• KSBB Journal
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• 제18권5호
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• pp.363-370
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• 2003

본 연구에서는 썩은 고구마 및 감자로부터 amylase 생산균주인 사상균 FM04를 분리하였으며, 분리균주의 섬유소분해 효소 생산에 관한 배양의 환경변수 및 기질특성을 조사하였다. 최적의 효소생산을 위한 온도, pH, 교반조건은 각각 28∼3$0^{\circ}C$, 5.0∼6.0, 100rpm이였다. FM04는 Amylase 생산을 위해 탄소원으로서 starch을 잘 이용하였다. 경제적인 효소생산을 위해 전분이 많이 함유된 음식물쓰레기를 이용하였고, 1% (w/v)의 기질농도에서 5.2 U/ml의 amylase 효소활성을 얻을 수 있었다. Amylase 활성의 최적온도 및 PH는 각각 6$0^{\circ}C$와 4.5이었으며, 열안정성은 5$0^{\circ}C$에서 2일 동안 90%의 활성이 유지되었다. 음식물쓰레기의 효소학적 가수분해에서는 2.5 U/ml의 amylase 배양상등액에 음식물쓰레기 20% (w/v)의 첨가한 반응물을 5$0^{\circ}C$, 48시간의 반응한 결과 72.6 g/L의 환원 당을 얻을 수 있었다.

• Applied Biological Chemistry
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• 제28권4호
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• pp.233-238
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• 1985

Glucoamylase를 $ZrO_2$로 피복된 96% porous glass에 azo-linkage를 형성시켜 결합하게 한후, 2.5% glutaraldehyde로 처리하여 효소를 고정화시켰다. 효소기질로는 용해도가 높고 점도가 낮은 30% enzyme thinned cornstarch (dextrose equivalent 값 : 24)를 사용하여 plug flow-column reactor에서 연속반응시켰다. 반응 최적 pH는 수용성효소의 5.0보다 alkaline 쪽으로 기울어져 7.0으로 나타났고, 고정화반응에 따라 열안정성이 높아지고 $40{\sim}60^{\circ}C$에서 최적 온도범위를 가리키며, Km값은 수용성 효소의 1.25mM보다 낮은 1.04mM값을 보여 주었다. 따라서, pH 7.0, $45^{\circ}C$에서 160시간 동안 corn starch를 기질로 효소반응을 시켜 glucose 90.3%, maltose 8.0%인 DE값 94.0인 전분당분해산물을 획득할 수 있었다.

• Food Science and Biotechnology
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• 제17권4호
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• pp.755-760
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• 2008

The aim of this study was to produce resistant starch preparations from acid-modified com starches prepared at various hydrolysis levels (0.5-4.0 hr). Effect of autoclaving cycles on resistant starch (RS) formation was investigated. Molecular weight distribution, pasting and functional properties of acid-modified com starches were determined. For RS formation native and acid-modified starch samples were gelatinized and autoclaved (1 or 2 cycles). While native and acid-modified starches did not contain any RS, the levels increased to 9.0-13.5% as a result of storage at $95^{\circ}C$ after first autoclaving cycle. Second autoclaving cycle together with storage at $95^{\circ}C$ brought final RS contents of the samples incubated at 4 and $95^{\circ}C$ after the first cycle to comparable level. As acid modification level increased, the amount of high molecular weight fractions decreased, resulting in significant decreases in viscosities (p<0.05). The samples produced in this study had low emulsion stability and capacity values.

