• Journal of Ginseng Research
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• 제24권1호
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• pp.41-45
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• 2000

인삼전분으로부터 기능성 말토올리고당을 생산하기 위하여 인삼전분에 대한 말토 올리고당 생산 최적조건을 검토하고 이들을 정제 한 후 물리화학적 특성과 장내 유용 세균에 대한 생육효과를 조사하였다. Amano-A amylase를 사용하였을 때 glucose가 4개 이상 결합된 말토 올리고당이 많이 생성되어 최적 효소로 선정하였고, 이 효소를 이용한 말토 올리고당 생산 최적조건은 인삼전분 10%, 효소 첨가 농도 50 unit/g 전분 과 반응시간 24시간이었다. 인삼전분을 효소분해하여 생산하고 carbon-celite로 정제한 말토올리고당의 점도와 보수력은 각각 37.7 cps(20。C)와 110%(75%상대습도)로 설탕에 비하여 높았으며, 감미도는 설탕의 25.6% 이었다. 또한 생산된 말토올리고당은 장내 유용세균인 Biflidobacterium infantis의 생육을 촉진시켰다

• 한국식품영양과학회지
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• 제27권4호
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• pp.639-647
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• 1998

This study was carried out to produce the maltooligosaccharides directly from the culture medium containing high concentration of soluble starch as carbohydrate source by Bacillus cereus IAM 1072. Optimum conditions for the production of maltopentaose and maltooligosaccharides were predicted as 10.62 and 10.92 in C/N ration, 115.74 and 116.51 rpm in agitation speed, 30.19 and 30.9$0^{\circ}C$, respectively. And at these conditions, products of maltopentaose and maltooligosaccharides were 23.23 and 50.33g/L, respectively. From the results of continuous culture for maltopentaose, the productivity increased up to 6.9 times, showing 6.6g/L/hr compared with 0.96g/L/hr batch culture. Maltopentaose showed lower sweetness at 3% concentration representing 1/5 of that sugar. Also, swelling power of maltooligosaccharides was reached to the same point with sugar after fermentation.

• Bulletin of the Korean Chemical Society
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• 제27권8호
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• pp.1243-1245
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• 2006

• Biotechnology and Bioprocess Engineering:BBE
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• 제8권1호
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• pp.47-53
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• 2003

An experimental study on the chromatographic separation of maltopentaose from a mixture, including glucose, maltose, maltotriose, and maltopentaose, was carried out in a nonionic polymeric sorbent column while varying the operating conditions, such as the solution pH, buffer contents, and isopropyl alcohol (1PA) concentration. Unlike the pH and buffer contents, the IPA concentration had a Significant impact on the single component chromatograms for maltopentaose. The retention times of the maltooligosaccharides with the nonionic polymeric sorbent Sp207 were in the following order: glucose < maltose < maltotriose < maltopentaose. From the experimental binary, ternary, and quaternary chromatograms, gradient chromatographic separation with a changing IPA concentration as a function of time was required to obtain high-purity maltopentaose and reduce the elution time.

• Journal of Microbiology and Biotechnology
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• 제18권3호
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• pp.457-464
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• 2008

An extracellular enzyme (RMEBE) possessing ${\alpha}-(1{\rightarrow}4)-(1{\rightarrow}6)$-transferring activity was purified to homogeneity from Rhodothermus marin us by combination of ammonium sulfate precipitation, Q-Sepharose ion-exchange, and Superdex-200 gel filtration chromatographies, and preparative native polyacrylamide gel electrophoresis. The purified enzyme had an optimum pH of 6.0 and was highly thermostable with a maximal activity at $80^{\circ}C$. Its half-life was determined to be 73.7 and 16.7 min at 80 and $85^{\circ}C$, respectively. The enzyme was also halophilic and highly halotolerant up to about 2M NaCl, with a maximal activity at 0.5M. The substrate specificity of RMEBE suggested that it possesses partial characteristics of both glucan branching enzyme and neopullulanase. RMEBE clearly produced branched glucans from amylose, with partial ${\alpha}-(1{\rightarrow}4)$-hydrolysis of amylose and starch. At the same time, it hydrolyzed pullulan partly to panose, and exhibited ${\alpha}-(1{\rightarrow}4)-(1{\rightarrow}6)$-transferase activity for small maltooligosaccharides, producing disproportionated ${\alpha}-(1{\rightarrow}6)$-branched maltooligosaccharides. The enzyme preferred maltopentaose and maltohexaose to smaller maltooligosaccharides for production of longer branched products. Thus, the results suggest that RMEBE might be applied for production of branched oligosaccharides from small maltodextrins at high temperature or even at high salinity.

• Journal of Microbiology and Biotechnology
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• 제19권12호
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• pp.1547-1556
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• 2009

A novel thermostable $\alpha$-glucosidase (TtGluA) from Thermoanaerobacter tengcongensis MB4 was successfully expressed in E. coli and characterized. The TtgluA gene contained 2,253 bp, which encodes 750 amino acids. The native TtGluA was a trimer with monomer molecular mass of 89 kDa shown by SDS-PAGE. The purified recombinant enzyme showed hydrolytic activity on maltooligosaccharides, p-nitrophenyl-$\alpha$-D-glucopyranide, and dextrin with an exotype cleavage manner. TtGluA showed preference for short-chain maltooligosaccharides and the highest specific activity for maltose of 3.26 units/mg. Maximal activity was observed at $60^{\circ}C$ and pH 5.5. The half-life was 2 h at $60^{\circ}C$. The enzyme showed good tolerance to urea and SDS but was inhibited by Tris. When maltose with the concentration over 50 mM was used as substrate, TtGluA was also capable of catalyzing transglycosylation to produce $\alpha$-1,4-linked maltotriose and $\alpha$-1,6-linked isomaltooligosaccharides. More importantly, TtGluA showed exclusive regiospecificity with high yield to produce $\alpha$-1,6-linked isomaltooligosaccharides when the reaction time extended to more than 10 h.

