• 한국식품영양학회지
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• 제10권1호
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• pp.92-96
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• 1997

시판 식혜에는 설탕과 프룩토오스, 글루코오스, 말토오스 및 여러 사이즈의 말토올리고당, 한계덱스트린이 함유되어 있다. 그 중 한계덱스트린은 0.09%, 밥알은 0.2%를 나타냈다. 1H-NMR 분석 결과, 한계덱스트린은 $\alpha$-1,4-결합 및 $\alpha$-1,6-결합이 15:1의 비율을 나타냈다. Pullulanase 처리로, 말토오스에서 글루코오스 10잔기 이상의 말토올리고당까지 다양한 분포를 나타냈다. 한계덱스트린은 여러 아미라아제 처리 결과, 전통식혜보다 가수분해율이 훨씬 높았다. $\alpha$-글루코시다아제와 타액 $\alpha$-아밀라아제를 공동 작용시킨 경우는 62% 가수분해되었다. 그러나, 밥알의 가수분해율이 매우 낮았다. 그래서 전통 식혜에 비해 한계덱스트린의 비피두스 인자로서의 효과는 적고, 밥알의 식이섬유 작용은 커졌다.

• 한국식품영양학회지
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• 제11권2호
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• pp.150-158
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• 1998

한국산 맥주 3종류, 일본산 맥주 21종류의 한계 덱스트린을 에탄올 침전법으로 분리하였다. 한계 덱스트린의 양은 평균 1.1%로 전체 당 3.15%의 34.5%를 나타냈다. FPLC 분석 결과 한계 덱스트린은 평균 글루코오스 잔기 25개 정도로 형성된 것으로 나타났다. 1H-NMR 분석으로 한계 덱스트린의 $\alpha$-1, 4-결합에 대한 $\alpha$-1, 6-결합의 비율은 평균 1:0.183을 나타냈다. 한계 덱스트린을 $\alpha$-아밀라아제와 $\alpha$-글로코시다아제로 5시간 가수분해 하여 소화성을 평가한 결과 평균 57.22% 가수분해 되었다. 그 중 한국산 맥주의 한계 덱스트린이 가장 높은 소화성 70.38%를 나타냈다. 아밀라아제로 소화된 부분과 에탄올 침전법으로 상징액으로 제거된 작은 당을 합하면 평균 86%가 소화성 당으로, 14%가 비피두스균 증식 인자로 평가된다.

• 한국미생물·생명공학회지
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• 제18권1호
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• pp.39-43
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• 1990

본 저해물질은 10Mug의 Alpha-D-glucosidase에 대해서 50Mug 및 100Mug을 첨가했을 때 저해율은 각각 60, 80 정도였으며 enzyme-inhibitor complex를 비교적 서서히 형성하여 5분간 진처리하였을 때 약 55의 저해율을 나타내었다. 그리고 Alpha-D-glucosidase, Alpha-galactosidase및 Beta-galactosidase를 제외한 탄수화물 분해효소에 대해서는 저해능이 없었으며, Alpha-D-glucosidase에 대한 저해양상은 non-competitive type 이었으며 Ki 값은 118 $\mu$g/m$\ell$였다.

• Journal of Microbiology and Biotechnology
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• 제17권8호
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• pp.1242-1248
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• 2007

Genomic analysis of a hyperthermophilic archaeon, Thermococcus onnurineus NA1 [1], revealed the presence of an open reading frame consisting of 1,377 bp similar to ${\alpha}$-amylases from Thermococcales, encoding a 458-residue polypeptide containing a putative 25-residue signal peptide. The mature form of the ${\alpha}$-amylase was cloned and the recombinant enzyme was characterized. The optimum activity of the enzyme occurred at $80^{\circ}C$ and pH 5.5. The enzyme showed a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7), but not pullulan and cyclodextrin. Surprisingly, the enzyme was not highly thermostable, with half-life ($t_{1/2}$) values of 10 min at $90^{\circ}C$, despite the high similarity to ${\alpha}$-amylases from Pyrococcus. Factors affecting the thermostability were considered to enhance the thermo stability. The presence of $Ca^{2+}$ seemed to be critical, significantly changing $t_{1/2}$ at $90^{\circ}C$ to 153 min by the addition of 0.5 mM $Ca^{2+}$. On the other hand, the thermostability was not enhanced by the addition of $Zn^{2+}$ or other divalent metals, irrespective of the concentration. The mutagenetic study showed that the recovery of zinc-binding residues (His175 and Cys189) enhanced the thermo stability, indicating that the residues involved in metal binding is very critical for the thermostability.

• Journal of Microbiology and Biotechnology
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• 제18권9호
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• pp.1555-1563
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• 2008

A novel $\alpha$-amylase ($\alpha$-1,4-$\alpha$-D-glucan glucanohydrolase, E.C. 3.2.1.1), ScAmy43, was found in the culture medium of the phytopathogenic fungus Sclerotinia sclerotiorum grown on oats flour. Purified to homogeneity, ScAmy43 appeared as a 43 kDa monomeric enzyme, as estimated by SDS-PAGE and Superdex 75 gel filtration. The MALDI peptide mass fingerprint of ScAmy43 tryptic digest as well as internal sequence analyses indicate that the enzyme has an original primary structure when compared with other fungal a-amylases. However, the sequence of the 12 N-terminal residues is homologous with those of Aspergillus awamori and Aspergillus kawachii amylases, suggesting that the new enzyme belongs to the same GH13 glycosyl hydrolase family. Assayed with soluble starch as substrate, this enzyme displayed optimal activity at pH 4 and $55^{\circ}C$ with an apparent $K_m$ value of 1.66 mg/ml and $V_{max}$ of 0.1${\mu}mol$glucose $min^{-1}$ $ml^{-1}$. ScAmy43 activity was strongly inhibited by $Cu^{2+}$, $Mn^{2+}$, and $Ba^{2+}$, moderately by $Fe^{2+}$, and was only weakly affected by $Ca^{2+}$ addition. However, since EDTA and EGTA did not inhibit ScAmy43 activity, this enzyme is probably not a metalloprotein. DTT and $\beta$-mercaptoethanol strongly increased the enzyme activity. Starting with soluble starch as substrate, the end products were mainly maltotriose, suggesting for this enzyme an endo action.

