• Analytical Science and Technology
• /
• v.22 no.4
• /
• pp.319-325
• /
• 2009

An effective and specific procedure for confirmation of neomycin, aminoglycoside antibiotic in honey was developed and validated. Honey was adjusted to pH 2 with 0.1M HCl and applied to weak cation-exchange SPE cartridge. Neomycin was eluted with basified methanol. Following separation by ion-pairing liquid chromatography, neomycin was analysed with positive electrospray ionization and MRM mode. Quantification was linear over the range of $5.0{\sim}250.0{\mu}g/kg$ ($r^2$ >0.9951). The precision (R.S.D.) and accuracy (as a bias) of quality control samples in honey ranged 11.5~18.7% and 10.9~20.9%, respectively. Established method can be applied to analysis of neomycin in honey.

• Analytical Science and Technology
• /
• v.20 no.2
• /
• pp.164-169
• /
• 2007

A selective analytical method of LC/MS/MS has been applied to determine the levels of acrylamide in food products. Food samples were 17 including 6 potato chips, and 11 french fries. The analysis of food samples includes extraction with DDDW, clean-up using C18 and mixed ion exchange SPE cartridges and detection by liquid chromatography tandem mass spectrometry. The mobile phase was a mixture of 0.1 % acetic acid and 0.5 % methanol in water. The target ions were identified and determined by ESI mass spectrometer. The overall recoveries were ranged from 91 % to 101 % and the limit of quantitation was $10{\mu}g/kg$. Depending on food kinds, the levels of acrylamide were variable and the average was 0.71 mg/kg for potato chips, and 0.34 mg/kg for french fries.

• Journal of Life Science
• /
• v.11 no.2
• /
• pp.111-115
• /
• 2001

This study was designed to clone the SNF2/SW12 helicase-related genes from the fission yeast Schizosaccha-romyces pombe and thereafter to elucidate the common functions of the proteins in this family. The $hrp^{2+}$gene was cloned by polymerase chain reaction amplification using degenerative primers from conserved SNF2 motifs within the ERCC6 gene, which encodes a protein involved in DNA excision repair. Like other SNF2/SW12 family proteins, the deduced amino acid sequence of Hrp2 contains DNA-dependent ATPase/7 helicase domains as well as the chromodomain and the DNA binding domain. This configuration is similar to that of mCHD1 (mouse chromo-ATPase/helicase-DNA-dinding protein 1), suggesting that Hrp2 is a S. pombe homolog of mCHD1, which is thought to function in altering the chromatin structure to control the gene expression. To characterize the function of Hrp2, 4 Uracil-Hrp2 fusion protein, it was purified near homogeneity by affinity chromatography on $Ni^{2+}$-NTA agarose, DEAE-Sepharose ion exchange arid Sephacryl S-200 gel filtration chromatographies. The purified fusion protein exhibited DNA-dependent ATPase activity, which was stimulated by both double-stranded and single-stranded DNA. To determine the steady-state level of $hrp^{2+}$ transcripts during growth, cells were cultured in medium and collected at every 2hr to prepare total RNAs. The northern blot analysis showed that the level of $hrp^{2+}$ transcripts reached its maximum before the cells entered the exponential growth phase and then decreased gradually, This result implies that Hrp2 may be required at early stages of cell growth.h.

• Mycobiology
• /
• v.51 no.5
• /
• pp.360-371
• /
• 2023

Hispidin is an important styrylpyrone produced by Sanghuangporus sanghuang. To analyze hispidin biosynthesis in S. sanghuang, the transcriptomes of hispidin-producing and non-producing S. sanghuang were determined by Illumina sequencing. Five PKSs were identified using genome annotation. Comparative analysis with the reference transcriptome showed that two PKSs (ShPKS3 and ShPKS4) had low expression levels in four types of media. The gene expression pattern of only ShPKS1 was consistent with the yield variation of hispidin. The combined analyses of gene expression with qPCR and hispidin detection by liquid chromatography-mass spectrometry coupled with ion-trap and time-of-flight technologies (LCMS-IT-TOF) showed that ShPKS1 was involved in hispidin biosynthesis in S. sanghuang. ShPKS1 is a partially reducing PKS gene with extra AMP and ACP domains before the KS domain. The domain architecture of ShPKS1 was AMP-ACP-KS-AT-DH-KR-ACP-ACP. Phylogenetic analysis shows that ShPKS1 and other PKS genes from Hymenochaetaceae form a unique monophyletic clade closely related to the clade containing Agaricales hispidin synthase. Taken together, our data indicate that ShPKS1 is a novel PKS of S. sanghuang involved in hispidin biosynthesis.

