• Journal of Life Science
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• 제11권2호
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• pp.92-93
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• 2001

Bacillus sp. KYJ 963, which was isolated from Korean salt-fermented anchovy (anchovy-jeot), produces an extracellular ${\beta}$-amylase. The analysis of the digestion products of substrates by thin layer chromatography from the purified protein revealed that the enzyme could not hydrolyze maltose or ${\alpha}$-cyclodextrin. In the amino acid composition analysis, the major characteristic of the ${\beta}$-amylase was the high proportion of amino acids that possess short side chain such as glycine and alanine.

• 한국미생물·생명공학회지
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• 제27권3호
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• pp.203-207
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• 1999

V. alginolyticus 138-2, a marine halophilic bacterium, produced an extracellular amylase with a molecular weight of ca. 56,000. The analysis of the digestion products of soluble starch by thin layer chromatography(TLC) revealed that the extracellular amylase of V. alginolyticus 138-2 is a saccharifying-type alpha-amylase. The alpha-amylase activity of the culture supernatant of soluble starch was optimal at pH 6.0 and 45$^{\circ}C$. Ca2+ slightly increased the alpha-amylase activity, whereas Hg2+, An2+, Cu2+, Ni2+, Fe2+, and Mn2+inhibited the enzymatic activity. Alkylating thiol group agent, iodoacetic acid did not affect the alpha-amylase activity, but reduced thiol reagents such as dithiothreitol, cysteine, and beta-mercaptoethanol stimulated theenzymatic activity. On the other hand, even if V. alginolyticus 138-2 is a marine halophilic bacterium, its alpha-amylase activity was significantly inhibited by NaCl.

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2001년도 제31회 학술심포지움 및 춘계학술대회
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• pp.37-37
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• 2001

• 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.

• 한국식품영양과학회지
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• 제16권2호
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• pp.128-135
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• 1987

고온성 cellulose 분해이용세균인 Herpetosiphon geysericola CUM 317 균주가 생성하는 ${\alpha}-amylase$, ${\beta}-amylase$ 및 glucoamylase를 황산암모늄 염석, DEAE-cellulose chromatography, CM-cellulose chromatography 방법으로 각각 부분정제하였다. 이들 ${\alpha}-amylase$, ${\beta}-amylase$ 및 glucoamylase의 감자 전분에 대한 Km치는 $2.31mg/m{\ell}$, $7.69mg/m{\ell}$ 및 $8.33mg/m{\ell}$였으며, 각 분자량은 84,000 dalton, 76,000 dalton 및 80,000 dalton의 크기로 나타났다.

• Mycobiology
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• 제39권2호
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• pp.118-120
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• 2011

The ability of Ganoderma to produce extracellular enzymes, including ${\beta}$-glucosidase, cellulase, avicelase, pectinase, xylanase, protease, amylase, and ligninase was tested in chromogenic media. ${\beta}$-glucosidase showed the highest activity, among the eight tested enzymes. In particular, Ganoderma neo-japonicum showed significantly stronger activity for ${\beta}$-glucosidase than that of the other enzymes. Two Ganoderma lucidum isolates showed moderate activity for avicelase; however, Ganoderma neojaponicum showed the strongest activity. Moderate ligninase activity was only observed in Ganoderma neo-japonicum. In contrast, pectinase, amylase, protease, and cellulase were not present in Ganoderma. The results show that the degree of activity of the tested enzymes varied depending on the Ganoderma species tested.

