• Korean Journal of Food Science and Technology
• /
• v.31 no.6
• /
• pp.1458-1464
• /
• 1999

The whole body of three species of fishes, raw anchovy (Engraulis japonica), big eyed herring (Harengula zunasi), and northern sand lance (Ammodytes personatus) catched at the south adjacent coast of Korea, were analyzed for extractive nitrogen, free amino acids, combined amino acids, ATP and its related compounds quaternary ammonium bases, and guanidino compounds using specimens collected in May and July 1991, and the composition of these nitrogenous components were compared with each other. The contents of extractive nitrogen in anchovy, big eyed herring, and northern sand lance were 633 mg, 601 mg, and 455 mg/100 g, respectively. Thirty-one or thirty-two kinds of free amino acids were found in the extracts of the three species of fishes. Histidine, taurine, alanine, leucine, carnosine, glutamic acid, and lysine were the major free amino acids in every sample. The composition of the major extractive components such as free amino acids, combined amino acids, ATP and its related compounds, TMAO, and creatine in the extracts were similar to each other, but their contents were some different individually.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.31 no.3
• /
• pp.361-366
• /
• 2002

A. capillaris Thunberg is often used as a medicinal herb. This analysis on A. capillaris Thunberg, showing its natural ingredients and nutritive elements, is to provide a better understanding of its content and help find more various ways of use. The ingredients of A. capillaris Thunberg are as follows : 14.12% of crude protein, 4.80% of crude lipid, 2.30% of crude ash, 8.10% of crude fiber, and the rest of the ingredients are vitamins and minerals. Minerals are 3295.02 mg% of K, 2787.01 mg% of P, 1436.01 mg% of Ca, 172.32 mg% of Mg, 21.23 mg% of Fe, 18.02 mg% of Mn, 8.11 mg% of Na, 1.24 mg% of Cu, and 0.002 mg% of Sn, and vitamins are 18602.00 ug% of $\beta$-carotene and 5.82 mg% of ascorbic acid. Fatty acids in A. capillaris Thunberg are of 23.86% of oleic acids (C18:1), 46.67% of saturated fatty acids, 33.40% of monousaturated fatty acids, and 19.83% of polyunsaturated fatty acids. Oleic acid (C18:1) is the most abundant fatty acid in A. capillaris Thunberg. P/S is 0.24. A. capillaris Thunberg contains about 20 kinds of amino acid. The total amount of amino acids is 1345.29 mg%, which can be divided into 79.95% of amino acids and 13.11% of essential amino acids. This 79.95% of amino acids consist of proline, tyrosine, asparagines, glutamic acid, and valine with amount of 438.58mg%, 310.20mg%, 120.30mg%, 118.66mg%, and 88.02mg% respectively. The essential amino acid is 176.83mg%. It is shown that A. capillaris Thunberg contatins various nutrients such as minerals, vitamins, fatty acids, and amino acids, so A. capillaris Thunberg can be regarded as a highly nutritious food.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.42 no.6
• /
• pp.574-579
• /
• 2009

Acid- and pepsin-solubilized collagens were extracted from the skin of shark (Isurus oxyrinchus) and their physicochemical properties were characterized by amino acid analysis, SDS-PAGE, the composition of collagen types, solubility and denaturation temperature. Acid - and pepsin-solubilized collagens from shark skin had an imino acid of 188.8 and 186.2 residues/1,000 amino acids, respectively. SDS-PAGE showed two different${\alpha}$ chains ($\alpha1$ and $\alpha2$) and $\beta$-component. The component ratio of type I and V was 10:1, and the type III was not found. Solubility of acid-soluble collagen was low in the range of pH 6.0 to pH 11.0. On the other hand, pepsin-solubilized collagen showed a low solubility in the range of pH 7.0-9.0. Temperature for denaturation of acid- and pepsin-solubilized collagens were $25^{\circ}C$ and $27^{\circ}C$, respectively.