• Food Science of Animal Resources
• /
• v.44 no.3
• /
• pp.533-550
• /
• 2024

Peptides with bioactive effects are being researched for various purposes. However, there is a lack of overall research on pork-derived peptides. In this study, we reviewed the process of obtaining bioactive peptides, available analytical methods, and the study of bioactive peptides derived from pork. Pepsin and trypsin, two representative protein digestive enzymes in the body, are hydrolyzed by other cofactors to produce peptides. Bicinchoninic acid assay, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, chromatography, and in vitro digestion simulation systems are utilized to analyze bioactive peptides for protein digestibility and molecular weight distribution. Pork-derived peptides mainly exhibit antioxidant and antihypertensive activities. The antioxidant activity of bioactive peptides increases the accessibility of amino acid residues by disrupting the three-dimensional structure of proteins, affecting free radical scavenging, reactive oxygen species inactivation, and metal ion chelating. In addition, the antihypertensive activity decreases angiotensin II production by inhibiting angiotensin converting enzyme and suppresses blood pressure by blocking the AT1 receptor. Pork-derived bioactive peptides, primarily obtained using papain and pepsin, exhibit significant antioxidant and antihypertensive activities, with most having low molecular weights below 1 kDa. This study may aid in the future development of bioactive peptides and serve as a valuable reference for pork-derived peptides.

• Journal of Ginseng Research
• /
• v.48 no.4
• /
• pp.366-372
• /
• 2024

Background: The biological activity and pharmacological effects of rare ginsenosides have been proven to be superior to those of the major ginsenosides, but they are rarely found in ginseng. Methods: Ginsenoside Rb1 was chemically transformed with the involvement of methanol molecules by a synthesized heterogeneous catalyst 12-HPW@MeSi, which was obtained by the immobilization of 12-phosphotungstic acid on a mesoporous silica framework. High-performance liquid chromatography coupled with mass spectrometry was used to identify the transformation products. Results: A total of 18 transformation products were obtained and identified. Methanol was found to be involved in the formation of 8 products formed by the addition of methanol molecules to the C-24 (25), C-20 (21) or C-20 (22) double bonds of the aglycone. The transformation pathways of ginsenoside Rb1 involved deglycosylation, addition, elimination, cycloaddition, and epimerization reactions. These pathways could be elucidated in terms of the stability of the generated carbenium ion. In addition, 12-HPW@MeSi was able to maintain a 60.5% conversion rate of Rb1 after 5 cycles. Conclusion: Tandem and high-resolution mass spectrometry analysis allowed rapid and accurate identification of the transformation products through the characteristic fragment ions and neutral loss. Rare ginsenosides with methoxyl groups grafted at the C-25 and C-20 positions were obtained for the first time by chemical transformation using the composite catalyst 12-HPW@MeSi, which also enabled cyclic heterogeneous transformation and facile centrifugal separation of ginsenosides. This work provides an efficient and recyclable strategy for the preparation of rare ginsenosides with the involvement of organic molecules.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.44 no.8
• /
• pp.1206-1211
• /
• 2015

Grape juice is consumed worldwide and studied due to the high antioxidant activities and contents. The color of grape juice is due to the presence of phenolic compounds such as anthocyanins. Therefore, color values can be an indicator of antioxidant capacities of grape juice. However, the correlation between color values and antioxidant activities in grape juice has not been well studied. In this study, the physicochemical characteristics and correlation between color values and antioxidant capacities of Korean red grape juices (five commercial juices from market and two juices prepared in the laboratory) were investigated to estimate antioxidant capacities. Antioxidant capacities were determined by 1,1-diphenlyl-2-picrylhydrazyl radical scavenging assay, ferric ion reducing antioxidant power assay, and oxygen radical absorbance capacity assay. Total phenolic contents, total flavonoid contents, and total anthocyanin contents, including five kinds of polyphenolic compounds, were examined by high performance liquid chromatography (HPLC). The results for physicochemical properties showed similar values, except titratable acidity. The color hue values of the prepared juices were higher than those of commercial juices, which was in contrast to the lower color intensity values (P<0.05). The Hunter L, a, and b values showed almost no difference between commercial and prepared juices. The antioxidant activities and total phenolic contents of commercial juices were higher than those of prepared ones. Gallic acid, catechin, and quercetin were confirmed by HPLC in all samples. The total phenolic and total flavonoid contents showed positive correlation with antioxidant activities. In addition, antioxidant activities and contents correlated with color values. Thus, estimation of antioxidant capacity could be feasible through the spectrophotometric measurement of color values.

