• Applied Biological Chemistry
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• v.38 no.6
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• pp.502-506
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• 1995

A Bacillus strain which produces ${\beta}-galactosidase$ with high transgalactosylation activity, was isolated from soil and tentatively designated as Bacillus sp. A1. When ${\beta}-galactosidase$ from Bacillus sp. A1 reacted with 40% (w/w) lactose, transgalactosylation ratio reached up to 90% at the 70% conversion of the initial lactose. The biosynthesis of the enzyme in Bacillus sp. A1 required lactose as an inducer and was repressed by glucose. Observing that the addition of amino acids to culture medium resulted in enhancing, to a significant extent, both the growth and the enzyme production of the strain, yeast extract and commercially available hydrolysates of protein were examined for the suitability as amino acid source. As it turned out, SMP, an enzymatic hydrolysis product of soybean protein from Fuji Oil Co.(Japan), was the most suitable for optimization of the culture medium. When Bacillus sp. A1 was cultured in the presence of 0.5% SMP and 2% lactose, the enzyme activity increased up to $1.8\;U/m{\ell}-broth$.

• Journal of Microbiology and Biotechnology
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• v.33 no.1
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• pp.127-134
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• 2023

Laccase activity is influenced by copper (Cu) as an inducer. In this study, laccase was immobilized on Cu and Cu-magnetic (Cu/Fe₂O₄) nanoparticles (NPs) to improve enzyme stability and potential applications. The Cu/Fe₂O₄ NPs functionally activated by 3-aminopropyltriethoxysilane and glutaraldehyde exhibited an immobilization yield and relative activity (RA) of 93.1 and 140%, respectively. Under optimized conditions, Cu/Fe₂O₄ NPs showed high loading of laccase up to 285 mg/g of support and maximum RA of 140% at a pH 5.0 after 24 h of incubation (4℃). Immobilized laccase, as Cu/Fe₂O₄-laccase, had a higher optimum pH (4.0) and temperature (45℃) than those of a free enzyme. The pH and temperature profiles were significantly improved through immobilization. Cu/Fe₂O₄-laccase exhibited 25-fold higher thermal stability at 65℃ and retained residual activity of 91.8% after 10 cycles of reuse. The degradation of bisphenols was 3.9-fold higher with Cu/Fe₂O₄-laccase than that with the free enzyme. To the best of our knowledge, Rhus vernicifera laccase immobilization on Cu or Cu/Fe₂O₄ NPs has not yet been reported. This investigation revealed that laccase immobilization on Cu/Fe₂O₄ NPs is desirable for efficient enzyme loading and high relative activity, with remarkable bisphenol A degradation potential.

• Applied Biological Chemistry
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• v.11
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• pp.55-61
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• 1969

This K-17 strain was not absolutely requiring xylose as an inducer for enzyme formations. The most activity of this enzyme was lost when treated at $75^{\circ}C$. for 30 hours but was not influenced at $70^{\circ}C$. for 70 hours of treatment. The activity of this enzyme was increased by the addition of magnesium ions or cobalt ions in the reaction system. In the studies, we found that the magnesium ions simply activate the enzyme reaction and the cobalt ions do not but protect the enzyme from heat inactvation. And it was also found the phosphate buffer solution was very suitable as glucose dissolving solvent on the enzyme reaction. The mixed carbon source medium containing glucose, fructose, sorbitol, xylose and sucrose was more favorable for enzyme production then a sole carbon source containing medium on the shaking culture method.

• Proceedings of the Korean Environmental Health Society Conference
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• 2005.11a
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• pp.166-168
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• 2005

The induction of heme oxygenase-1(HO-1) by ultraviolet(UV) radiation provides a protective defense against oxidative stress, and has been well demonstrated in UVA-irradiated skin, but not UVB. In this study in mice, we show that the UVB(290-320nm) radiation can be attributed to the induction of cutaneous heme oxygenase-1. The expression of HO-1 mRNA was assessed in vivo by the reverse transcription-polymerase chain reaction (RT-PCR) analysis, and HO-1 enzyme activity was measured in microsomal preparation from irradiated mice. The mRNA level of HO-1 increases in liver and skin from 24h to 72h after UVB($3KJ/m^3$) radiation. The results of gene expression were same pattern of HO enzyme activity in skin, but not in liver. HO-1 mRNA in liver resulted in a progressive increase to 96h after UVB radiation, but HO activity in liver increased to 48h. This finding indicates that UVB radiation is an important inducer of HO-1 and increases in HO activity may protect tissues directly or indirectly from oxidative stress.

