• Applied Biological Chemistry
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• 제30권4호
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• pp.305-310
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• 1987

대두 및 고구마로부터 얻은 ${\beta}-Amylase$의 단백질 구조를 CD Spectra, 항체반응, 화학적 절단을 통하여 비교하였다. 고구마 ${\beta}-Amylase$는 4개의 동일한 subunit로 구성되어 있으며 대두 ${\beta}-Amylase$는 Subunit구조를 하고 있지 않았다. 또한 두 효소는 변성시킨 상태에서 SDS-gel전기영동, gel filtration한 결과 분자량은 동일하였다. 그리고 대두 및 고구마 ${\beta}-Amylase$는 CD spectra상 유사한 2차구조를 나타내고 있으나 방향족 측쇄가 상이함을 나타냈다. 한편 cyteine 잔기 및 methionine 잔기의 화학적 절단한 결과 두 효소는 동일한 아미노산 배일을 나타냈다. 또한 면역학적인 방법에 의해서도 두 효소는 유사성이 인정되었다. 한편 대두 ${\beta}-Amylase$에 대한 항체는 고구마 ${\beta}-Amylase$의 활성을 억제하였으나 밀, 보리, 무우 ${\beta}-Amylase$에 대해서는 활성 억제가 나타나진 않았다.

• 한국식품영양학회지
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• 제3권2호
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• pp.149-160
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• 1990

The soybean $\beta$-amylase ($\alpha$-1, 4-glucan maltohydrolase, EC 3.2.1.2) is composed of seven isozymes(I', I, II, III, IV, V and VI), and isozyme II and IV are the main components among these. The Purification of $\beta$-amylase isozymes from soybean whey were performed by ammonium sulfate fractionation, CM-Sephadex C-50 column chromatography, DEAE-Sephadex chromatography and Gel filtration. The resulted purity of $\beta$-amylase was throughly confirmed by electrophoresis, and then determined its isoelectric point and molecular weight. The results obtained were as follows, 1. Five active fractions of soybean p-amylase were derived on CM-Sephadex C-50 column chromatography. 2. Seven active bands of p-amylase isozymes were detected by isoelectric focusing gel electrophoresis, and their isoelectric points(I' to VI) were 5.07, 5.15, 5.25, 5.40, 5.55, 5.70 and 5.93, respectively. 3. Isozyme II and IV were main components of soybean $\beta$-amylase. 4. The molecular weights of both isozyme II and IV were determined to be 56,000 daltons by the result of SDS polyacrylamide gel electrophoresis. 5. Km values of main isozyme II & IV for amylopectin were determined to be 2.25 mg/ml, which suggest the same function of each isozyme.

• 한국식품저장유통학회지
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• 제8권4호
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• pp.405-411
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• 2001

Monascus속 곰팡이를 이용한 메주의 효소류 활성을 조사하기 위하여 M perpureus와 M. pilasus의 두 균주를 사용하여 쌀 메주와 콩 메주의 효소활성을 조사하였다. M Manascus 백미 및 백미붙말 메주의 효소휴 활성은 전반 적으로 M pilasus를 사용한 경우에 높았다 Prote잃e 활 성응 쌀 분말 메주가 남알상태의 쌀 메주에 비하여 높 았으나. ($\alpha$-amylase, $\beta$-amylase 및 glucoamyJa않는 날알 쌀 메주에서 높았다. 균주 배양액을 사용한 콩 메주는 효소활성온 높았으나 외관적 품질이 양호하지 못히였다. 균주 배양액 10%와 쌀 분말을 0-12% 범위로 챔 가한 결과 prot,않se의 활성온 두 균주 다같이 10%일 때 최대를 나타내었다. ($\alpha$-anylase의 활성은 쌀 분말의 첨가량이 2%일 때 가장 낮았으나 첨가량이 증가할수록 활성이 증가하였다 $\beta$-와nylase와 gluecoamnylase의 훨-성 은 우 균주 다같이 쌀 분말의 첨가량이 증가할수록 감소하였다 메주용 균주로는 M pilosus몹가 양호하였으며 이 균의 쌀 메주 분말을 증자 콩에 10% 되게 첨가 하여 발효시킨 콩 메주는 일반 Aspergillus oryzzae 콩 메주에 비하여 protease 활성은 높았다. 그러나 $\beta$-amylase 와 glueoarnylase는 약 50% 이하의 활성을 나타내었다.

• 한국식품영양학회지
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• 제7권1호
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• pp.23-28
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• 1994

Soybean $\beta$-amylase was purified by DEAE-cellulose ion exchange chromatography, Sephadex G-100 gel chromatography, CM Sephadex C-50 ion exchange chromatography and CM Sephadex C-50 ion exchange rechromatography The purified enzyme showed 1, 020 unit/mg of specific activity. The purified enzyme was identified as homogenious by disc PAGE and analysis of reaction product.