• Journal of Microbiology and Biotechnology
• /
• v.7 no.6
• /
• pp.373-377
• /
• 1997

The gene for isopenicillin N synthase (cyclase; IPNS) was cloned from Lysobacter lactamgenus using DNA probe amplified with primers based on the consensus sequences of isopenicillin N synthase genes of other ${\beta}$-lactam-producing microorganisms. The genomic library of L. lactamgenus using pUC18 plasmid cloned at the SacI site were screened with the PCR-generated DNA probe and three positive clones were isolated. Enzyme activities in E. coli clones were confirmed by bioassay and HPLC assay. Throughout the functional mapping, it was observed that the gene for isopenicillin N synthase is located at the 1.3-kb XhoI-BamHI fragment of insert of positive clones. Nucleotide sequencing at both ends of the XhoI-BamHI fragment revealed that IPNS of L. lactamgenus has the common amino acid sequences at amino- and carboxy-termini.

• Bulletin of the Korean Chemical Society
• /
• v.32 no.5
• /
• pp.1569-1574
• /
• 2011

The presence of replication-competent adenovirus (RCA) subpopulations in adenoviral vector products raises a variety of safety issues for development of therapies based on gene therapy. To analyze the differing effects of adenoviral vector and RCA in vivo, we examined alterations in amino acids (AAs) using rat plasma following injection of ${\beta}$-galactosidase expressing recombinant adenovirus (designated rAdLacZ) or RCA. Plasma AAs were examined by gas chromatography-mass spectrometry. A total of 16 AAs were positively measured. In the rAdLacZ group compared to the control group, the level of aspartic acid was significantly increased (Student's t-test), while the level of glutamic acid was significantly reduced. Additionally, in the RCA group compared to the control group, the level of four AAs, valine, leucine, and isoleucine as branched-chain amino acids, and proline were significantly increased, whereas the levels of three AAs, glycine, threonine, and glutamic acid were significantly reduced. Altered plasma free AA metabolic patterns in rAdLacZ and RCA groups, compared with the control group, may explain the disturbance of AA metabolism related to viral infection.

• Journal of Microbiology and Biotechnology
• /
• v.14 no.6
• /
• pp.1295-1302
• /
• 2004

A gene encoding the mannanase of Bacillus subtilis WL-7, which had been isolated from Korean soybean paste, was cloned into Escherichia coli, and the gene product was purified from the culture filtrate of the recombinant E. coli. This mannanase gene, designated manA, consisted of 1,086 nucleotides, encoding a polypeptide of 362 amino acid residues. The deduced amino acid sequence was highly homologous to those of mannanases belonging to the glycosyl hydrolase family 26. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum at 6.0 and a temperature optimum at $55^{\circ}C$. The enzyme was active on locust bean gum, konjak, guar gum, and lichenan, while it did not exhibit activity towards yeast mannan, laminarin, carboxymethylcellulose, $\beta$­glucan, xylan, and para-nitrophenyl-$\beta$-mannopyranoside.

• Fisheries and Aquatic Sciences
• /
• v.7 no.3
• /
• pp.99-108
• /
• 2004

Vitellogenin (VTG) was purified from serum of $estradiol-l7{\beta}-treated rockfish$(Sebastes schlegeli) by precipitation with $EDTA-Mg^{2+}$ and ammonium sulfate and two step chromatography (anion exchange chromatography and gel permeation chromatography) was performed on FPLC system. Rockfish VTG (rfVTG) was characterized and its properties were determined. The monomers have apparent, molecular mass of about 188 kDa as indicated by SDS-PAGE. Amino acid composition analysis of rfVTG was similar to VTG from other oviparous teleosts. Cysteine and lysine were present at relatively high level. Leucine was present at relatively lower level than in other species. The N-terminal amino acid sequence was evaluated to identify rfVTG. Western blot analysis using an antibody against the purified VTG showed that the antibody reacted with both plasma of $estradiol-l7{\beta}-treated rockfish$ treated male and purified VTG, whereas there was no reaction with male serum of the control. An ELISA was developed using monoclonal and polyclonal antibodies against rfVTG. The assay range was 3.2 ng/mL and 1,000 ng/mL and the value of the intra and inter assay variations were within $9.7{\%}$ and $11.2{\%}$, respectively. Recovery rate was $96.8{\%}$. The sandwich ELISA could be useful for the detection of VTG and could be good for screening of estrogenic compounds.

