• 미생물학회지
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• 제40권3호
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• pp.230-231
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• 2004

꽃송이버섯(Sparassis crispa DSMZ 5201)의 균사를 사용하여 균사외 효소활성을 측정하였다. Yeast-malt extract-glucose 배지를 사용하여 $24^{\circ}C$에서 15일간 배양 후 배양여액을 조효소원으로 사용하였을 때, $\alpha$-amylase효소의 활성은 44.27 unit/$mg{\cdot}protein$이었다. 배양여액 중의 Protease, CMCase, $\beta$-glucosidase, chitinase 및 exo-$\beta$-1,4-glucanase의 세포외 효소활성은 상대적으로 높았으나, xylanase 효소활성은 낮게 나타났다.

• 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.

• 한국식품영양학회지
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• 제6권4호
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• pp.307-313
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• 1993

Bacillus cereus $\beta$-amylase was purified by Sephadex G-100 gel filtration, CM Sephadex C-50 ion exchange chromatography and CM Sephadex C-50 ion exchange rechromatography The purified enzyme showed 871 unit/mg of specific activity. The purified enzyme was identified as homogenious by disc PAGE, SDS-PAGE and analysis of reaction product. The purified enzyme showed optimum pH 7.0. optimum temperature 5$0^{\circ}C$, and was stable at 0~5$0^{\circ}C$ and at pH range of 6~10.

• Food Science and Biotechnology
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• 제17권3호
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• pp.519-526
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• 2008

To improve the quality of traditional kochujang, strains with high protease and amylase activity were isolated and identified from Sunchang traditional kochujang. Twenty-three strains strongly producing protease and 16 strains strongly producing $\alpha$- and $\beta$-amylase were isolated by using 1% isolated soy protein agar medium and 2% starch agar medium, respectively. Protease activities of the IA7, I5, and IA2 strain were 22.5, 21.2, and 20.6 unit/mL, respectively, and were higher than those of the other strains. Stains with high $\alpha$-amylase activity included K9 (967.8 unit/mL), K14 (828.3 unit/mL), K13 (662.5 unit/mL), K8 (601.5 unit/mL), and K11 (405.9 unit/mL). The $\beta$-amylase activity of the K11 strain was the highest, 34.3 unit/mL, among the isolated strains. Based on morphological, physiological properties, and API 50CHB-kit test for assimilation of 49 carbohydrates, 8 strains selected according to protease, $\alpha$-amylase, and $\beta$-amylase activities were tentatively identified as Bacillus megaterium (IA2), Bacillus subtilis (IA7, 15), Bacillus amyloliquefaciens (K8, K9, K11, and K13), and Bacillus stearothermophillus (K14). The IA7, 15, and K11 strains were finally identified as B. subtilis (99% ID) based on 16S rDNA sequencing.

• Journal of Microbiology
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• 제42권4호
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• pp.319-327
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• 2004

An additional amylase, besides the typical $\alpha-amylase,$ was detected for the first time in the cytoplasm of B. subtilis SUH4-2, an isolate from Korean soil. The corresponding gene (bbmA) encoded a malto­genic amylase (MAase) and its sequence was almost identical to the yvdF gene of B. subtilis 168, whose function was unknown. Southern blot analysis using bbmA as the probe indicated that this gene was ubiquitous among various B. subtilis strains. In an effort to understand the physiological function of the bbmA gene in B. subtilis, the expression pattern of the gene was monitored by measuring the $\beta-galactosidase$ activity produced from the bbmA promoter fused to the amino terminus of the lacZ struc­tural gene, which was then integrated into the amyE locus on the B. subtilis 168 chromosome. The pro­moter was induced during the mid-log phase and fully expressed at the early stationary phase in defined media containing $\beta--cyclodextrin\;(\beta-CD),$ maltose, or starch. On the other hand, it was kept repressed in the presence of glucose, fructose, sucrose, or glycerol, suggesting that catabolite repression might be involved in the expression of the gene. Production of the $\beta-CD$ hydrolyzing activity was impaired by the spo0A mutation in B. subtilis 168, indicating the involvement of an additional regu­latory system exerting control on the promoter. Inactivation of yvdF resulted in a significant decrease of the $\beta-CD$ hydrolyzing activity, if not all. This result implied the presence of an additional enzyme(s) that is capable of hydrolyzing $\beta-CD$ in B. subtilis 168. Based on the results, MAase encoded by bbmA is likely to be involved in maltose and $\beta-CD$ utilization when other sugars, which are readily usable as an energy source, are not available during the stationary phase.

