• Asian-Australasian Journal of Animal Sciences
• /
• 제31권8호
• /
• pp.1267-1274
• /
• 2018

Objective: The objective of the study was to investigate the effects of zinc amino acid complex (ZnAA) on growth performance, hematological and biochemical parameters in weanling pigs. Methods: In Exp. 1, a total of 216 Duroc${\times}$Landrace${\times}$Large White weanling pigs were assigned randomly to 6 dietary treatments. Each treatment had 6 replicates (pens) with 6 pigs each. The diets were corn-soybean meal based with supplementation of 0, 20, 40, 80, 120 mg Zn/kg from ZnAA or 40 mg Zn/kg from feed-grade zinc sulfate. The experiment lasted 42 days. In Exp. 2, a total of 180 weanling pigs were assigned randomly to 3 dietary treatments supplemented with 0, 80, or 800 mg Zn/kg from ZnAA. Results: In Exp. 1, pigs fed 40 to 80 mg Zn/kg from ZnAA had higher (p<0.05) average daily gain (ADG) than the unsupplemented group during d 0 to 14. During d 0 to 42, the pigs fed 20 to 120 mg Zn/kg from ZnAA had increased (p<0.05) ADG. Pigs fed 20 to 120 mg/kg Zn from ZnAA had lower feed:gain (p<0.05), increased the activity of serum Cu-Zn superoxide dismutase on d 14, and increased serum Zn levels on d 42 (p<0.05). In Exp. 2, pigs fed diets with 800 mg Zn/kg had increased average daily feed intake during d 15 to 28 (p<0.05) compared to the unsupplemented group. During d 0 to 28, the pigs fed supplemental Zn had increased ADG (p<0.05). On d 14 and d 28, pigs fed supplemental Zn had higher the serum alkaline phosphatase activities (p<0.05). No significant differences were observed in the hematological parameters and organ indices. Conclusion: Supplementation with 20 to 80 mg/kg Zn from ZnAA improved the growth performance in weaned pigs. The piglets can tolerate up to 800 mg/kg Zn from ZnAA with limited potential health effects.

• Bulletin of the Korean Chemical Society
• /
• 제19권6호
• /
• pp.654-660
• /
• 1998

$[Fe^{II}Fe^{III}BPLMP(OAc)_2](BPh_4)_2$ (1), a new model for the reduced form of the purple acid phosphatases, has been synthesized by using a dinucleating ligand, 2,6-bis[((2-pyridylmethyl)(6-methyl-2-pyridylmethyl)amino) methyl]-4-methylphenol (HBPLMP). Complex I has been characterized by X-ray diffraction method as having (μ-phenoxo)bis(acetato)diiron core. Complex 1 was crystallized in the monoclinic space group C2/c with the following cell parameters: a=41.620(6) Å, b=14.020(3) Å, c=27.007(4) Å, β=90.60(2)°, and Z=8. The iron centers in the complex 1 are ordered as indicated by the difference in the Fe-O bond lengths which match well with typical $Fe^{III}-O\; and\; Fe^{II}-O$ bond lengths. Complex 1 has been studied by electronic spectral, NMR, EPR, SQUID, and electochemical methods. Complex 1 exhibits strong bands at 592 nm, 1380 nm in $CH_3CN$ (ε = 1.0 × 103 , 3.0 × 102). These are assigned to $phenolate-to-Fe^{III}$ and intervalence charge-transfer transitions, respectively. Its NMR spectrum exhibits sharp isotropically shifted resonances, which number half of those expected for a valence-trapped species, indicating that electron transfer between $Fe^{II}\;and\;Fe^{III}$ centers is faster than NMR time scale. This complex undergoes quasireversible one-electron redox processes. The $Fe^{III}_2/Fe^{II}Fe^{III}\;and\;Fe^{II}Fe^{III}/Fe^{II}_2$ redox couples are at 0.655 and -0.085 V vs SCE, respectively. It has $K_{comp}=3.3{\times}10^{12}$ representing that BPLMP/bis(acetate) ligand combination stabilizes a mixed-valence $Fe^{II}Fe^{III}$ complex in the air. Complex 1 exhibits a broad EPR signal centered near g=1.55 which is a characteristic feature of the antiferromagnetically coupled high-spin $Fe^{II}Fe^{III}$ system $(S_{total}=1/2)$. This is consistent with the magnetic susceptibility study showing the weak antiferromagnetic coupling $(J= - 4.6\;cm^{-1},\; H= - 2JS_1{\cdot}S2)$ between $Fe^{II}\; and \;Fe^{III}$center.