• Journal of Aquaculture
• /
• v.17 no.1
• /
• pp.62-68
• /
• 2004

A cDNA encoding the masu salmon, Oncorhynchus masou, estrogen receptor $\alpha$ (msER$\alpha$) was cloned from the pituitary gland by polymerase chain reaction (PCR). This cDNA contains an open reading frame encoding 513 amino acid residues, and the calculated molecular weight of this protein is about 56,430 Dalton. The amino acid sequences of the DNA binding and ligand binding domains of msER$\alpha$ showed high homology to those of other fish species (84-100%). Reverse transcription PCR analysis showed that the mRNA level of msER$\alpha$ in the pituitary was slightly higher in estradiol-17$\beta$(E2) injected masu salmon than that of control fish. To test the biological activity of msER$\alpha$, the cDNA was ligated to a mammalian expression vector and transfected into a gonadotrope-derived cell line, L$\beta$T2, with a reporter plasmid including estrogen responsive element. Expression of the reporter protein, luciferase, was E2 and msER$\alpha$-dependent. The masu salmon ER$\alpha$ is structurally conserved among teleost species and functions as a transcriptional activator in the pituitary cells.

• Microbiology and Biotechnology Letters
• /
• v.28 no.4
• /
• pp.195-201
• /
• 2000

Glucoamylase of Saccharomyces diastaticus is produced as a large precursor composed of signal peptide (21 amino acid residues), Thr and Ser-rich region and functional glucoamylase. To evaluate the utility of the glucoamylase signal peptide (GSP) for the secretion of foreign proteins, four types of GSP mutants (ml : Pro-18 longrightarrowLeu-18, m2 : Tyr-13 longrightarrowLeu, m3 : Ser-9longrightarrowLeu-9, m4 : Asn-5 longrightarrowPro-5) were constructed and secretion efficiency of each mutant was compared with that of native GSP by the expression and secretion of Bacillus subtilis CMCase under the control of GAP in N-terminal domain and hydrophobic domain. n mutant 4, a polar amino acid was replaced by a helix - breaking Pro residue. CMCase activity assay and Western blot analysis revealed that CMCase secretion by GSP mutants replaced by Leu were increased compared with native GSP. In the case of m2 and m3, the substitution of Leu for Tyr-13 and Ser-9 in the hydrophobic region resulted in a twofold increase in the extracellular CMCase activity.

• Journal of the Korean Wood Science and Technology
• /
• v.47 no.3
• /
• pp.371-380
• /
• 2019

Termites are pests that cause serious economic and cultural damage by digesting wood cellulose. Termites are arthropods and have an epidermis surrounded by a chitin layer. To maintain a healthy epidermis, termites have chitinase (${\beta}$-1,4-poly-N-acetyl glucosamidinase, EC 3.2.1.14), an enzyme that hydrolyzes the ${\beta}$-1,4 bond of chitin. In this study, the amino acid sequence of the gene, which is presumed to be termite chitinolytic enzyme (NCBI accession no. KC477099), was obtained from a transcriptomic analysis of Reticulitermes speratus KMT001 in Bukhan Mountain, Korea. An NCBI protein BLAST search confirmed that the protein is a glycoside hydrolase family 18 (GH18). The highest homology value found was 47%, with a chitinase from Araneus ventricosus. Phylogenetic analysis indicated that the KC477099 protein has the same origins as those of arthropods but has a very low similarity with other arthropod chitinases, resulting in separation at an early stage of evolution. The KC477099 protein contains two conserved motifs, which encode the general enzymatic characteristics of the GH18 group. The amino acid sequences $Asp^{156}-Trp^{157}-Glu^{158}$, which play an important role in the enzymatic activity of the GH18 group, were also present. This study suggests that the termite KC477099 protein is a new type of chitinase, which is evolutionarily distant from other insect chitinases.