• 한국식품과학회지
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• 제31권2호
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• pp.482-487
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• 1999

과요오드산으로 산화시킨 당을 유리아미노산과 반응시켜서 ${\alpha}-NH_2$기와 펩티딜리신의 ${\varepsilon}-NH_2$기와 반응하여 결합한 것을 확인하였다. 그래서, 제조한 과요드산-산화당은 단백질 분자 표면의 리신의 ${\varepsilon}-NH_2$기와 Schiff 염기 반응으로 공유결합하여 당단백질을 만드는 것으로 볼 수 있다. 과요드산 산화당으로 변형한 고구마 ${\beta}$-아밀라아제는 C, H는 증가, N은 감소하였다. N말단의 ${\alpha}-NH_2$기는 70% (pentamer), 73% (monomer), ${\varepsilon}-NH_2$기는 33% (pentamer), 26% (monomer)가 산화당과 반응하였다. 페놀-황산법에 의한 총당 정량과 DNP 법으로 분석한 결과, $IO_4$-산화말토헥사오스는 고구마 ${\beta}$-아밀라아제 1몰당 6몰이 결합된 것으로 나타났고, 고구마 ${\beta}$-아밀라아제에 결합된 산화가용성 전분은 효소단백질 대비 13.2% (monomer), 13.5% (pentamer), 산화말토헥사오스는 9.7% (pentamer), 9.3% (monomer)로 나타났다.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2001년도 추계학술발표대회
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• pp.656-659
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• 2001

Cyclodextrin glucanotransferase (CGTase) (EC 2.4.1.19) use starch to produce cyclic maltooligosaccharides (cyclodextrins, CDs) which are of interest in various applications. To obtain a novel CGTase having high CD-forming activity, ${\beta}-cyclodextrin$ glucanotransferase $({\beta}-CGTase)$ from Bacillus firmus var. alkalophilus was modified through site-directed mutagenesis and constructed five mutants, H59T, H59Q, Y96M, 9O-PPI-93, and ${\Delta}(148-154)D$, respectively. Y96M and ${\Delta}(148-154)D$ showed much higher level of conversion yields of starch into CDs from 28.6% to about 39% compared to wild-type ${\beta}-CGTase$, respectively, but 90-PPI-93 maintained similar convesion yields of starch to CDs. And their ${\beta}-CD$ ratios to total CDs were not changed and maintained, and convesion yields to linear maltooligosaccharides of all mutants were not changed significantly. These results indicates that five mutations of ${\beta}-CGTase$ from Bacillus firmus var. alkalophilus appears to be important roles for increase of overall CD production rather than change of its product specificity, especially.

• 한국식품과학회지
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• 제40권1호
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• pp.70-75
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• 2008

두 개의 amylase를 호알칼리성 Pseudomonas sp. KFCC 10818의 배양액으로부터 정제하여 그 특성을 조사하였다. 정제된 효소의 분자량은 각각 50 kDa과 75 kDa이었다. 이 효소들의 최적반응온도는 각각 $35^{\circ}C$와 $40^{\circ}C$였으며 50 kDa의 효소는 칼슘이온에 의하여 효소활성이 두 배로 촉진되었다. 이 두 효소는 최적 pH가 6-8 부근이었으며 pH 12의 조건에서도 효소활성을 유지하는 알칼리내성을 나타냈다. Maltooligosaccharide이나 soluble starch로부터 maltose와 maltotriose를 최종 효소반응산물로 생산하였다. 두 amylase는 N-말단 아미노산 서열이 각각 QTVPKTTFV와 DTVPGNAFQ로 분석되었다.

• 한국식품저장유통학회지
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• 제15권1호
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• pp.99-104
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• 2008

현미(고아미) 비열처리 알코올발효 부산물을 식품소재로 활용하고자 cellulase처리조건에 따른 품질특성 변화를 조사하였다. 그 결과, 가수분해 온도에 따른 고아미 부산물의 가용성 고형분 및 총당은 추출온도가 높을수록 함량이 증가하였고 총식이섬유소는 약 0.67%로 비슷하게 나타났다. 환원당은 가수분해 온도 $70^{\circ}C$에서 가장 높은 함량을 나타내었다. 말토올리고당은 $80^{\circ}C$ 가수분해하였을 때 가장 많이 검출되었으며 maltotetraose와 maltopentaose도 검출되었다. Cellulase농도에 따른 가용성 고형분, 총식이섬유소, 환원당 및 총당은 cellulase첨가구들이 무첨가구에 비해 높은 함량을 나타내었으며 cellulase 첨가구들은 각각 약 6.30 및 0.69%와 3,600 및 5,500 mg%로 비슷하게 나타났다. 말토올리고당은 cellulase 농도가 높을수록 증가하였으며 cellulase 농도 0.6%(w/w)이상에서는 비슷한 함량을 나타내었다. 가수분해 시간에 따른 가용성 고형분 및 총식이섬유소는 60분 이상에서 각각 약 6.25 및 0.70%로 비슷한 함량을 나타내었다. 환원당, 총당 및 말토올리고당은 가수분해 시간이 경과할수록 증가하였으며 120분 이상에서는 각각 약 3,800, 5,680 및 1,950mg%로 비슷한 함량을 나타내었다. 이상의 결과, 고아미 부산물은cellulase 0.6%(w/w)를 첨가하여 $80^{\circ}C$에서 120분간 가수분해하였을 때 식이섬유소 및 말토올리고당 함량이 가장 높은 것으로 나타나 식품 소재로의 다양한 활용이 기대되었다.