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Aspergillus ficuum 조효소액으로부터 Endoinulinase의 정제 및 특성
한상배,유향숙,노민환,이태규,손희숙,우순자,엄태붕 한국산업미생물학회 1991 한국미생물·생명공학회지 Vol.19 No.2
Aspergillus ficuum이 생산하는 endoglycosidase가 conventional CM, DEAE 및 HPLC DEAE, gel chromatography에 의해 단백질 ㎎당 460±40U의 specific activity로 정제되었다. 이 효소는 약 72,000분자량을 가지는 단량체로 이루어져 있었으며 당을 함유하고 있었다. 분해산물의 조사에 의한 작용기작은 전형적 endo cleavage mode를 보여주었으며 특이하게도 sucrose와 palatinose를 분해할 수 있었다. Endoinulinase was purified from a commercial inulin preparation produced by Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAE-Sepharose 6B, HPLC gel filtration on a Protein Pak 125 Column and HPLC ion exchange chromatography on a TSK DEAE-5pw Column. The endoinulinase had a molecular weight of 72,000±1,000 and was glycoprotein with 23 to 25% w/w sugar content. The enzyme was much more active on inulin with random cleavage mode than on sucrose and on palatinose: The ratio of activity on inulin and sucrose (I/S ratio) was 10∼14.
부패된 팥앙금으로부터 분리된 미생물의 동정과 그 균의 생리적 특성
이태규(Tae-Kyoo Lee),노민환(Min-Hwan Roh) 한국식품영양과학회 2006 한국식품영양과학회지 Vol.35 No.10
In order to determine the causes of sweetened adzuki ann spoilage, the characteristics of microorganism isolated from spoiled adzuki ann were investigated. The isolated microorganism was gram-positive, rod-shaped and spore-forming bacteria; its surface was smooth and glazed. From the results of the assimilation test of 46 different biochemicals by the Vitec 2 Compact test and comparison of the cellular wall composition of fatty acid by the data bank of Midi sherlock system, the microorganism was identified as Bacillus subtilis. D-value of the B. subtilis spore was 4.85 min at 115℃, 0.69 min at 121℃ and 0.48 min at 125℃; Z-value was 9.71. The Bacillus subtilis growth was not observed below water activity of 0.92 at 45℃. However, bacteria growth increased gradually as water activity increased above 0.93.
Effect of Degumming Reagents on the Recovery and Nature of Acetone Insolubles from Rice Bran Oil
이태규(Tae-Kyoo Lee),노민환(Min-Whan Rho),양희천(Hee-Cheon Yang),김충기(Choong-Ki Kim),송근섭(Geun-Seoup Song),엄태붕(Tai-Boong Uhm),권용주(Yong-Ju Kwon) 한국식품영양과학회 1991 한국식품영양과학회지 Vol.20 No.3
물 및 다섯가지 탈검제(citric acid, phosphoric acid, oxalic acid, acetic anhydride 및 maleic anhydride)를 사용하여 미강유를 탈검하고 그 탈검효율을 비교하였다. 미강유 원유로부터 인 함유 물질을 제거하는데 있어서 모든 탈검제가 보다 효과적이었으며, 특히 acetic anhydride와 phosphoric acid는 각각 92.5% 및 93.3%까지 인 함유율을 저하시켰다. 또한 비수화성 인지질 특히 Lyso PC를 제거하는데 있어서 모든 탈검제가 효과적이었다. 미강유로부터 추출한 AI의 인지질은 주로 PC, PI, PE 및 Lyso PC로 구성되어 있었으며, 주요 지방산은 oleic acid, linoleic acid 및 plamitic acid의 순이었다. Acetic anhydride를 사용하여 얻은 AI가 가장 안정된 유화를 형성하였으며, 반면에 phosphoric acid 및 oxalic acid를 처리하여 얻은 AI는 매우 빈약한 유화성을 나타냈다. Six reagents (water, citric acid, phosphoric acid, oxalic acid, acetic anhydride and maleic anhydride) were evaluated for their effectiveness in degumming rice bran oil. All chemical reagents tested were found to be significantly more effective than water in removing phosphatides from crude rice bran oil. Especially acetic anhydride and phosphoric acid were effective in reducing phosphorous levels (92.5% and 93.3% removal, respectively). Nonhydratable phospholipids, lysophosphatidyl choline, were removed more effectively by the chemical reagents than by the water degumming. The major phospholipid(PL) components were phosphatidyl choline. Oleic, linoleic and palmitic acids were the major fatty acids of PL in rice bran acetone insolubles(AI). The AI recovered by acetic anhydride degumming produced the most stable emulsions. However, the AI obtained from phosphoric acid or oxalic acid treatments had very poor emulsifying properties.
Aspergillus ficuum 조효소액으로부터 Exoinulinase의 정제 및 특성
한상배,송근섭,유향숙,노민환,이태규,손희숙,우순자,엄태붕 한국산업미생물학회 1991 한국미생물·생명공학회지 Vol.19 No.3
Aspergillus ficuum이 생산하는 exoinulinase가 CM-Sephadex, DEAE-Sepharose 6B 및 HPLC gel filtration을 통해 단백질 ㎎당 약 2,800U의 specific activity로 정제되었다. 이 효소는 native 상태에서 약 83,000±1,000의 분자량을 나타냈으며 당을 함유하고 있었다. 이 효소는 최적 pH가 4.4∼4.7이었고 55℃에서 8시간 노출 후에도 그 활성을 95% 유지하였다. 이 효소의 I/S ratio는 약 0.35이고 전형적인 non-speific β-fructofuranosidase의 특성을 나타내었으며 raffinose와 stachyose를 분해할 수 있었다. An exoinulinase (EC 3.2.1.80) was purified from a commercial inulinase preparation from Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAE-Sepharose 6B and HPLC gel filtration on a Protein Pak 125 column. Native exoinulinase had a molecular weight of 83,000±1,000 and was glycoprotein. Optimal pHs of the enzyme were ranged from 4.4 to 4.7. About ninety five percent of the whole activity was maintained even after incubation of 8 hours at 55℃. The enzyme was a typical non-specific β-fructofuranosidase, of which I/S ratio appears to be 0.35.