• Journal of Environmental Health Sciences
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• v.34 no.1
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• pp.49-54
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• 2008

The induction of heme oxygenase-1(HO-1) by UV radiation provides a protective defence against oxidative stress, and has been well demonstrated in skin irradiated with UVA, but not UVB. In this study, we show that the induction of cutaneous HO-l can be attributed to UVB radiation. The expression of HO-1 mRNA was assessed in vivo by reverse transcription-polymerase chain reaction (RT-PCR) analysis, and HO-1 enzyme activity was measured in microsomal preparation from irradiated mice. The mRNA level of HO-1 increases in liver and skin from 1d to 3d after UVB $(3KJ/m^2)$ exposure. The results of gene expression were same pattern of HO-1 enzyme activity in skin, but not in liver. HO-1 mRNA in liver resulted in a progressive increase to 4d after UVB exposure, but HO-1 activity in liver increased to 2d. This finding indicates that UVB radiation is an important inducer of HO-1 and increases in HO activity may protect tissue directly or indirectly from oxidative stress.

• Journal of Microbiology and Biotechnology
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• v.6 no.1
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• pp.12-18
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• 1996

A chitosanase-producing bacteria was isolated on chitosan agar plate from soil samples. The strain was spore-forming gram positive bacteria, catalase positive, and rod shape. The strain was identified as Bacillus cereus. The strain did not need an inducer for the synthesis of chitosanase. Chitosanase from Bacillus sp. HW-002 was constitutive enzyme. The optimal medium for the production of the enzyme was composed of 0.5$\%$ sucrose and $1.5\%$ yeast extract-tryptone (1:1 w/w) mixture at pH 6.5. After Bacillus sp. HW-002 was cultivated at $32^{\circ}C$ for 32 h, maximal productivity was gained to be about 27, 200 U/l. Chitosanase from Bacillus sp. HW-002 was a mixed growth-linked metabolite.

• Microbiology and Biotechnology Letters
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• v.17 no.5
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• pp.524-528
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• 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
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• v.35 no.2
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• pp.141-148
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• 1997

Alcaligenes xylosoxydans strain SMN3 capable of utilizing biphenyl grew not only on phenol, and benzoate, but also on salicylate. Catabolisms of biphenyl and salicylate appear to be interrelated since benzoate is a common metabolic intermediate of these compounds. Enzyme levels in the excatechol 2. 3-dioxygenas which is meta-cleavage enzyme of catechol, but did not induce catechol 1, 2-dioxygenase. All the oxidative enzymes of biphenyl and 2, 3,-dihydroxybiphenyl (23DHBP) were induced when the cells were grown on biphenyl and salicylate, respectively. Biphenyl and salicylate could be a good inducer in the oxidation of biphenyl and 2, 3-dihydroxybiphenyl. The two enzymes for the degradation of biphenyl and salicylate were induced after growth on either biphenyl or salicylate, suggesting the presence of a common regulatory element. However, benzoate could not induce the enzymes responsible for the oxidation of these compounds. Biphenyl and salicylate were good inducers for indigo formation due to the activity of biphenyl dioxygenase. These results suggested that indole oxidation is a property of bacterial dioxygenase that form cis-dihydrodiols from aromatic hydrocarbon including biphenyl.

• Korean Journal of Pharmacognosy
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• v.34 no.4 s.135
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• pp.297-302
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• 2003

Cnidii Rhizoma water extract (CRW) was tested for liver cancer chemopreventive potential by measuring the inhibition of phase I enzyme and benzo[a]pyrene-DNA adduct formation and induction of phase II detoxification enzymes. There was 17.0% inhibition in the activity of cytochrome P450 1A1 enzyme with the treatment of 150 mg/ml CRW. At concentration of 30 mg/ml CRW, the binding of $[^3H]B[a]P$ metablites to DNA of NCTC-clone 1469 cell was inhibited by 33.3%. CRW was potent inducer of quinone reductase (QR) and glutathione S-transferase (GST) activities in cultured murine hepatoma Hepalc1c7 cells. However, hepatic glutathione (GSH) level was not influenced by CRW. These findings suggest that CRW has chemopreventive potential of liver cancer by inhibiting cytochrome P450 1A1 activity and benzo[a]pyrene-DNA adduct formation and inducing QR and GST activities.

• Applied Biological Chemistry
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• v.47 no.3
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• pp.287-292
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• 2004

The optimum conditions for lignin peroxidase production were studied. Lignin peroxidase was produced almost exclusively in stationary culture with the optimum media composition of malt extract 1 g, yeast extract 0.4 g, glucose 0.4 g and distilled water 100 ml. Tween 80 at 0.005% concentration and veratryl alcohol at 0.4 mM were very effective inducers for lignin peroxidase production.