• Journal of Plant Biotechnology
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• 제36권3호
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• pp.207-213
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• 2009

Starch serves not only as an energy source for plants, animals, and humans but also as an environmentally friendly alternative for fossil fuels. Progress in understanding of starch biosynthesis, and the isolation of many genes involved in this process have enabled the genetic modification of crops in a rational manner to produce novel starches with improved functionality. Starch is composed of two glucose polymers, amylose and amylopectin. The amylose and amylopectin ratio in starch affects its physical and physicochemical properties. Alteration in starch structure can be achieved by modifying genes encoding the enzymes responsible for starch biosynthesis and starch hydrolysis. Here, we describe recent findings concerning the starch modification in sweetpotato. Sweetpotato [Ipomoea batatas (L.) Lam] ranks seventh in annual production among food crops in the world as an important starch source. To develop transgenic sweetpotato plants with modifying starch composition, we constructed transformation vectors overexpressing granule bound starch synthase I and inhibiting amylopectin synthesis genes such as starch branching enzyme and isoamylase under the control of 35S promoter, respectively. Transformation of sweetpotato (cv. Yulmi) is in progress.

• Journal of Preventive Medicine and Public Health
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• 제7권1호
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• pp.107-113
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• 1974

위생공학에서 하수나 공장폐수를 처리할 때 이용하는 생물학적 처리과정은 미생물에서 생성되는 효소에 의하여 이루어 진다. 본 연구에서는 diastase의 활성에 대하여 수소이온 농도, 온도, 기질 농도 및 방해물질 등 여러가지 요인이 미치는 영향을 실험적으로 관찰하여 다음과 같은 결론을 얻었다. (1) diastase의 활성도는 pH $4.0{\sim}7.0$의 범위가 적당하였고 최적치는 pH 5.0이었다. (2) diastase의 활성도는 $30^{\circ}C{\sim}50^{\circ}C$ 높았으며 최적온도는 $40^{\circ}C$였다. (3) 기질농도의 영향을 보면 녹말농도 $750{\mu}g/ml$까지는 diastase의 활성도가 급격히 증가하였고, 그 이후에는 한정속도를 나타냈다. Michaelis 방정식을 적용시켜 보면 한정속도는 $415{\mu}g/ml$ starch removed/ml of reaction mixture/min였고 Michaelis 상수는 $340{\mu}g/ml$였다. (4) 방해물질의 영향을 보면 NaCl 농도 1.0%, $HgCl_2$ 농도 0.001%에서 diastase의 활성은 완전히 억제되었다.

• Mycobiology
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• 제39권4호
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• pp.278-282
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• 2011

The objective of this study was to find useful fungi with ${\alpha}$-amylase activity from the Korean traditional nuruk for the quality of traditional Korean alcoholic beverage. In this study, 165 samples of traditional nuruk were collected from 170 regions throughout Korea and the fungi were isolated to a total of 384 strains. In order to investigate the effect of microflora on nuruk, ${\alpha}$-amylase activity, saccharogenic power (SP), starch hydrolysis activity and acid producing activity were evaluated. Ten strains were selected by ${\alpha}$-amylase activity, which ranged from 458.47 to 1,202.75 U/g. The size of the discolored zone for the starch hydrolysis activity of each fungus ranged from 0.3 to 2 cm. The SP of the 10 strains ranged from 228.8 to 433.4 SP. Of the 10 stains, three were identified as Aspergillus oryzae, two as Aspergillus flavus, two as Lichtheimia sp., one as Rhizopus oryzae and two as other strains. The total aflatoxins present in the nuruks were examined using enzyme-linked immunosorbent assay. The 10 nuruks had less than 1.11 ppb of aflatoxins.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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• pp.35-35
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• 1999

Amylases catalyze the hydrolysis of starch material and play central roles in carbohydrate metabolism. The structure and a size exclusion column chromatography proved that the enzyme is a dimer in solution. The N -terminal segment of the enzyme folds into a distinct domain and comprises the enzyme active site together with the central (${\alpha}$/ ${\beta}$)$\sub$8/ barrel of the adjacent subunit.(omitted)

• Journal of Microbiology and Biotechnology
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• 제18권9호
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• pp.1544-1549
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• 2008