• 한국식품영양과학회지
• /
• 제43권5호
• /
• pp.756-762
• /
• 2014

전통 장류 유래 효소 활성 및 항균 활성 우수 Bacillus sp.를 스타터로 한 콩 발효물의 품질 특성을 분석하였다. 총균수는 HJ5-2를 접종한 시료가 $3.00{\times}10^9CFU/mL$로 가장 높았으며, 유산균은 스타터 첨가 콩 발효물에서 $2.50{\times}10^2{\sim}7.30{\times}10^4CFU/mL$를 나타나는 것으로 보아 접종된 균주가 우점종이 된 것을 확인하였다. ${\alpha}$-Amylase 활성은 RD7-7(20.82 unit/mL)과 HJ18-4(18.45 unit/mL), protease 활성은 RD7-7(647.92 unit/mL)을 접종한 콩 발효물이 높은 활성을 나타내었다. 환원당 함량은 HJ18-4(2.35%), 아미노태 질소 함량은 RD7-7(227.96 mg%) 접종 콩 발효물에서 높은 함량을 나타내었다. 아미노산 함량은 glutamic acid, aspartic acid, leucine, lysine, arginine 순으로 검출되었다. 유기산은 oxalic acid(36.51~63.57 mg/100 g)가 모든 실험군에서 검출되었으며, succinic acid(600.15~429.49 mg/100 g)는 control과 RD7-7 접종 콩 발효물에서 검출되었다. 향기 성분을 분석한 결과 총 28종(esters 3종, ketones 6종, aldehydes 2종, alcohols 4종, hydrocarbons 2종, pyrazines 2종, acids 4종, 기타 4종)이 검출되었으며, RD7-7과 HJ18-4를 접종한 콩 발효물에서 23종의 향기 성분이 검출되었다. 본 연구는 고품질 장류용 스타터 개발을 위한 단일균 접종 콩 적용 시험으로 향후 혼합배양 스타터 개발 및 기능성 콩 발효소재 개발을 위한 기초자료로 제시하고자 한다.

• Journal of Microbiology and Biotechnology
• /
• 제15권5호
• /
• pp.1094-1099
• /
• 2005

Photosynthetic dinoflagellates contain a water-soluble, light-harvesting antenna called the peridinin-chlorophyll-protein (PCP) complex, which has an apoprotein with no sequence similarity to other known proteins. There are two forms of PCP apoproteins; the 15-kDa short form and the 32- to 35­kDa long form. The present study describes the PCP protein and its cDNA from Alexandrium tamarense. A cDNA library was constructed from mRNA isolated from A. tamarense. The complete PCP cDNA was generated by reverse-transcription coupled to polymerase chain reaction (RT-PCR), together with rapid-amplification of cDNA ends (RACE). The A. tamarense PCP cDNA encoded a 55-amino acid signal peptide and a 313-amino acid mature protein with a calculated mass of 32 kDa, which corresponded to that of the long form of PCP. Phylogenetic analysis indicated that the sequence of A. tamarense PCP did not cluster with the short-form PCPs, to which it was only about $55\%$ identical, but which were $79-83\%$ identical to other long-form PCPs. The deduced amino acid sequence of A. tamarense PCP contains an internal duplication, which suggests the possibility that long-form PCPs arose by gene duplication or by the fusion of genes encoding the short form. The abundance of PCP mRNA changed substantially in response to different light conditions, indicating the possible existence of a photo-acclimation response in A. tamarense.

• 한국식품영양학회지
• /
• 제10권4호
• /
• pp.528-532
• /
• 1997

새조개 여체부의 긴발을 제외한 나머지인 가공 부산물을 식량자원으로서 효율적 이용을 위한 한 방안으로 효소분해 후 가수분해물의 물성을 개선하여 다소의 조직감을 갖는 반고형 상태의 페이스트 젓갈의 제조와 품질개선에 관하여 검토하였다. 새조개 가공부산물에 절반량의 물과 4% Protease N. P.를 첨가하여 가수분해 후 여과하여 그 여액에 4% glucose를 첨가하여 10$0^{\circ}C$에서1시간 열처리하여 풍미개선, 효소의 불활성화 및 멸균을 시켰다. 물성개량제 즉 0.5% alginic acid, 1% pectin, 0.2% agar를 병용 첨가한 제품이 대조구에 비하여 조직감 및 물성개선의 효과를 나타내었고, 10,000 rpm에서 60분간 원심분리 후에도 조직감이 파괴되지 않아 그 때의 혼합안정성은 98.1%였다. 페이스트 젓갈의 성분은 수분 함량 57.7%, 총당 함량 20.6%, 총질소함향 1,458% 및 아미노질소량 1,187mg%이었으며, 총질소중 아미노질소가 차지하는 비율은 81.4%였다.