• 한국작물학회지
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• 제47권6호
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• pp.413-417
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• 2002

온대 수도작에 있어서 발아시의 조건에 가까운 저온.담수 토양조건에서의 출아에 관련된다고 생각되어지는 $\beta$-아밀라제 유전자 발현과 발현 양상이 실제로 호분층 인접 부분의 전분 분해에 영향을 미치는지 in situ hybridization과 현미화학적방법으로 검토하였다. 1. $18^{\circ}C$의 저온.담수토양조건하에서 출아했던 장향도 품종은 호분층에서 $\beta$-아밀라제 유전자의 발현이 보였다. 2. $18^{\circ}C$의 저온.담수토양조건하에서 출아하지 못했던 수원 287호는 $\beta$-아밀라제 유전자의 발현이 보이지 않았다. 3. $\beta$-아밀라제 활성의 유무에 의해 배반세포에 인접한 배유부분의 전분분해량에 변화를 보여 $\beta$-아밀라제 활성이 높은 장향도, 은방주(Ginbozu), Fortana I-133가 $18^{\circ}C$의 저온.담수토양조건하에서는 $\beta$-아밀라제 활성을 나타내지 않는 수원 287호와 시험한 모든 조건하에서 $\beta$-아밀라제의 활성이 보이지 않았던 농림(Norin) 6호, 고시히까리(Koshihikari) 보다 배반상피세포 및 배반상피세포에 인접한 호분층 근접 배유부분의 전분립 감소가 컸다. 이상의 결과 저온.담수토양조건하에서 벼 종자의 출아에 $\beta$-아밀라제 유전자의 발현과 전분 분해의 연관 가능성을 확인하였다.

• 동아시아식생활학회지
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• 제25권1호
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• pp.139-145
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• 2015

본 연구에는 메밀을 ${\alpha}$-amylase, ${\beta}$-amylase, glucoamylase 세 종류의 효소로 당화한 결과, 당도와 rutin, quercetin, 총 폴리페놀 함량이 증가하였고, 항산화 활성이 개선됨을 확인하였다. 당화 전 약 $1^{\circ}Brix$를 나타내던 메밀은 ${\alpha}$-amylase, ${\beta}$-amylase, glucoamylase로 당화하였을 때 최고 $10.27^{\circ}Brix$, $5.13^{\circ}Brix$, $11.13^{\circ}Brix$를 각각 나타내었다. Rutin과 quercetin의 함량도 당화 전보다 당화를 거치면서 증가하는 경향을 나타내었으며, ${\alpha}$-amylase로 당화하였을 때 rutin은 1.76배, quercetin은 2.09배 증가하였으며, ${\beta}$-amylase로 당화하였을 때 rutin은 1.58배 증가하였으며, glucoamylase로 당화하였을 때 rutin은 3.36배, quercetin은 6.58배 증가하였다. 총 폴리페놀과 DPPH radical 소거능을 측정한 결과, 당화를 하기 전과 비교하여 당화 후 총 폴리페놀 함량과 DPPH radical 소거능이 유의하게 증가하였다. 이러한 결과를 바탕으로 메밀의 당화는 메밀에 함유되어 있는 기능성 성분을 증가시켜 기능성 식품으로의 개발가능성을 높이는 것으로 판단된다.