MhMTS and MhMTH are trehalose ($\alpha$-D-glucopyranosyl-[1,1]-$\alpha$-D-glucopyranose) biosynthesis genes of the thermophilic microorganism Metallosphaera hakonensis, and encode a maltooligosyltrehalose synthase (MhMTS) and a maltooligosyltrehalose trehalohydrolase (MhMTH), respectively. In this study, the two genes were fused in-frame in a recombinant DNA, and expressed in Escherichia coli to produce a bifunctional fusion enzyme, MhMTSH. Similar to the two-step reactions with MhMTS and MhMTH, the fusion enzyme catalyzed the sequential reactions on maltopentaose, maltotriosyltrehalose formation, and following hydrolysis, producing trehalose and maltotriose. Optimum conditions for the fusion enzyme-catalyzed trehalose synthesis were around $70^{\circ}C$ and pH 5.0-6.0. The MhMTSH fusion enzyme exhibited a high degree of thermostability, retaining 80% of the activity when pre-incubated at $70^{\circ}C$ for 48 h. The stability was gradually abolished by incubating the fusion enzyme at above $80^{\circ}C$. The MhMTSH fusion enzyme was active on various sizes of maltooligosaccharides, extending its substrate specificity to soluble starch, the most abundant natural source of trehalose production.

• KSBB Journal
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• 제11권1호
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• pp.86-91
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• 1996

전분이 충전된 폴리에틸렌 필름의 생분해도를 측정하기 위해, ${\alpha}$-amylase가 효과적으로 전분을 분해 시킬 수 있는 반응조건을 설정하고 설정된 반응조건 에서 반응시킨 후 산물인 당을 측정하여 분해정도를 결정하였다. 효과적 인 반응온도는 $80^{\circ}C$이고, pH는 6.3-7.3 사이가 적당하였다. 효소반응에 적당한 r amylase량은 1 mg 전분당 100unit이 었다. 이와 같 은 반응조건하에서, 전분의 무게함유량이 각각 5%. 10%, 15%. 20% 인 폴리에틸렌 필름을 ${\alpha}$-amylase 와 반응시킨 결과 전분이 함유된 비율과 생성된 환 원당간에 대융의 관계를 보였다. 따라서 필름 내에 함유된 생분해가 가능한 전분량을 정량화하는데 calibration 역할을 할 것으로 기대된다. 이 때 분해되 어진 전분의 양은 충전된 전체 전분량의 약 40%에 해당하는 값으로 나타났으며, 나머지는 필름 내부에 분산되 어 있어 ${\alpha}$-amylase의 공격을 받지 못하기 때 문으로 생각된다. 본 실험을 통해 최적화된 반응조 건하에셔 분해시킴으로써, 계면활성제를 첨가하여 분해도를 높인 기존의 데이타보다 더 높은 분해도를 얻을 수 있었다.

• 미생물학회지
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• 제13권3호
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• pp.85-90
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• 1975

Crude cellulases freshly prepared from cultures of Aspergillus niger, Prnicillum motatum, Trichoderma vride 16273 and Trichoderma viride 16374 were assayed on 4 different substrates including Na-CMC, cellulose powder, starch and sucrose. Enzyme prepared from A. niger contained highly active hydrolytic enzymes of the 4 substrates assayed. P. notatum [yielded relatively lower amount of cellulase but the extracts were also highly reactive on starch and sucrose. Trichoderma viride 16274 yielded very little cellulase and invertase, but the extracts showed a high degree of amylase activity. Trichoderma viride 16374, however, yielded collulase comparable to that of Penicillium notatum, but lower activities of amylase and invertase were seen. Commercial cellulases prepared from Penicillium notatum (cellulase[K]) and Trichoderma viride(cellulase[J]) indicated enzyme activities closely parallel to the crude enzymes freshly prepared from fungus cultures. The optimum pH's of cellulolytic activities of cellulase[K] and cellulase[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase[K] and cellualse[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase [K] and cellulase [J] were $60{\circ}C$ and $50{\circ}C$ respectively. Assuming the average molecular weight of Na-CMC is about 115,000, the Km values of cellulase [K] and cellulase[J] were found to be $3.3{\times}10^{-5}/nM$ and $3.3{\times}10^{-4}/nM$ respectively.