• Microbiology and Biotechnology Letters
• /
• v.28 no.4
• /
• pp.219-222
• /
• 2000

To produce and utilize microbial cyclomaltodextrinase being industrially useful, we isolated an alkalophilic Bacillus strain from soil which was capable of degrading cyclodextrins. The newly isolated strain was aerobic, gram-positive, spore-forming, motile, rod shape(0.2~0.4$\times$1.4~4.4 $\mu\textrm{m}$), and 35.8 mol% of DNA base composition. Based on its morphological, phisiological, and biochemical properties, it was identified as alkalophilic Bacillus sp. KJ-133 and cultivated well in the ranges of $30~40^{\circ}C$ and pH 8.0~9.0 . The cyclomaltodextrinase of the strain showed maximal production after 48h of cultivation at $37^{\circ}C$, and the activity was inhibited by Ag2+, Hg2+, Cu2+, and p-chloromercuribenzoate.

• Journal of Microbiology and Biotechnology
• /
• v.11 no.4
• /
• pp.558-563
• /
• 2001

A new alkalophilic strain of Bacillus pumilus JB¬05 producing bleach-stable and halo-tolerant alkaline protease was isolated from cement industry effluents in Karnataka, India. The effects of carbon and nitrogen sources on protease production by this alkalophilic strain were observed after a 30-h incubation. A high level of alkaline protease activity was obtained in the presence of starch as the carbon and peptone as the nitrogen sources. The partially purified enzyme showed an optimum temperature and pH activity at $58^{\circ}C$ and 10.5, respectively. The enzyme was completely inhibited by PMSF (95.0%) indicating it as a serine protease. It is bleach-stable as it retained 35% original activity in the presence of 10% (v/v) hydrogen peroxide at $30^{\circ}$C after 2 h and is halo-tolerant as it retained 70% original activity in the presence of 2.5 M sodium chloride at $30^{\circ}C$ after 2 h incubation.

• The Korean Journal of Food And Nutrition
• /
• v.8 no.3
• /
• pp.253-261
• /
• 1995

A strain of alkalophilic Bacillus sp. C-21 has been Isolated from sold. The strain was capable of producing large amount of cyclodextrin glycosyltransferase (CGTase) in the high alkaline pH medium. The preferable medium composition was determined to be as follows : 1.0% soluble starch, 1.0% peptone, 0.5% yeast extract, 0.1% K2HP04, 0.02% MgSO4.7H2O and 1.0% Na2CO3(pH 10.0) The highest enzyme production was observed after 30hours of cultivation at 33$^{\circ}C$. The optimum temperature and pH for the activity of crude enzyme were 6$0^{\circ}C$ and 6.0, respectively. The enzyme was stable between pH 6.0 and 9.6, and up to 55$^{\circ}C$.

• Microbiology and Biotechnology Letters
• /
• v.21 no.2
• /
• pp.119-124
• /
• 1993

An alkalophilic microorganism for overproduction of cyclodextrin glucanotransferase (CGTase) was newly isolated from hot-water spring soil, and identified as Bacillus firmus var. alkalophilus H609. The strain maintained stability during preservation and cultivation for the enzyme production, and produced significant amount of CGTase corresponding to the volumetric activity of 75 units/mL at 37C, initial pH of 11.2, and after 40 hours. The strain excreted several different proteins showing CGTase activity that catalyzed the formation of mainly beta-and Gamma-type cyclodextrin (ratio of 7:1) from soluble starch without accumulation of alpha-type. Other enzymatic properties were also investigated.

• Textile Coloration and Finishing
• /
• v.22 no.2
• /
• pp.145-154
• /
• 2010

An alkalophilic microorganism capable of degrading dyes was developed for the treatment of alkaline dye solution. This strain was identified as Pseudomonas species. Using this microorganism, biological treatment of dye was studied in Erlenmeyer flasks. The characteristics of this microorganism were observed under various incubating-condition such as temperature, pH, nitrogen source, and macronutrients concentration. The removal effciencies of Disperse Red 60 from synthetic wastewater were 33.5 ~ 36.9% at the range of $30{\sim}40^{\circ}C$, and they were 31.1 ~ 36.7% at the range of initial pH 8 ~ pH 10, respectively. The optimal culture medium was found to be 0.25%(w/v) yeast extract, 0.25%(w/v) polypeptone, 0.1%(w/v) $KH_2PO_4$, 0.2%(w/v) $MgSO_4{\cdot}7H_2O$, and 1.0%(w/v) $Na_2CO_3$. In treatment of various dyes using Erlenmeyer flasks, the removal effciencies of Disperse Blue 87, Disperse Yellow 64, Disperse Red 60, Acid Blue 193, Acid Red 138, and Direct Yellow 23 were found to be 76%, 71%, 58%, 93%, 94%, and 90% respectively after 24hrs reaction of alkalophilic strain Pseudomonas sp. YBE-12.