• Korean Journal of Agricultural Science
• /
• v.18 no.1
• /
• pp.49-73
• /
• 1991

To elucidate enzymatic properties of $\alpha$-galactosidases (EC3, 2, 1, 22) from germinated soybean and Aspergillus niger changes in the enzyme activities and oligosaccharide contents during germination of soybean were determined and $\alpha$-galactosidases from germinated soybean and wheat bran culture of Aspergillus niger were purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. Their chemical and enzymatic properties were investigated and the results obtained were summarized as follows : 1. $\alpha$-Galactosidase activity of soybean was maximized when it was germinated at $25^{\circ}C$ for 120 hours. And raffinose and stachyose in soybean were decomposed completely after 96 hours and 120 hours of germination, respectively. 2. The highest level of $\alpha$-Galactosidase activity was obtained when Aspergillus niger was grown on wheat bran medium at $30^{\circ}C$ for 96 hours. 3. Soybean $\alpha$-galactosidase was purified by 6.6 fold by ammonium slufate fractionation, ion exchange chromatography on DEAE-Cellulose and Sephadex A-50., and gel filtration on Sephadex G-150. Its specific activity was 825 units/mg protein and the yield was 2.5% of the total activity of crude extracts. 4. Aspergillus niger $\alpha$-galactosidase was purified by 23.7 fold. Its specific activity was 1,229 units/mg protein and the yield was 14% of the total activity of wheat bran culture. 5. The purified $\alpha$-galactosidases of soybean and Aspergillus niger were found to be homogeneous by polyacrylamide gel electrophoresis and by HPLC. 6. Chemical properties of the purified $\alpha$-galactosidases were : 1) The soybean $\alpha$-galactosidase was monomeric and its molecular weight was estimated to be 30,000 by SDS-PAGE whereas the Aspergillus niger $\alpha$-galactosidase was a tetrameric glycoprotein which consisted of identical subunits with molecular weight of 28,000 each.

• Journal of the Korean earth science society
• /
• v.34 no.7
• /
• pp.681-692
• /
• 2013

We aimed to evaluate the effectiveness of the Giggenbach bottle method and develop the related pretreatment and analytical methods using artificial fumarolic gases. The artificial fumarolic gases were generated by mixing $CO_2$, CO, $H_2S$, $SO_2$, $H_2$, and $CH_4$ gas streams with a $N_2$ stream sparged through an acidic medium containing HCl and HF, with their compositions varied by adjusting the gas flow rates. The resultant fumarolic gases were collected into an evacuated bottle partially filled with a NaOH absorption solution. While non-condensible gases such as CO, $H_2S$, and $CH_4$ accumulated in the headspace of the bottle, acidic components including $CO_2$, $SO_2$, HCl, and HF that were dissolved into the alkaline solution. Like other acidic components, $H_2S$ also dissolved into the solution, but it reacted with dissolved $Cd^{2+}$ to precipitate as CdS when $Cd(CH_3COO)_2$ was added. The non-condensible gases were analyzed on a gas chromatography. Then, CdS precipitates were separated from the alkaline solution by filtration, and they were pretreated with $H_2O_2$ to oxidize CdS-bound sulfide into sulfate. In addition, a portion of the solution was also pretreated with $H_2O_2$ to oxidize sulfite to sulfate. Following the pretreatment, the resultant samples were analyzed for $SO_4^{2-}$, $Cl^-$ and $F^-$ on an ion chromatography. In the meanwhile, dissolved $CO_2$ was analyzed on a total organic carbon-inorganic carbon analyzer without such pretreatment. According to our experimental results, the measured concentrations of the fumarolic gases were shown to be proportional to the gas flow rates, indicating that the Giggenbach bottle method is adequate for monitoring volcanic gas. The pretreatment and analytical methods employed in this study may also enhance the accuracy and reproducibility of the Giggenbach bottle method.

• Korean Journal of Poultry Science
• /
• v.14 no.2
• /
• pp.103-108
• /
• 1987

This study was conducted to bioassay of amino acid availability of feather meal processed by a different methods, commercial feather meal and raw feather meal, The feather meals were processed by labolatory pressure cooker(autoclave) at 2kg/$\textrm{cm}^2$ for 30 minutes ; 3kg/$\textrm{cm}^2$ for 90 minutes : 4kg/$\textrm{cm}^2$ for 120 minutes. Chick employed in the present experiment were Abor Acre strain, male or meat type (body weight, 100-140g), fed with semipurified diet and protein free diet was given during the determination of the metabolic and endogeneous amino acid. The contents of amino acid of samples were investigated by ion-exchange chromatography. The results were as follows; 1. The amino acid availability of raw, 2kg/$\textrm{cm}^2$ for 30 minutes, commercial, 4kg/$\textrm{cm}^2$ for 120 minutes and 3kg/$\textrm{cm}^2$ for 90 minutes of feather meal were -3.09, 63.28, 67.47, 71.22 and 73.75% respectively. 2. The essential amino acid availability of raw, 2kg/$\textrm{cm}^2$ for 30 minutes, commercial, 4kg/$\textrm{cm}^2$ for 120 minutes and 3kg/$\textrm{cm}^2$ for 90 minutes of feather meal were 2.55, 66.78, 66.89, 72,56 and 73.62%, respectively. 3. In individual amino acid of the different processing loather meal and commercial feather meal, biovailabilities were increased methionine, phenylalanine, leucine, arginine, threonine, isoleucine, however, histidine, lysine and aspartic acid were remarkely decreased. In conclusion, the bioavailability or amino acid for the feather meal processed at 3kg/$\textrm{cm}^2$ for 90 minutes was superior to those of other treatment or raw feather meal.