• Archives of Pharmacal Research
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• 제8권2호
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• pp.67-75
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• 1985

To find emylase inhibitors produced by microorganisms from soil, a strain which had a strong inhibitory activity against bacteria .alpha.-amylase was isolated from the soil smaple collected in Seoul. The morphological and physiological characteristics of this strain on several media and its utilization of carbon sources showed that it was one of Streptomyces specties according to the international Streptomyces Project method. The amylase inhibitor of this strain was purified by means of acetone precipitation, adsorption on Amberlite XAD-2, and column chromatography on Amberlite CG-50 and SP-Sephadex C-25. The inhibitor was stable at the pH range of 1-10 and at 100.deg.C for half an hour, and had inhibitory activities against other amylases such as salivary .alpha.-amylase, pancreatic .alpha.-amylase, fungal .alpha.-amylase and glucoamylase. The kinetic studies of the inhibitor showed that its inhibitory effect on starch hydrolysis by .alpha.-amylase was non-competitive.

• 한국식품과학회지
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• 제31권6호
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• pp.1421-1426
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• 1999

엿기름의 품질 요소인 당화력(DP)은 보리품종에 따라 큰 차이를 나타내 $139{\sim}220^{\circ}L$의 범위에 있었다. 당화력은 ${\alpha}-amylase$ 보다 ${\beta}-amylase$와 높은 상관관계가 있어 엿기름의 ${\beta}-amylase$ 활성이 매우 중요한 인자였으며, 엿기름 첨가에 따른 amylograph 전분기질 점도 감소는 ${\alpha}-amylase$와 관련이 있는 것으로 확인되었다. 보리품종들의 품질요소들을 분석하여 엿기름 당화력과의 상관관계를 조사한 결과 엿기름의 당화력은 원맥의 품질인자와 상관관계가 별로 높지 않았으나 중량이 낮은 품종이나 덜 풍만한 품종에서 당화력이 높은 경향을 보여주었다. 보리원맥이 지니고 있는 ${\beta}-amylase$ 활성은 엿기름의 당화력과 상관관계가 있는 것으로 평가되었으며 엿기름의 당화력을 예측할 수 있는 잠재적인 당화력으로서 엿기름 제조에 매우 유용한 품질인자인 것으로 판단되었다.

• Journal of Microbiology and Biotechnology
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• 제29권5호
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• pp.765-775
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• 2019

A new ${\alpha}$-amylase-encoding gene (amySL3) of glycoside hydrolase (GH) family 13 was identified in soda lake isolate Alkalibacterium sp. SL3. The deduced AmySL3 shares high identities (82-98%) with putative ${\alpha}$-amylases from the genus Alkalibacterium, but has low identities (<53%) with functionally characterized counterparts. amySL3 was successfully expressed in Escherichia coli, and the recombinant enzyme (rAmySL3) was purified to electrophoretic homogeneity. The optimal temperature and pH of the activity of the purified rAmySL3 were determined to be $45^{\circ}C$ and pH 7.5, respectively. rAmySL3 was found to be extremely halophilic, showing maximal enzyme activity at a nearly saturated concentration of NaCl. Its thermostability was greatly enhanced in the presence of 4 M NaCl, and it was highly stable in 5 M NaCl. Moreover, the enzyme did not require calcium ions for activity, and was strongly resistant to a range of surfactants and hydrophobic organic solvents. The major hydrolysis products of rAmySL3 from soluble starch were maltobiose and maltotriose. The high ratio of acidic amino acids and highly negative electrostatic potential surface might account for the halophilic nature of AmySL3. The extremely halophilic, calcium-independent, and surfactant-resistant properties make AmySL3 a promising candidate enzyme for both basic research and industrial applications.

• 한국미생물·생명공학회지
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• 제17권5호
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• pp.529-532
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• 1989

A strain of Streptomyces sp. (YS-221-B) extracellularly produced an inhibitory substance for $\alpha$-D-Glucosidase. The substance was purified 96-fold from culture filtrate by dialysis, heat treatment, adsorption on active carbon, Bio-Gel P-10 and Sephadex G-75 column chromatography with yield of 9.2%. The substance was stable in pH range from 7.0 to 11.0 at 37$^{\circ}C$, and a treatment at 10$0^{\circ}C$ for 20 min diminished only 15% of the original activity. The inhibitor was not inactivated by the treatment of $\alpha$-, $\beta$-amylases, glucoamylases, trypsin and chymotrypsin but inactivated by pyoteases from Streptomyces griseus and Tritirachium album.

• 한국미생물·생명공학회지
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• 제13권3호
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• pp.223-232
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• 1985

한국의 토양에서 분리한 균 중 bacterial $\alpha$-amylase에 저해효과가 있는 균주를 분리하여 DMC-47 균주라 명명하였고, 이 균주는 Streptomyces 속의 균임을 확인하였다. 이 균주를 옥수수 전분 배지에서 진탕 배양한 결과 4일후에 최대 저해 효과를 나타내었다. 이 균주가 생성한 저해물질은 bacterial $\alpha$-amylase, pancreatic $\alpha$-amylase, salivary $\alpha$-amylase, glucoamylase에 저해효과를 보였고, $\beta$-amylase 에는 저해효과가 없었다.