• Journal of Industrial Technology
• /
• v.7
• /
• pp.59-68
• /
• 1987

In order to obtain a strain of producing lipase which has resistance against alkaline and detergent, a screening test was carried out. Among 500 strains isolated from soil samples, the strain J-19 was selected for this study. The composition of the optimum medium for the highest lipase production was 2.0% glycerin, 1.0% corn steep liquor, 2.0% yeast extract, 0.1% $MgSO_4$ $7H_2O$, 0.2% $K_2HPO_4$, 1.5% soybean oil and 0.1% LAS(linear alkylbenzene sulfonate) with initial pH value of 10.0 and 3-day cultivation at $25^{\circ}C$. The lipase activity of the strain J-19 under optimal condition was 3.3. units/ml, which was increased about 1.3-fold than that of basal medium.

• Microbiology and Biotechnology Letters
• /
• v.17 no.5
• /
• pp.524-528
• /
• 1989

A $\beta$-Galactosidase producing strain, Alkalophilic Bacillus sp, YS-309, has been isolated from soil sample. The strain was capable of producing large amount of intracellular $\beta$-galactosidase in the alkaline media rather than in the neutral media. The preferable medium composition has been determined to be as follows: 0.5% lactose, 0.5% yeast extract, 0.5% soybean meal, 0.1% KH$_2$PO$_4$, 0.02% MgSO$_4$7$H_2O$ 0,0.6% Na$_2$CO$_3$ (pH 9.9). The enzyme was produced by lactose or IPTG as in-ducer. But both Enzyme synthesis and cellular growth were decreased when lactose was added at the higher concentrations than 1.5% (v/v).

• Journal of Microbiology and Biotechnology
• /
• v.8 no.5
• /
• pp.501-508
• /
• 1998

An alkalophilic mi.croorganism (strain YB380), which produces yeast cell wall hydrolase extracellulary, was isolated from Korean soil. The rod-shaped cells were 0.3~0.4 by 2~4${\mu}{\textrm}{m}$ long, motile, aerobic, gram-positive, and spore-forming. The color of the colony was light yellow. The temperature range for growth at pH 9.0 was 25 to $45{\circ}C, with optimum growth at $35{\circ}C. The pH range for growth at $35{\circ}C was 8 to 11 with an optimum pH of 9.0. Therefore, the strain YB380 is an obligate alkalophile. The 16S rRNA of strain YB380 has a 99% sequence similarity with that of Bacillus alcalophilus. On the basis of physiological properties, cell wall fatty acid composition, and phylogenetic analysis, we propose that the isolated strain is Bacillus alcalophilus. The yeast cell wall hydrolase from Bacillus alcalophilus subsp. YB380 has been purified and partially characterized. The molecular weight was estimated to be 27,000 daltons with an optimum temperature and pH of $60{\circ}C and 9.0, respectively. The N-terminal amino acid sequence of the enzyme was analyzed as Gln- Thr- Val- Pro- Trp- Gly- Ile- Asn- Arg- Val.

• Microbiology and Biotechnology Letters
• /
• v.23 no.2
• /
• pp.197-202
• /
• 1995

The conditions for the $\beta$-fructofuranosidase production from alkalophilic, thermophilic Bacillus sp. TA-11 were investigated. The maximal enzyme production was obtained when the strain was cultured at 50$\circ$C for 36 hrs with batch culture in the optimal medium containing 1.0% sucrose, 0.6% yeast extract, 0.1% each of KH$_{2}$PO$_{4}$, K$_{2}$HP0$_{4}$, NaH$_{2}$PO$_{4}$, and initial pH 9.5, and the final enzyme activity under the above condition was 102 units per ml of cell free extract.

• Microbiology and Biotechnology Letters
• /
• v.17 no.6
• /
• pp.587-592
• /
• 1989

A strain of alkalophilic Bacillus sp. YS-309 capable of producing large amount of $\beta$-galactosidase has been isolated from soil sample. Intracellular $\beta$-galactosidase was purified 6.9 folds by procedures including ammonium sulfate precipitation, DEAE-cellulose chromatography, gel-filtration, DEAE-Sephadex A-50 chromatography with over-all yield of 17.8%. The molecular weight of native enzyme was 205, 000 by HPLC, and SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of 4 identical subunits with a molecular weight of 56, 000.