH 6.0∼8 .0에서 안정성이 좋았다. 4. 본 고정화 효소의 활성은 Cu^++와 Hg^++에는 활성이 저하되었으나 MgCl₂, NaCl등을 포함한 다른 금속이온과 L-glutathion, L-cysteine 등의 보호제에는 큰 영향을 받지 않았다. 5. ONPG와 유당에 대한 Km값은 각각 1.82×10^-2 M과 2.94×10^-2 M, Vmax값은 3.57×10^-8 mole/min와 1.68×10^-7 mole/min로 나타났다. 6. 본 고정화 효소는 4℃에서 40일간 저장후 95% 이상의 높은 잔존활성과 5회 재사용시 (50℃ 30분 반응후 세척냉장보관) 81%의 잔존활성을 나타내었으며 5% Skim milk와 5% 유당용액을 50℃에서 9시간 반응시켰을 때의 분해율은 각각 51%와 43%이었다. The purpose of this experiment was to examine the condition for immobilization of the partial purified beta-galactosidase extracted fromwheat bran solid culture of Bacillus subtilis HP-4 and the properties of the immobilized enzyme. The results obtained are summarized as follows 1. The crude enzyme precipitated with cold acetone was purified about 42 fold through DEAE-cellulose and Sephadex G-100 chromatography and its recovery was 28.1% 2. When beads were being manufactured, the immobilized enzyme showed its best activity in sodium alginate concentration 2%, in enzyme solution concentration 15%, and when stirred in CaCl₂solution 2% for 2 hours. The optimum shaking speed in 50℃ for the highest enzyme activity was 120 spm, 4cm. 3. The optimum temperature and pH for the activity of the immobilized enzyme in sodium alginate were 55℃ and 6.5, respectively. Its residual activity was shown 25 % after heat treatment at 65℃ for a hour, and found its high stability in pH 6.0 ∼8.0 . 4. The activity of the immobilized enzyme was not affected by EDTA, 2mercaptoethanol, KCN, and other metal ions except Hg++ and Cu++, and protect agents including L-glutathione and L-cysteine. 5. The Km and Vmax values of the immobilized enzyme on ONPG were 1.82×10^-2M and 3.57×10^-8 mole/min, whereas those on lactose were 2.94×10^-2M and 1.68×10^-7 mole/min, respectively. 6. The high residual activity of the immobilized enzyme was above 95 % when it was storaged at 4℃ for 40 days and those of 81% was remained after 5 times reuse. When skim milk- and lactose solution 5 % were reacted with the immobilized enzyme at 50℃ for 9 hours, these hydrolysis rates were 51 % and 43%, respectively.
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