• Journal of Microbiology and Biotechnology
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• 제18권4호
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• pp.695-703
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• 2008

A locally isolated thermophile, Geobacillus sp. SAB-40, producing thermostable extracellular amylase constitutively and an induced intracellular ${\beta}$-galactosidase was characterized and identified based on 16S rRNA sequencing. A phylogenetic analysis then revealed its closeness to Geobacillus stearothermophilus. To evaluate the effect of the culture conditions on the coproduction of both enzymes by G stearothermophilus SAB-40, a Plackett-Burman fractional factorial design was applied to determine the impact of twenty variables. Among the tested variables, $CaCI_2$, the incubation time, $MgSO_4{\cdot}7H_2O$, and tryptone were found to be the most significant for encouraging amylase production. Lactose was found to promote ${\beta}$-galactosidase production, whereas starch had a significantly negative effect on lactase production. Based on a statistical analysis, a preoptimized medium attained the maximum production of amylase and ${\beta}$-galactosidase at 23.29 U/ml/ min and 12,958 U/mg biomass, respectively, which was 3-and 2-fold higher than the yield of amylase and lactase obtained with the basal medium, respectively.

• 한국식품영양학회지
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• 제7권4호
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• pp.259-266
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• 1994

The hyperthermophilic archaebacterium Thermococcus profundus Isolated from a deep-sea hydrothermal vent system, produced several amylolytic enzymes such as extracellular amylase and pullulanase, intracellular a-1,4-91ucosidase in respone to the presence of complex carbohydrates In the growth medium. This strain showed high activities on 0.5% maltose than on complex carbohydrates One of the amylases was partially purified by ammonium sulfate precipitation, DEAE-Toyopearl chromatography. The amylase exhibited maximal activity at pH 5.5 and 80$^{\circ}C$, and was stable in the range of pH 5.5 to 9.5 and up to 80$^{\circ}C$ for 30 min. The enzyme activity was no dependence on Ca2+ and not inhibited by detergents. The amylase hydrolyzed soluble starch, amylose, amylopectin and glycogen to produce maltose and maltotriose with trace amounts of glucose, but not pullulan and ${\alpha}$-, ${\beta}$-, ${\gamma}$-cyclodextrin. Malto-oligosaccharides ranging from maltotetraose to maltoheptaose were hydrolyzed in an endo fashion.

• 한국균학회지
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• 제26권4호통권87호
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• pp.496-501
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• 1998

송이균사(Tricholoma matsutake DGUM 26001, DGUM 26101, DGUM 26210, FRI 91024)를 사용하여 균사의 효소활성을 측정하였다. $24^{\circ}C$에서 30일간 배양후 그 여액을 조효소 용액으로 사용하였을 때, ${\alpha}-amylase$ 효소의 평균 비활성은 6142.3 unit/mg protein이었다. 배양여액 중의 xylanase의 세포의 효소활성은 상대적으로 높았으나, ${\beta}-glucosidase$, ligninase, CMCase, chitinase, pretense및 lipase의 효소활성은 낮거나 거의 없었다.

• 한국미생물·생명공학회지
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• 제25권2호
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• pp.109-114
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• 1997

The Oomycete Saprolegnia ferax produces an extracellular $\beta$-amylase, Maximum enzyme yield was attained after 7 days of growth in YNB starch medium (pH 6.5) at 25$\circ$C. The amylase was pu- rified 24-fold by ultrafitration, HPLC DEAE column and HPLC gel filtration. The purfied enzyme was a monomeric glycoprotein with a molecular weight of about 44,000 dalton. The pH and temperature optima were 6.5 and 50$\circ$C, respectively. The enzyme was fairly stable up to 50$\circ$C and at acidic pH region (pH 4.0-7.0). The apparent Km and Vmax values of the enzyme against soluble starch were 0.77 mg/ml and 2,174 $\mu$moles/mg protein, respectively. Amino acid analysis indicated that the enzyme was enriched in alanine, glycine, leucine and acidic amino acid. Starch hydrolysis with the enzyme released maltose but not glucose, whereas maltotriose, Schardinger dextrin ($\alpha$-cyclodextrin) and pullulan were not hydrolysed by the enzyme. The enzyme was inhibited by Schardinger dextrin, p-chloromercuribenzoate(PCMB), CU$^{2+}$' and Hg$^{2+}$. Inhibition of the enzyme by PCMB could be reversed by the addition of cysteine and mercaptoethanol.