• 한국수산과학회지
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• 제15권1호
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• pp.52-58
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• 1982

염기성 아미노산 (lysine, histidine, arginine)의 과잉투여가 흰쥐의 체중 및 혈액중의 urea nitrogen 농도에 미치는 영향을 조사하였다. $10\%$ casein 먹이와 염기성 아미노산이 각각 $5\%$씩 첨가된 먹이로 28일간 사육한 결과는 아래와 같다. 1. 염기성 아미노산이 과잉 투여된 군은 대조군($10\%$ casein diet)에 비하여 성장율과 사료 섭취율이 감소되었으며 L-histidine HCl 첨가군의 성장이 가장 저조했다. 2. 혈액중의 urea nitrogen 의 농도는 염기성 아미노산이 과잉 투여된 군이 대조군에 비하여 모두 높았으며 L-arginine 첨가군이 가장 높았다. 3. 혈액중의 urea nitron 농도는 사료에 포함된 질소의 양과 관계가 있으며 성장량과는 무관한 것으로 나타났다.

• 한국식품영양과학회지
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• 제36권6호
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• pp.766-772
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• 2007

참치가공 부산물의 효율적 이용을 위하여 건강 기능성이 고려된 참치 자숙액 조미 소스의 제조를 시도하였고, 그 특성에 대하여도 살펴보았다. 참치 조미 소스는 단백질이 11.8%로 시판 조미 소스의 약 2배에 해당하였고, pH, brix 및 염도는 각각 $577,348^{\circ}$ 및 11.9%이었다. 관능검사 결과, 참치 조미 소스는 시판 조미 소스에 비하여 맛, 냄새 및 색조에 있어 차이가 없었다. ACE 저해능은 참치 조미 소스가 시판 조미 소스(9.9 mg/mL)에 비하여 37% 정도 높았고, 항산화능은 20 mM ascorbic acid에 비하여는 약하였으나 인지는 되었다. 참치 조미 소스는 총 유리아미노산 함량이 1,905.2 mg/100 mL로 시판 조미 소스(712.7 mg/100 mL)에 비하여 약 2.7배 높았으며, 주요 유리아미노산은 taurine, glutamic acid, histidine 및 anserine이었다. 참치 조미 소스는 total taste value가 58.65로 시판 조미 소스의 34.30에 비하여 맛의 강도가 훨씬 강하리라 추정되었고, 맛에 크게 기여하는 주요 아미노산으로는 glutamic acid 및 histidine 등이었다. 총 아미노산 함량은 참치 조미 소스가 10,965 mg/100 mL로 시판 조미 소스의 4,818 mg/100 mL에 비하여 높았고, 참치 조미 소스의 주요 구성 아미노산으로는 glutamic acid, proline, histidine 및 glycine 등이었다. 참치 조미 소스의 섭취에 의한 무기질 강화 효과는 기대하기 어려우리라 판단되었다.

• Macromolecular Research
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• 제17권11호
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• pp.912-918
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• 2009

An optically active diacid containing the L-histidine moiety was prepared by reacting pyromellitic dianhydride (1,2,4,5-benzenetetracarboxylic acid 1,2,4,5-dianhydride) 1 with L-histidine 2 in acetic acid, and was polymerized with several aromatic diamines 5a-g to obtain a new series of optically active poly(amide-imide)s (PAIs) using two different methods, such as direct polycondensation in a medium consisting of N-methyl-2-pyrrolidone (NMP)/triphenyl phosphite (TPP)/calcium chloride ($CaCl_2$)/pyridine (Py) and direct polycondensation in a tosyl chloride (TsCl)/pyridine (Py)/N,N-dimethylformamide (DMF) system as a condensation agent. The resulting new polymers 6a-g with inherent viscosity was obtained in good yield. The polymers were readily soluble in polar organic solvents, such as N,N-dimethyacetamide (DMAc), N,N-dimethyformamide (DMF), and dimethyl sulfoxide (DMSO). The obtained polymers were characterized by FTIR, specific rotation, elemental analysis as well as $^1$H-NMR spectroscopy and gel permeation chromatography (GPC). The thermal stability of the resulting PAIs was evaluated with thermogravimetric analysis techniques under a nitrogen atmosphere.

• Bulletin of the Korean Chemical Society
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• 제32권1호
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• pp.53-58
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• 2011

Cysteine and histidine-capped water-dispersible ZnS:Mn nanocrystals (ZnS:Mn-Cys and ZnS:Mn-His) were synthesized and their effects on E. coli and human cells were investigated. Particle sizes of these nanocrystals were found from HR-TEM images to be 3.5 nm and 4.0 nm, respectively. Their solution photoluminescence spectra showed identical broad emission peaks at 580 nm. ZnS:Mn-His significantly suppressed the growth of E. coli at $100{\mu}g/mL$ and 1 mg/mL concentrations, something not observed with ZnS:Mn-Cys. Consistent with this, greater inhibition of cell proliferation and viability were observed in HEK293 and IMR90 cells in ZnS:Mn-His at $100{\mu}g/mL$ and 1 mg/mL concentrations.

