• Journal of Microbiology and Biotechnology
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• v.19 no.10
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• pp.1161-1168
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• 2009

Ethanol production by the simultaneous saccharification and fermentation (SSF) of low-value rice wine cake (RWC) without cooking was investigated. RWC is the filtered solid waste of fermented rice wine mash and contains 53% raw starch. For the SSF, the RWC slurry was mixed with the raw-starch-digesting enzyme of Rhizopus sp. and yeast, where the yeast strain was selected from 300 strains and identified as Saccharomyces cerevisiae KV25. The highest efficiency (94%) of ethanol production was achieved when the uncooked RWC slurry contained 23.03% starch. The optimal SSF conditions were determined as 1.125 units of the raw-starch-digesting enzyme per gram of RWC, a fermentation temperature of $30^{\circ}C$, slurry pH of 4.5, 36-h-old seeding culture, initial yeast cell number of $2{\times}10^7$ per ml of slurry, 17 mM of urea as the nitrogen additive, 0.25 mM of $Cu^{2+}$ as the metal ion additive, and a fermentation time of 90 h. Under these optimal conditions, the ethanol production resulting from the SSF of the uncooked RWC slurry was improved to 16.8% (v/v) from 15.1% (v/v) of pre-optimization.

• Microbiology and Biotechnology Letters
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• v.47 no.4
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• pp.555-564
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• 2019

Biodiesel is produced through the transesterification process in the presence of alcohol and a catalyst that catalyzes the conversion of triglycerides to esters and glycerol compounds. A more optimal product conversion can be achieved using enzymes, such as lipase. Lipase is reported to be produced in osmophilic yeasts due to the low water content in their natural habitats. Wild forest honey is one of the osmophilic natural habitats in Indonesia. However, lipase-producing yeast has not been reported in the Indonesian honey. In this study, we screened the lipase-producing yeasts isolated from wild forest honey collected from Central Sulawesi. The production profile and activity of lipase were determined at different pH values and temperatures. One promising yeast was isolated from the honey, which was identified as Zygosaccharomyces mellis SG 1.2 based on ITS sequence. The maximum lipase production (24.56 ± 1.30 U/mg biomass) was achieved by culturing the strain in a medium containing 2% olive oil as a carbon source at pH 7 and 30℃ for 40 h. The optimum pH and temperature for lipase activity were 6 and 55℃, respectively. The enzyme maintained 80% of its activity upon incubation at 25℃ for 4 h. However, the enzyme activity decreased by more than 50% upon incubation at 35 and 40℃ for 2 h. This is the first study to report the lipase producing capability of Z. mellis. Further studies are needed to optimize the enzyme production.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.232-237
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• 2005

The cellulloytic enzymes, such as FPase and amylase, production by Trichoderma inhamatum KSJ1 using 10L air circulation bioreactor were tried. Physical properties of the employed bioreactor, mixing time, $k_{L}$ a were examined in airflow conditions of enzyme production cultures. Mixing time of distilled water at 0.6, 1.2, 1.8 vvm were 25, 21, 9 sec, respectively, and mandel's medium using rice straw and pulp as carbon sources were 31, 25, 15 sec. Mixing time decreased when airflow rate increased. $k_L$ a of distilled water at 0.6, 1.2, 1.8 vvm were measured -22.52, -29.31, -39.62, respectively, and the mandel's medium were -47.8, -18.5, -21.4. The $k_L$ a values was increased linearly as the air-flow rates increased. However the values in mandel's medium showed different results, especially at 0.6 vvm. Amylase and FPase activity at the 1.2 vvm was 3.39U/mL, 0.72U/mL in 5 days cultivation. and the activities at 0.6 vvm were 2.01U/mL, 0.39U/mL, respectively. The enzyme productivity at 1.2 vvm was higher than at 0.6 vvm, indicating that high oxygen tension is requested for the efficient enzyme production culture of T. inhamatum KSJ1.

