• Microbiology and Biotechnology Letters
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• v.34 no.3
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• pp.228-234
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• 2006

The culture conditions were investigated to maximize the production of laccase from Fomitella fraxinea mycelia. Among the tested media, mushroom complete medium (MCM) showed the highest production of the enzyme. The optimum culture medium was 2% dextrose, 0.4% $(NH_4)_{2}HPO_4$, 0.05% $Na_{2}HPO_{4}{\cdot}7H_{2}O$, and 0.05% KCl as carbon, nitrogen, phosphorus, and inorganic salt sources respectively. SDS-PAGE followed by laccase activity staining using 2,6-djmethoxyphenol as the substrate was performed to identify the laccase activity under culture conditions studied. Zymogram analysis of the culture supernatant showed a laccase band with a molecular mass of 50 kDa. The enzyme production from F. fraxinea was reached to the highest level after the cultivation for 10 days at $25^{\circ}C$ and initial pH 8. The enzyme activity of the culture supernatant was most active at $50^{\circ}C$ and pH 5.

• Textile Coloration and Finishing
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• v.8 no.1
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• pp.15-25
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• 1996

Wool fabric and merino wool top were dyed with two dyes, C.I. Acid Red 13 and C.I. Direct Blue 1 in presence of hydrogen peroxide/glyoxal redox system at various conditions such as dyeing time, temperature and redox concentration. The pH of dye bath was 4.5 in buffer solution of $KH_{2}PO_{4}$ (0.1mol/1)/$Na_{2}HPO_{4}$ (0.1mol/1). Also dyeing of cotton fabric was carried out with C.I. Direct Blue 1 in absence or presence of redox system. The color depth(K/S) increased with redox concentration and dyeing temperature. The increases in dyeing rate and equilibrium dye exhaustion of Acid Acid 13 and Direct Blue 1 on wool fiber and fabric in the present of hydrogen peroxide/glyoxal have been caused by decreasing in pH value during dyeing process which due to the decomposition of hydrogen ion in glyoxal with the assistance of hydrogen peroxide. But the decreases in exhaustion of Direct Blue 1 on cotton may be attributed to repulsive interac ion between salt and salt.

• BMB Reports
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• v.44 no.5
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• pp.341-346
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• 2011

The single-stranded DNA binding activity of the Escherichia coli RecA protein is crucial for homologous recombination to occur. This and other biochemical activities of ssDNA binding proteins may be affected by various factors. In this study, we analyzed the effect of $CaCl_2$, NaCl and $NH_4NO_3$ salts in combination with the pH and nucleotide cofactor effect on the ssDNA-binding activity of RecA. The studies revealed that, in addition to the inhibitory effect, these salts exert also a stimulatory effect on RecA. These effects occur only under very strict conditions, and the presence or absence and the type of nucleotide cofactor play here a major role. It was observed that in contrast to ATP, ATP${\gamma}$S prevented the inhibitory effect of NaCl and $NH_4NO_3$, even at very high salt concentration. These results indicate that ATP${\gamma}$S most likely stabilizes the structure of RecA required for DNA binding, making it resistant to high salt concentrations.

• Microbiology and Biotechnology Letters
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• v.45 no.1
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• pp.12-18
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• 2017

Microbial strains exhibiting proteolytic activity were isolated from kimchi, one of traditional fermented foods in Korea. Eight strains formed clear zones around their colonies when grown on TSA plates supplemented with skim milk. MBE/L865 exhibited 2.6-fold higher protease activity than that of control strain (Bacillus subtilis KCTC13112). MBE/L865 was identified as B. subtilis and deposited in the Korean Collection for Type Cultures under the accession number of KCCM43059. The optimum growth conditions for B. subtilis KCCM43059 were determined to be $37^{\circ}C$ and pH 8. The strain showed maximum protease activity ($429.37{\pm}18.65U/mg$ protein) at $60^{\circ}C$ and pH 6. Further, B. subtilis KCCM43059 had a higher salt (NaCl) tolerance than that of the control strain.

• Food Science and Biotechnology
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• v.15 no.3
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• pp.453-457
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• 2006

Activity and stability of kiwifruit actinidine was determined in various conditions of pH, salt, and temperature using N-${\alpha}$-CBZ-lysine P-nitrophenyl ester as the substrate. Actinidine activity was low below pH 6, and undetectable below pH 3. The enzyme was stable in a pH range of 6.0-8.5. At $4^{\circ}C$ the enzyme was inactive in the presence of greater than 36% vinegar and in 2 M NaCl. Actinidine at $25^{\circ}C$ was unstable in 24% vinegar but stable in up to 3 M NaCl. With regard to freeze-thaw stability, actinidine retained 85% residual activity after being frozen at $-20^{\circ}C$ for 3 days. Based on Arrenius and Lineweaver-Burk plots, actinidine became unstable at greater than $45^{\circ}C$ with only 30% residual activity remaining after 6 min. The Km, kcat, and kcat/Km values of actinidine were $56\;{\mu}M$, 67/sec, and $1.2\;{\mu}M/sec$, respectively.

