• Current Research on Agriculture and Life Sciences
• /
• v.7
• /
• pp.153-163
• /
• 1989

The activity changes and biochemical properties of ${\beta}$-gal in tomato fruits during ripening were investigated. The total activity was increased during ripening and three isoenzymes (${\beta}$-gal I, II and III) were purified through DEAE Sephadex A-50 and Sephadex G-100 column chromatography. The activities of ${\beta}$gal isoenzymes (${\beta}$-gal I, II and III) during ripening were 69.8, 31.8 and 170.0 units in mature green phase, while those were 48.7, 88.4 and 136.8 units in Red phase, respectively. As the ripening proceeded the activities of ${\beta}$-gal I and III were some what decreased but the activity of ${\beta}$-gal II was incresed more than 2.8 fold. The optimum pH of ${\beta}$-gal I, II and III were 3.9, 4.2 and 3.9 and the optimum temperature of those were $60^{\circ}C$, $56^{\circ}C$ and $60^{\circ}C$, respectively. All isoenzymes were stable at pH 3.6~6.0 and lost their activity about 50% when it heated at $55^{\circ}C$ for 5 minute. $Mg^{{+}{+}}$-activated the three isoenzymes but $Ca^{{+}{+}}$ and SDS inhibited about 30~40%. $Hg^{{+}{+}}$ inhibited completely. The km value of ${\beta}$-gal I, II and III was 0.36mM, 0.63mM and 0.45mM, reaction rate was rapidly increased until the concentration of substrate was $6.0{\times}10^{-5}M$.

• Microbiology and Biotechnology Letters
• /
• v.16 no.2
• /
• pp.119-125
• /
• 1988

$\beta$-Glucosidase of Cellulomonas sp. CS1-1 in cellular compartment was localized with cell-bound form while Avicelase and carboxymethylcellulase (CMCase) were appeared with extracellular enzyme. Cell growth on cellulose or CMC minimal broth was increased by glucose addition. $\beta$-Glucosidase production on cellobiose or CMC minimal broth was repressed by the addition of glucose. However, on CMC minimal broth, the enzyme production was specially stimulated by cellobiose addition. $\beta$-Glucosidase production was also induced by CMC, starcth and maltose compared with glycerol, arabinose, xylose and trehalose. From the above results, it was concluded that glucose effect on $\beta$-glucosidase biosynthesis showed catabolite repression, but enzyme production was induced by cellobiose, CMC, and starch, indicating that $\beta$-glucosidase is inducible enzyme. Yeast extract stimulated $\beta$-glucosidase production more than peptone and ammonium sulfate. $\beta$-Glucosidase activity was increased with 50mM MgCl$_2$in 10mM potassium phosphate buffer (pH 7.0). Optimum conditions for enzyme activities were pH 6.0 and 42$^{\circ}C$, Km value of $\beta$-glucosidase for p-nitrophenyl-$\beta$-D-glucosidase was 0.256mM and Ki for $\beta$-D(+)-glucose was 9.0mM.

• Korean Journal of Food Science and Technology
• /
• v.37 no.5
• /
• pp.776-782
• /
• 2005

The effects of purification using ${\alpha}-amlyase$ (Termamyl 120L) on physicochemical properties of ${\beta}-glucan$ from oat bran were studied. Four fractions were selected as fraction A ($55^{\circ}C$, 15%, pH 6), fraction B ($45^{\circ}C$, 15%, pH 6), fraction C ($50^{\circ}C$, 0%, pH 7), and fraction D ($50^{\circ}C$, 10%, pH 5) from the result of physiological test, and three consecutive subfractions were obtained by repeated ${\alpha}-amlyase$ treatments on the each fractions. The contents of ${\beta}-glucan$, protein, and ash after purification were in 81.4-88.2%, 4.1-6.3% and 2.6-6.2%, respectively. The apparent viscosities of purified ${\beta}-glucan$ aqueous solutions were similar to those of hydroxy methyl cellulose. Glucose was a major monosaccharide of ${\beta}-glucan$ extracts, and xylose and arabinose were also detected as minor constituents on TLC. The average molecular weight ranged $2.0{\times}10^6-5.1{\times}10^6$ and was decreased after purification. From the result of the differential scanning calorimetry, the melting point ranged $130-140^{\circ}C$ with purification step and thermal transition enthalpy was increased. The ratio of ${\beta}-(1{\rightarrow}3)\;to\;{\beta}-(1{\rightarrow}4) $ linkages were 1:2.22-1:2.52, and increased up to 1:5.50 after purification.