• 한국작물학회지
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• 제45권2호
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• pp.139-142
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• 2000

The experiment was carried out to study the variations and geographical distribution of $\beta$-amylase isozyme by isoelectric focusing (IEF) within Korean, Chinese and Japanese soybean land races. In pH 3-10 gel of IEF, the amylase of soybean accessions was separated into low pI group isozymes (TEX>${$Sp_1$}^b$) and high pI group isozymes(${$Sp_1$}^a$). In pH4-6.5 gel, isoelectric points were at 5.07, 5.15, 5.25, 5.40, and 5.94, and h, j, and k bands also were found. The distribution of Sp$_1$$^{a}$ allele (high pI type) was 29.3% in soybean accessions from Korea, 10.1 % in those from China, and 6.9% in Japanese accessions. The percentage of ${$Sp_1$}^a$) allele was the highest in soybean accessions from Kyungsang province (35 %) in Korea, then central China (32 %) in China, and Honshu (10%) in Japan.

• 한국식품영양학회지
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• 제4권2호
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• pp.161-166
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• 1991

The blocked N-terminus and N-terminal sequence of soybean B-amylase were aetermined by analyzing the acidic peptides derived on peptic digestion of the enzyme. The acidic peptides were separated from the digest on a Dowex 50$\times$2 column(1X5cm) and purified by reversed phase-high performance liquid chromatography(RP-HPLC). The major acidic peptide, PEP-1, was a heptapeptlde. The N-terminal 7 amino acid sequence of soybean B-amylase was deduced to be acetyl-Ala-Thf-Ser-Asp-Ser-Asn-Met- from the results of sequence analysis of PEP-1 and amino acid analysis of other acidic peptides.

• 한국환경과학회지
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• 제22권6호
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• pp.723-732
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• 2013

This study was carried out to investigate changes of protease and amylase activities and nitrogen content in Chungkookjang prepared by Bacillus subtilis S8 and different soybean. Amino-type nitrogen and ammonia-type nitrogen contents increased with an increase in fermentation time and was the highest in black soybean Chungkookjang. The number of viable cells increased up to 24 h of fermentation at all temperatures tested; especially, their levels were the highest at $40^{\circ}C$. Protease activity was the highest in black soybean Chungkookjang. ${\alpha}$-amylase activity increased significantly up to 6 h of fermentation at $30^{\circ}C$ and $40^{\circ}C$ and then maintained constantly. It also increased up to 30-36 h of fermentation at $45^{\circ}C$ and then decreased. ${\beta}$-amylase activity was the highest in black soybean Chungkookjang at $35^{\circ}C$ and $40^{\circ}C$ and in yellow soybean Chungkookjang at $45^{\circ}C$. Production pattern of reducing sugar was similar to that of ${\beta}$-amylase. Amino-type nitrogen, viable cell number and reducing sugar content and ${\beta}$-amylase activity was the highest in Chungkookjang fermented at $40^{\circ}C$. Considering amino-type and ammonia-type nitrogen contents, Chungkookjang fermentation using yellow soybean was favorable. However, the fermentation using black soybean was favorable, considering protease and amylase activities and reducing sugar content.

• 동아시아식생활학회지
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• 제16권4호
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• pp.447-452
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• 2006

This study examined the growth and sensory characteristics of soybean sprout cultured at 25$\pm$1$^{\circ}C$ for 4 days with distilled water control and green tea extracted water (0.03% and 0.05%). The proximate composition of soybean sprout in the green-tea water was better than that of the control in ash, protein and fat, while the soybean sprout was especially higher in 0.05% green-tea water. The contents of vitamin C and $\beta$-carotene were higher in soybean sprout in green-tea water than the control. The total free amino acids composition of soybean sprout in green-tea water was better than that of the control, with the highest being obtained in soybean sprout in 0.03% green-tea water. Antioxidative activity was assayed by DPPH radical scavenging ability with spectrophotometer at 514 nm. The soybean sprout in green-tea water was higher than control. The amylase activity of the soybean sprout increased steadily during the first 4 days and that of the control was higher than soybean sprout in green-tea water. The proteinase of soybean sprout steadily increased during 4 day culture. Furthermore, the proteinase activity of soybean sprout in green-tea water was higher than that of the control up to 2 days. Whereas after 3 days, it was the highest in 0.03% green-tea water and then decreased remarkably in 0.05% green-tea water.

• Applied Biological Chemistry
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• 제35권4호
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• pp.232-236
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• 1992

생대두를 이용한 발효장류의 개발을 위한 기초조사로서 대두의 처리조건을 찾고저 처리방법 [생콩(A), 수침탈각(B), 건열처리(C) 및 습열처리(D)]을 달리한 대두의 일반성분과 효소활성변화를 검토하였다. 그 결과 일반성분 중 수분함량은 A, D구가 B, C구 보다 $2.0{\sim}3.0%$, 조지방 함량은 A, B구가 C, D구 보다 약 2%, 조단백질 함량은 C, D구가 A, B구 보다 $1.16{\sim}1.74%$, 조섬유 함량은 A구가 B, C, D구 보다 $0.11{\sim}1.41%$ 많았으나, 회분은 B, C, D구가 A구 보다 0.49% 많았다. ${\alpha}-amylase$, ${\beta}-amylase$, protease, lipase 활성도는 생콩(A) 및 수침탈각(B) 구가 전열처리(C) 및 습열처리(D)구 보다 약 $2{\sim}5$배 이상 높았다. Trypsin inhibitor 활성도 크기는 $B(56.7{\sim}119.2%)>A(42.9{\sim}95.6%)>D(32.9{\sim}39.6%)>C(20.8{\sim}38.3%)$구 순이었다.

• Journal of Microbiology and Biotechnology
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• 제14권6호
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• pp.1196-1199
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• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.