• Journal of Microbiology and Biotechnology
• /
• 제16권9호
• /
• pp.1434-1440
• /
• 2006

The stable anchorage of pyridoxal 5'-phosphate (PLP) in the active site of D-amino acid transaminase (D-AT) is crucial for the enzyme catalysis. The three-dimensional structure of D-AT revealed that Glu32 is one of the active site groups that may playa role in PLP binding. To prove the role of Glu32 in PLP stability, we firstly checked the rate of the potential rate-limiting step. The kinetic analysis showed that the rate of the ${\alpha}$-deprotonation step reduced to 26-folds in E32A mutant enzyme. Spectral analyses of the reaction of D-AT with D-serine revealed that the E32A mutant enzyme failed to stabilize the key enzyme-substrate intermediate, namely a quinonoid intermediate (E-Q). Finally, analysis of circular dichroism (CD) on the wild-type and E32A mutant enzymes showed that the optical activity of PLP in the enzyme active site was lost by the removal of the carboxylic group, proving that Glu32 is indeed involved in the cofactor anchorage. The results suggested that the electrostatic interaction network through the groups from PLP, Glu32, His47, and Arg50, which was observed from the three-dimensional structure of the enzyme, plays a crucial role in the stable anchorage of the cofactor to give necessary torsion to the plane of the cofactor-substrate complex.

• Journal of Microbiology and Biotechnology
• /
• 제8권2호
• /
• pp.146-151
• /
• 1998

The aminoglycoside multiple-resistance determinant from Streptoalloteichus hindustanus was cloned into Streptomyces lividans and named nbrB. The 1.2-kb ApaI- BclI fragment encompassing nbrB was located within a 2.6-kb ApaI fragment by successive subcloning experiments. The complete DNA nucleotide sequence of 1.2-kb containing nbrB was determined. The sequence contains an open reading frame that putatively encodes a polypeptide of 281 amino acids with a predicted molecular weight of 30,992. The deduced amino acid sequence of nbrB shows identities of 85.1% to kgmB of S. tenebrarius, 59.6% to sgm of Micromonospora zionensis, and 57.7% to grm of M. rosea. The similarity of nbrB to kgmB suggests that nbrB encodes a 16S rRNA methylase similar to that encoded by kgmB and that both genes might be derived from a common ancestral gene.

• Bulletin of the Korean Chemical Society
• /
• 제20권12호
• /
• pp.1475-1478
• /
• 1999

Ligand field calculations have been performed based on the data from the absorption and low temperature sharp-line excitation spectra of fac-Cr(gly)₃, fac-Cr(L-serine)₃ · 2H₂O and fac-Cr(L-leucine)₃·2H₂O. The optimized ligand field parameters for all complexes show that the carboxylate and the amino groups are moderate σ-donor. The values of $e_{{\pi}O}$ are typical of other complexes with carboxylate ligands. However, the π-interaction of carboxylic oxygen to the chromium in serinato complex is much weaker than that of other complexes. The inclusion of π-anisotropy is necessary to adequately explain the large doublet splittings.

• Archives of Pharmacal Research
• /
• 제12권1호
• /
• pp.58-61
• /
• 1989

Studies of selectivity of hydrogen bond formation in chiral solute-solvent systems have been performed by $^1H\;and\;^{13}C$ nuclear magnetic resonance techniques. These data are correlated with the results of gas chromatographic investigations of the same systems. Interactions between the optically active solvent(N-(N-benzoyl-L-amino acid)-anilide) and optically active solute (N-trifluoroacetyl -L-alanyl isopropyl ester) were examined. NMR evidence indicated that hydrogen bonding interaction occurred between two N-H portion and on peptidyl carbonyl portion in stationary phase and solute molecule on three points. The association constants of solvent-solute interaction were calculated and the structure of the diastereomeric association complex between N-(N-benzoyl-L-valyl)-anilide and N-TFA-L-alanyl isopropyl ester was proposed.

• 한국수산과학회지
• /
• 제46권4호
• /
• pp.359-364
• /
• 2013

Inordinate stress causes disorders of various systems in humans and activates defense mechanisms to maintain homeostasis in the body. Sleep is a vital, highly organized process regulated by complex systems of neuronal networks and neurotransmitters. Sleep is an essential biological process whose underlying regulating involves numerous anatomical structures and biochemical substances that can be compromised by stress and by the immune system. Gamma-amino butyric acid (GABA) is the main inhibitory neurotransmitter of the central nervous system, and activation of GABAA receptors is known to favor sleep. This study was conducted to evaluate the possible application of Lactobacillus brevis BJ20 fermentation to improve the functional qualities of sea tangle Saccharina japonica and oyster Crassostrea gigas. Antioxidant activity was determined by assaying levels of radical scavenging activity against 1,1-diphenyl-2-picrylhydrazyl (DPPH) and superoxide. L. brevis BJ20 fermentation of sea tangle and oyster enhanced both antioxidant and antiinflammatory activities. These results suggested that L. brevis BJ20 fermented sea tangle and oyster could be used for alleviation of stress and to promote sleep.