• 한국식품영양과학회지
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• 제27권2호
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• pp.259-267
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• 1998

Typical characteristics of Mejus must be understood to get the basic data for setting up mass production system of traditional fermented soybean products. One hundred and twenty one Mejus were collected from various places and analyed. Most of shapes were rectangular and some were spherical, conical, cylindrical and doughnut types. The weight of Mejus was 0.4~4.2kg. Chemical analysis showed: moisture content, 9.73~58.22% ; pH, 4.95~8.15; acidity, 0.6~3.8% ; soluble protein content, 4.45~12.31%; soluble sugar content, 0.82~10.95%. Enzyme assay showed: $\alpha$-amylase activity, 5.0~874.2 units/g; $\beta$-amylase activity, 0.02~27.74units/g; acidic protease activity, 31.3~225.1unts/g; lipase activity 1.0~53.0units/g. Total viable cells were 3.72$\times$107~1.35$\times$1010cfu/g, and yeast and mold count 6.46$\times$104~8.91$\times$106cfu/g. respectively. $\alpha$-Amylase activity of a traditional Meju from Incheon showed the highest activity of 732.8 units/g(interior section) and 823.2units/g (exterior section). $\beta$-Amylase activity was the highest{3.57 units/g (interior sectin) and 4.25units/g (exterior section)} in Meju from Chunbuk. Acidic protease activity was the highest in sample from Seoul, whereas traditional Meju from Kyongnam showed the highest activity of 21.5units/g(interior section) and 37.5units/g(exterior sectin).

• 약학회지
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• 제6권2호
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• pp.18-22
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• 1962

Purified preparation of .betha.-amylase is obtained from radish root by the means of fractional precipitation with ammonium sulfate. Purified preparation saccharifies the starch, .betha.-maltose being formed. Dextrinization in the true sense does not take place. Hydrolysis ceases when approximately 50% of the theoretical yield of maltose is obtained and there remains a substance (to be .betha.-limit dextrin) which gives a blue-violet with iodine, no glucose being formed. Stability of preparation is optimal at pH 4-9 and more completely inactivated at 65.deg. in fifteen minutes. .betha.-Amylase of radish exhibits optimal activity at and near pH 5.0, which varied depending upon the buffer. Calcium and chloride ions do not effect the activities of enzyme. The results of experiments with oxidizing, alkylating and mercaptide-forming reagents which have been reported to be specific for sulfhydryl groups confirm that free sulfhydryl groups are essential to the activity of .betha.-amylase from radish.

• 한국작물학회지
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• 제7권1호
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• pp.123-127
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• 1969

소맥품종의 내한성 정도를 간이하게 판정할 수 있는 연구로서 내한성정도가 이미 알려진 3계급 9품종을 대상으로 하여 발아종자의 Amylase 활력의 강약과 품종의 내한성 정도와의 관계를 5시기 별로 시험했든바 그 성적을 요약하면 다음과 같다. 1. 각 시기별로는 Amylase 활력에 있어 유의차를 나타내지 않았으나 각품군간에는 고도의 유의차가 인정되었다. 2. 내한성에 강한 품종인 수원8005, 진광, 육성003는 다른 2군의 품종군보다 높은 Amylas의 활력을 보여주었고 내한성이 약한 품종인 적달마, 강도신력, 농촌004는 낮은 Amylase 활력을 나타냈으며 내한성이 중간정도인 농림006, 강도, 농림1002는 중간정도의 활력을 나타내었다. 3. 포장조건에서 내한성 정도가 같아보이는 품종간에서도 Amylase 활력을 강약이 인정되어 보다 세밀한 분류가 가능했다. 4. 시기별로 보면 제1～2일 째에서는 내한성 강, 중, 약 3품종군중 Amylase 활력의 차가 크지 않았으나 3일째에 3품종군간에 더욱 명백한 Amylase 활력의 차를 보여 주었고 제4일과 제5일에는 다시 낮아졌으며 포장의 냉해정도와도 시기에 관계없이 고도의 부의 상관을 인정할수 있었으며 3일째에서 가장 높았다. 5. 고로 발아후 3일에 나타난 결과에 의거 Amylase 활력의 차로 내한성의 강, 중, 약을 구명하는 것이 가장 알맞은 것으로 보이며 내한성판별의 기준으로써 효율적 편법으로 인정되었다.