• Journal of Life Science
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• v.25 no.6
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• pp.673-679
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• 2015

The culture conditions needed to maximize the production of laccase from Pholiota highlandensis mycelia were investigated. Among the tested media for laccase production, Coriolus versicolor medium (CVM; 2% dextrose, 0.4% peptone, 0.6% yeast extract, 0.046% KH₂PO₄, 0.1% K₂HPO₄, 0.05% MgSO₄·7H₂O) showed the highest activity for the enzyme. Then, to optimize culture conditions for laccase activity, the influences of various carbon, nitrogen, phosphorus, and inorganic salt sources in CVM were investigated. The optimum culture medium was 2% fructose, 0.4% peptone with 0.6% yeast extract, 0.05% NaH₂PO₄, and 0.05% MgSO₄·7H₂O as carbon, nitrogen, phosphorus, and inorganic salt sources, respectively. Several aromatic compounds in the medium enhanced laccase activity to varying degrees. Guaiacol induced maximum laccase production, yielding 114.1 U/ml laccase activity after cultivation for 11 days at 25℃. The optimum pH and temperature for laccase production were 8.0 and 35℃, respectively. Native polyacrylamide-gel electrophoresis (PAGE) followed by laccase-activity staining with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) as the substrate was performed to identify the presence of laccase under the optimum conditions studied. Zymogram analysis of the supernatant culture showed an enzymatic band with a molecular mass of about 90 kDa.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.5
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• pp.752-757
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• 1995

The effect of fermentation temperature on the changes of pH, acidity, salt content, color and vitamin C of mustard leaf kimchi during various storage days was investigated. The conditions of fermentation temperature were set at $4^{\circ}C$ (sample A) and $20^{\circ}C$ (sample B), and $4^{\circ}C$ after keeping at $20^{\circ}C$ for 12 hours(sample C) and $20^{\circ}C$ for 36 hours(sample D). As the fermentation proceeded, pH of sample stored at low temperature(sample A) was drop ped gradually from initial pH of 5.24 but there was great pH drop in the sample stored at high temperature(sample B, D). The salt content of the sample B at high temperature increased remarkably, and then the values showed D > A > C. The Humter values of L and a increased at the optimum ripening period, the higher the initial fermentation temperature(B) and the later the initial fermentation time at $20^{\circ}C$ those values, then decreased. The Hunter value of b constantly increased until day of 108. As fermentation time passed, the content of total vitamin C decreased to the range of 9.0mg% to 14.0mg% up to 24 days of fermentation, and at the optimum ripening period, it increased to the range of 14.0mg% to 22.0mg%, and at the fermentation period(until day 108), it decreased gradually.

• Analytical Science and Technology
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• v.16 no.3
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• pp.198-205
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• 2003

The ammonium salt of nitrosophenylhydroxylamine, called cupferron, has been used not only as the ligand but also as an oxidizing agent for adsorptive catalytic stripping voltammetry (AdCtSV). Cyclic voltammetry was used for elucidating the electrochemical behavior of Os-cupferron complex in 1 mM phosphate buffer. The optimal conditions for osmium analysis were found to be 1 mM phosphate buffer solution (pH 6.0) containing 0.1 mM cupferron at scan rate of 100 mV/s. By using the plot of reduction peak currents of linear scan voltammograms vs. osmium concentration, the detection limit was $1.0{\times}10^{-7}M$.

• Korean Journal of Food Science and Technology
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• v.22 no.5
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• pp.569-574
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• 1990

The influence of NaCl and pH on degradation of chicken breast muscle myofibrillar proteins by porcine leukocyte lysosomal proteinases was investigated. The degradation reactions were carried out at $38^{\circ}C$ for 24hours under different conditions. The degradation of myofibrillar proteins by leukocyte lysosomal enzymes at various pH values was limited to partial hydrolysis. Reactions at higher pH values resulted in lower molecular weight degradation products while reactions at lower pH resulted in higher molecular weight degradation products. When NaCl was added into the reaction mixture, enzyme activities of degradation were increased at all pH values studied, as evidenced by NPN-analysis and SDS-PAGE. More severe degradation was observed with higher salt concentration. The concentration of 0.5M NaCl in the reaction mixture gave more degradation of myosin heavy chain by enzyme than that of 0.1M NaCl.

• Journal of Microbiology and Biotechnology
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• v.32 no.7
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• pp.892-901
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• 2022

The rising demand for carotenoids can be met by microbial biosynthesis as a promising alternative to chemical synthesis and plant extraction. Several species of lactic acid bacteria (LAB) specifically produce C₃₀ carotenoids and offer the added probiotic benefit of improved gut health and protection against chronic conditions. In this study, the recently characterized Lactiplantibacillus plantarum subsp. plantarum KCCP11226^T produced the rare C₃₀ carotenoid, 4,4'-diaponeurosporene, and its yield was optimized for industrial production. The one-factor-at-a-time (OFAT) method was used to screen carbon and nitrogen sources, while the abiotic stresses of temperature, pH, and salinity, were evaluated for their effects on 4,4'-diaponeurosporene production. Lactose and beef extract were ideal for optimal carotenoid production at 25℃ incubation in pH 7.0 medium with no salt. The main factors influencing 4,4'-diaponeurosporene yields, namely lactose level, beef extract concentration and initial pH, were enhanced using the Box-Behnken design under response surface methodology (RSM). Compared to commercial MRS medium, there was a 3.3-fold increase in carotenoid production in the optimized conditions of 15% lactose, 8.3% beef extract and initial pH of 6.9, producing a 4,4'-diaponeurosporene concentration of 0.033 A₄₇₀/ml. To substantiate upscaling for industrial application, the optimal aeration rate in a 5 L fermentor was 0.3 vvm. This resulted in a further 3.8-fold increase in 4,4'-diaponeurosporene production, with a concentration of 0.042 A₄₇₀/ml, compared to the flask-scale cultivation in commercial MRS medium. The present work confirms the optimization and scale-up feasibility of enhanced 4,4'-diaponeurosporene production by L. plantarum subsp. plantarum KCCP11226^T.