• The Korean Journal of Physiology and Pharmacology
• /
• v.15 no.5
• /
• pp.313-317
• /
• 2011

The effects of extremely low frequency electromagnetic fields (EMF) on intracellular $Ca^{2+}$ mobilization and cellular function in RBL 2H3 cells were investigated. Exposure to EMF (60 Hz, 0.1 or 1 mT) for 4 or 16 h did not produce any cytotoxic effects in RBL 2H3 cells. Melittin, ionomycin and thapsigargin each dose-dependently increased the intracellular $Ca^{2+}$ concentration. The increase of intracellular $Ca^{2+}$ induced by these three agents was not affected by exposure to EMF (60 Hz, 1 mT) for 4 or 16 h in RBL 2H3 cells. To investigate the effect of EMF on exocytosis, we measured beta-hexosaminidase release in RBL 2H3 cells. Basal release of beta-hexosaminidase was $12.3{\pm}2.3%$ in RBL 2H3 cells. Exposure to EMF (60 Hz, 0.1 or 1 mT) for 4 or 16 h did not affect the basal or $1{\mu}m$ melittin-induced beta-hexosaminidase release in RBL 2H3 cells. This study suggests that exposure to EMF (60 Hz, 0.1 or 1 mT), which is the limit of occupational exposure, has no influence on intracellular $Ca^{2+}$ mobilization and cellular function in RBL 2H3 cells.

• Journal of the Korean Ceramic Society
• /
• v.24 no.1
• /
• pp.23-32
• /
• 1987

Synthesis of high purity ultrafine Si3N4 and ${\beta}$-Sialon powders was investigated via the simultaneous reduction and nitriding of amorphous SiO2, SiO2-Al2O3 system prepaerd by hydrolysis of alkoxides, using carbonablack as a reducing agent. In Si(OC2H5)4-C2H5 OH-H2 O-NH4OH system, hydrolysis rate increased with increasing reaction temperature and pH. Pure ${\alpha}$-Si3N4 was formed at 1350$^{\circ}C$ for 5 hrs in N2 atmosphere. In Si(OC2H5)4-Al(OC3H7)3-C6H6-H2 O-NH4OH system, weight loss increased as Si/Al ratio decreased. Single phase ${\beta}$-Sialon consisted of Si/Al=2 was formed at 1350$^{\circ}C$ in N2 and minor phases of ${\alpha}$-Si3N4, AIN, and X-phase were existed besides theSialon phase at other Si/Al ratios. The Si3N4 and Sialon powders synthesized from alkoxides consisted of uniform find particles of 0.05-0.2$\mu\textrm{m}$ in diameter, respectively.

• Proceedings of the Botanical Society of Korea Conference
• /
• 1987.07a
• /
• pp.133-148
• /
• 1987

Gibberellin(GA) 3-$\beta$ hydroxylation is very important for the shoot elogation in the higher plants, since only 3$\beta$-hydryoxylated GAs promote shoot elogation in several plants. Fluctuation of 3$\beta$-hydryoxylase activity was examined during seed maturation using two cultivars of , P. vulgaris, Kentucky Wonder (normal) and Masterpiece (dwarf). Very immature seeds of both cultivars contain high level of 3$\beta$-hydroxylase activity (per mg protein). Both cultivars showed maximum of enzyme activity (per seed) in the middle of their maturation process. Gibberellin 3$\beta$-hydroxylase catalyzing the hydroxylation of GA20 to GA1 was purified 313-fold from very early immature seeds of P. vulgaris. Crude soluble enzyme extracts were purified by 15% methanol precipitation, hydrophobic interaction chromatogrphy, DEAE ion exchange column chromatography and gel filtration HPLC. The 3$\beta$-hydroxylase activity was unstable and lost much of its activity duting the purification. The molecular weight of purified enzyme was extimated to be 42, 000 by gel filtration HPLC and SDS-PAGE. The enzyme exhibited maximum activity at pH 7.7. The Km values for [2.3-3H] GA20 and [2.3-3H]GA9 were 0.29 $\mu$M and 0.33 $\mu$M, respectively. The enzyme requires 2-oxoglutarate as a cosubstrate; the Km value for 2-oxoglutarate was 250 $\mu$M using 3H GA20 as a substrate. Fe2+ and ascorbate significantly activated the enzyme at all purification steps, while catalase and BSA activated the purified enzyme only. The enzyme was inhibited by divalent cations Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+ and Hg2+. Effects of several GAs and GA anaogues on the putrified 3$\beta$-hydroxylase were examined using [3H]GA9 and GA20 as a substrates. Among them, GA5, GA9, GA15, GA20 and GA44 inhibited the enzyme activity. [13C, 3H] GA20 was converted by the partially purified enzyme preparation to [13C, 3H]GA1, GA5 and GA6, which were identified by GC-MS, GA9 was converted only GA4, GA15 and GA44 were converted to GA37 and GA38, respectively. GA5 was epoxidized to GA6 by the preparation. This suggests that 3$\beta$-hydroxylation of GA20 and epoxidation of GA5 are catalyzed by the same enzyme in P, vulgaris.

