• 한국식품영양과학회지
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• 제25권5호
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• pp.878-884
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• 1996

BailIus sp. IJ-3 균주는 균체외 효소로 대두단백 응고효소를 생산하고, 이 박테리아의 최적 효소생산에 대한 배지조성 및 배양조건을 검토하였다. 최대의 대두단백 응고효소를 생산하는 배지조성은 soymilk 20%(w/v), glucose 2.0%, yeast extract 5.0%, peptone 4.0% 및 potassium Phosphate, monobasic 1.0%였다. 초기 pH는 6.0이었고, $35^{\circ}C$ 배양에서 최대 효소활성을 보였다. 조정된 배지 조성에서 72시간 배양에 최대 효소활성을 나타내었으며, 기존배지 활성의 약 5.3배의 효소활성의 증가를 보였다. BaCilIus sp. IJ-3 균주효소는 7S globu1in에 대해 특이성을 갖고 있는 것으로 사료된다.

• 한국식품영양과학회지
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• 제23권6호
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• pp.973-979
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• 1994

Microorganisms, including the strain IJ-3 isolated from soil, were found to secrete an extracellular soybean protein coagulating enzyme and the strain, IJ-3 was identified as Genus Bacillus according to the Bergey's manual . The enzyme coagulated protein in soymilk , thus forming a curd at pHs 5.8-6.4 and at 55-75℃. The optimum temperature for soybean protein coagulating activity was 65-75℃ and the enzyme was stable at temperature below 50℃ and was found to be stable with about 60-100% of the original activity at a with pH ranges(pH6-7). The molecular weight of enzyme was estimated to be 28,000 by SDS-PAGE. The curd formed with the enzyme from Bacilus sp. IJ-3 has a smooth texture, and a mild taste without any bitterness or a beany flavor.

• Preventive Nutrition and Food Science
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• 제3권2호
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• pp.128-132
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• 1998

7S globulin has been isolate from the defatted soybean meal(glycine max,. merill) by Sepharose-6B column chromatography and CM-Sephadex column chromatography. Coagulum of 7S globulin formed at a temperature of $65^{\circ}C$ in microbial enzyme treatment. In order to characterize the structure of the coagulum, three kinds of coagulum (enzyme-, calcium-and acid-induced coagulum)were compared througth the Scanning Electron Microscope(SEM). The network structure was found to be of two levels. First, there was an appearance on the molecular level in the form of strands. Second, there was a denser network with a fine structure.

• Preventive Nutrition and Food Science
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• 제1권1호
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• pp.53-58
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• 1996

The characterstics of the soy protein curd(eczyme-, HCI- and Ca-surd) were shown by scanning electron micrographs and gel electrophoreis. The emulsion stability of enzyme-curd showed high value in the range of pH 2~10and wide range of temperature(20~8$0^{\circ}C$). While at the isoelectric point(pH5.0), the emulsion stability of the HCI-and Ca-curd was decreased remarkably, and the emulsion stability of temperature was reduced quickly to the 60% and 40% at the 4$0^{\circ}C$. The foam stability of enzyme-curd was slightly higher than that HCI-and CA-curd in all ranges of pH and temperature. The feature of SEM of enzyme-cured produced degradation products faster than that of the HCI- and Ca-curd.