• The Korean Journal of Food And Nutrition
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• v.18 no.1
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• pp.39-47
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• 2005

Using the bacteria isolated from Chungkookjang, Bacillus sublilis MG410 which is excellent in fibrinolytic enzyme activity was isolated. In increase the high production of fibrinolytic enzyme from Bacillus sublilis MG410, the effect of various carbon sources, nitrogen sources, inorganic sources, the initial pH of medium were investigated. The most effective carbon and nitrogen sources were founded cellobiose 0.5%(w/v) and soybean meal 2%(w/v) respectively. None of inorganic sources examined had any detectable stimulating effect on fibrinolytic enzyme production except Na₂HPO₄·12H₂O. The initial optimum pH for fibrinolytic enzyme production ranged from 5∼6 and agitation speed was effect at 150rpm. In jar fermentor experiments under optimal culture conditions, the activity of fibrinolytic enzyme reached about 5.050 unit after 48hours.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.6
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• pp.904-909
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• 2005

To produce functional food ingredient from the soybean curd residue (SCR), alkaline fermentation was performed with SCR from cold processed (D-SCR) or hot processed (P-SCR) tofu. The solid- state fermentation was performed by Bacillus firmus NA-1 at $42^{\circ}C$. The fermentation of heat-treated D- SCR resulted in higher production of peptides and fibrinolytic enzyme compared with D-SCR without heating. The P-SCR showed higher production of peptides, fibrinolytic enzyme, indicating alkaline pH after fermentation for 18 hr. When the moisture content of P-SCR was reduced to $60\%$, the production of peptides and fibrinolytic enzyme were enhanced. The P-SCR fortified with $10\%$ MFS (micronized full-fat soy flour) showed higher fibrinolytic enzyme activity and consistency index by fermentation of Bacillus firmus NA-1 Furthermore, the P- SCR fortified with $20\%$ MFS indicated relatively higher peptide content, fibrinolytic enzyme activity and enhanced flavor. By increasing the addition of MFS, the peptide content of fermented P-SCR was increased significantly, but fibrinolytic enzyme was slightly decreased.

• Journal of Life Science
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• v.20 no.6
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• pp.902-906
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• 2010

A producer of thermophilic extracellular lipase, Geobacillus kaustophilus DSM 7263, was selected from various microorganisms of the Geobacillus genus. We investigated optimum conditions for mass production of G. kaustophilus lipase. Among the different natural oil media, olive oil was optimal for enzyme production. The maximum amount of enzyme production was obtained when G. kaustophilus was grown in a medium containing 0.5% olive oil as a carbon source. The pH and temperature for optimal growth were pH 8.0 and $55^{\circ}C$, respectively, while the optimum pH and temperature for lipase production were pH 6.0 and $50^{\circ}C$, respectively. In the presence of $Mg^{2+}$ and $Mn^{2+}$, lipase production was dramatically enhanced by 247% and 157%, respectively, whereas enzyme production was inhibited by $Zn^{2+}$, $Cu^{2+}$, and $Cd^{2+}$. The addition of 0.1% (v/v) triton X-100 increased lipase production and cell growth when compared to the negative control.

• Microbiology and Biotechnology Letters
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• v.27 no.6
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• pp.471-476
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• 1999

Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseII) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAIII) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650M and gel filtration of Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH6.5~7.0 and $55{\circ}C$, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to $60^{\circ}C$. The Km of this enzyme for DFAIII production was 11.9mM. The enzyme was inactivated by $Hg^{2+}$ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition of DFAIII.

• Korean Journal of Microbiology
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• v.15 no.4
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• pp.145-153
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• 1977

Penicillin amidase (EC 3.5.1.11) was produced by a mutant strain of Bacillius megaterium ATCC 14945. Hydroxylamine assay method for the determination of 6-APT was modified by using "HCl addition techniques" in order to simplify the time consuming orginal assay method without sacrifice of accuracy. Using the new mutant strain, the effects of fermentation conditions on enzyme production were studied.e studied.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.1
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• pp.29-33
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• 1997

The efficient production of glucose isomerase (G. I0.) produced form Arthrobacter sp. L-3 was studied. The optimum culture time of the enzyme was 40hr. The maximum enzyme activity was found at glucose concentration 1%. G. I. activity did not affect inoculum size. The glucose isomerase activity was strongly influenced by the addition of glucose.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.2
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• pp.439-442
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• 2004

Bacterial strains showing the firinolytic and $\beta$-glucosidase activity were screened from Doeniang. The strain of KH-15 revealed a high level of fibrinolytic and $\beta$-gluocosidase activity. The isolated bacterium was identified and desingnated as Bacillus sp. KH-15. The carbon, nitrogen and salts sgnificantly influenced te fibrinolytic enzyme and $\beta$-glucosidase production. The optimized composition of medium appeared to be 2％ glucose, 0.5% yeast extract and 0.1% calcium chloride. The optimum pH and temperature for fibrinolytic enzyme and $\beta$-glucosidase activities were pH 7∼8, 4$0^{\circ}C$ and pH 6∼8, 30∼4$0^{\circ}C$, respectively.