• Archives of Pharmacal Research
• /
• v.25 no.6
• /
• pp.903-909
• /
• 2002

Research in the cytokine field has grown exponentially in recent years, and the validity of such studies relies heavily on the appropriate measurement of levels of cytokines in various biological samples. Transforming growth factor (TGF)-$\beta$, a hormonally active polypeptide found in normal and transformed tissue, is a potent regulator of cell growth and differentiation. The most widely used bioassay for TGF-$\beta$ is the inhibition of the proliferation of mink lung epithelial cells. Though detection of [$^3$H]thymidine incorporation is more sensitive than the MTT assay, it presents some disadvantages due to the safety and disposal problems associated with radioisotopes. In this study, we attempted to ascertain the experimental conditions which could be used for measuring the in vitro biological activity of TGF-$\beta$ in a safer and more sensitive way compared with the currently available methods. We compared the commonly used method, the MTT assay, to the XTT assay using different parameters including cell number, incubation time and the wave length used for detecting the product. We examined the anti-proliferative activities of TGF-$\beta$ in three different cell lines: Mv-1-Lu mink lung epithelial cells, MCF10A human breast epithelial cells and H-ras-transformed MCF10A cells. Herein, we present an experimental protocol which provides the most sensitive method of quantifying the biological activity of TGF-$\beta$, with a detection limit of as low as 10 pg/ml: Mv-1-Lu or H-ras MCF10A cells ($1{\times}10^5/well$) were incubated with TGF-$\beta$ at $37^{\circ}C$ in a humidified $CO_2$ incubator for 24 hr followed by XTT treatment and determination of absorbance at 450 or 490 nm. Our results may contribute to the establishment of an in vitro bioassay system, which could be used for the satisfactory quantitation of TGF-$\beta$.

• KSBB Journal
• /
• v.15 no.1
• /
• pp.9-13
• /
• 2000

In order to determine the characteristics of $\beta$-glucosidase associated with cellulose degradation, the enzyme produced extracellularly by the mycelia of Tricholoma matsutake DGUM 26001 in culture broth was partially purified. The enzyme activity was maintained in the range of temperatures trom 55 to $70^{\circ}C$ and its optimum temperature was $65^{\circ}C$. The $\beta$-glucosidase enzyme showed relatively high activity in the range of pH 3.0-5.0 and its optimum pH was 4.0. Under the optimal conditions, the specific activity of $\beta$-glucosidase for salicin as a substrate was 18.7 unit/mg protein. After thermal treatment of the enzyme at $55^{\circ}C$ for 60 min, more than 90% of the enzyme activity was still sustained. Iron($Fe^{++}$) stimulated enzyme activity, whereas mercury($Hg^{++}$) and copper($Cu^{++}$) inhibited. Compared to salicin as a substrate, the relative activity for cellobiose was observed to be 48.6%. The apparent $K_m$ and $V_{max}$ of the enzyme with cellobiose were 0.12 mM and 0.02 umol/min, respectively.

• Journal of applied mathematics & informatics
• /
• v.17 no.1_2_3
• /
• pp.49-58
• /
• 2005

In this paper we observe the structure of the roots of q-Bernoulli polynomials, ${\beta}_n(w,h{\mid}q)$, using numerical investigation. By numerical experiments, we demonstrate a remarkably regular structure of the real roots of ${\beta}_n(w,h{\mid}q)$ for $-{\frac{1}{5}},-{\frac{1}{2}}$. Finally, we give a table for numbers of real and complex zeros of ${\beta}_n(w,h{\mid}q)$.

• Journal of Powder Materials
• /
• v.6 no.3
• /
• pp.246-250
• /
• 1999

The effects of the ${\beta}-Si_3N_4$ starting particle size and $\alpha$/$\beta$ phase transformation during sintering process on the microstructure evolution of Yttrium $\alpha$-Sialon ceramics were investigated. As-received ${\beta}-Si_3N_4$ powder (mean particle size: 0.54$\mu$m) and classified ${\beta}-Si_3N_4$ powder(mean particle size: $0.26\mu{m}$) were used as starting powders. With decreasing the starting particle size, the growth of elongated grains was enhanced, which resulted in the whisker -like microstructure with elongated grains. These results were discussed in relation to the two-dimensional nucleation and growth theory. In the specimen heat treated at $1600^{\circ}C$ for 10h before sintering at $1950^{\circ}C$for 1h under 40atm(2-step sintering), the grain size was smaller than of the 1-step sintering at 195$0^{\circ}C$ for 1h. However, bimodal microstructure evolution were not not remarkable in both sample, which is ascribed to the $\alpha$-phase contents existing in ${\beta}-Si_3N_4$ starting powder.