• 한국식품조리과학회지
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• 제23권2호통권98호
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• pp.221-226
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• 2007

This study was carried out to investigate the optimun conditions for the isolation of low molecular weight peptides containing histidine, and to evaluate the antioxidant effects of skipjack boiled extracts(SBE). The results are summarized as follows : L-histidine contents of the ordinary muscle and dark muscle extracts were $ 83.1{\pm}1.75{\mu}M/g\;and\;11.0{\pm}2.39\;{\mu}M/g$, respectively. The L-histidine level of the dark muscle was much lower than that of ordinary muscle in the SBE. The extracts were treated with alcalase and neutrase under different pH levels, temperatures, and times. The optimum hydrolysis conditions of SBE were pH 7.0 and a $60^{\circ}$C temperature for 2 hr in the batch reactor, which hydrolyzed 63% of the SBE. HPLC analysis showed a removing effect of the ultrafiltration permeate (UFP) to high molecular weight impurities in SBE. SBE and pure carnosine participated as inhibiting agents to, which was confirmed through the autoxidation processing of linoleic acid. UFP treatment improved the inhibiting ability of SBE to the autoxidation of linoleic acid. The reducing power of the UFP-treated ordinary muscle extracts were 10-fold higher than the dark muscle extracts, and 0.7-fold higher than 20 mM pure carnosine. The UFP-treated ordinary muscle extracts had greater reducing power activity than pure carnosine. The scavenging activities on DPPH radical of the different treated-SBE and pure carnosine were also investigated. Scavenging activities of the ordinary and dark muscle extracts and the pure carnosine were 90%, 70%, and 45%, respectively. In summary, Skipjack boiled extracts (SBE) demonstrated that low molecular weight peptides containing histidine are capable of inhibiting lipid oxidation. They also possessed effective abilities as free radical scavengers and reducing agents, and these activities may increase with increasing concentrations.

• 환경생물
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• 제22권1호
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• pp.148-152
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• 2004

본 실험은 백두산 자생 참돌꽃의 발아조건과 종자, 유식물 및 뿌리유래 캘러스의 유리 아미노산 조성과 함량을 조사하여 다음과 같은 결과를 얻었다. 뿌리로부터 캘러스 유도는 2,4-D 및 NAA가 첨가된 MS배지에서 유도되었다. 캘러스 형성율은 2,4-D 2.0 mg $L^{-1}$에 kinetin 1.0 mg $L^{-1}$ 혼용 처리구가 NAA 2.0 mg $L^{-1}$에 kinetin 1.0 mg $L^{-1}$ 혼용 처리구보다 캘러스 형성율이 높았다. 유리 아미노산은 종자, 줄기, 뿌리 그리고 캘러스에서 aspartic acid, glutamic acid, serine 및 glycine 등의 25∼26종이 검출되었으며 종자, 줄기 그리고 뿌리부위에서는 lysine이 가장 많은 양을 나타냈으며 캘러스에서는 histidine이 높은 양을 나타냈다. 전체적인 유리아미노산 분포는 lysine, histidine 및 arginine의 함량이 높아 참돌꽃 유식물 및 캘러스의 경우 염기성 아미노산의 분포가 높은 식물임을 알 수 있었다. 또한 총 유리 아미노산 함량은 종자와 뿌리, 줄기에 비해 캘러스에서 신선중 g당 500∼l,000$\mu$mo1e정도 높아 우수한 약리작용을 지니고 있는 참돌꽃의 성분을 배양세포를 통하여 대량생산이 가능함을 시사하고 있다.

• 미생물학회지
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• 제12권3호
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• pp.115-130
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• 1974

Searches for the nutrition requirements of three strains of Brevibacterium ammoniagenes reported in the previous paper were carried out with an aim of achieving the striking accumulation of L-glutamic acid and the large multipication of cells. It was recognized that all three strains required both biotin and thiamine, together with amino acids such as histidine or cysteine, for their good growth and extracellular L-glutamic acid accumulation. The quantity of biotin required for remarkable growth of these microorganisms was quite different from that for the maximum production of L-glutamic acid. This result, however, did not apply in the case of thiamine. It was also confirmed that, of 18 amino acids, histidine and cysteine were the msot effective organic nitrogen sources, while the most available inorganic ammonium salt resulting in a large amount of L-glutamic acid-production and considerable cell gorwth was found to be only urea. Maximum accumulation of extracellular L-glutamic acid, more than 50%(w/w) of the initial sugar content, could be obtained from fermentation in the medium containing wheat-bran extract(Brev. ammoniagenes T-1 and Brev.ammoniagenes Y-2) or rice-bran extract(Brev. ammoniagenes YR-2), which confirmed us a possibility that these bacteria might be employed for industrial fermentation of L-glutamic acid.

• 한국식품영양학회지
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• 제12권4호
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• pp.421-426
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• 1999

The major flavor compounds of Takju mash which was brewed with a modified Nuruk made by inocu-lation and cultivation of Rhizopus japonicus T2, Aspergillus oryzae L2 and Hansenula sp. BC26 isolated from Nuruk, were analyzed, as compared with those with current fermenting agents such as commerical Nur-uk and rice koji of Aspergillus kawachii. The contents of isoamyl alcohol isobutyl alcohol and ethyl acet-ate which were known as aroma compounds in Takju were much higher in mash of modified Nuruk than in that of commercial Nuruk or ricd koji. The major organic acids were lactic fumalic and succinic acid in mash of modified and lactic and acetic acid in mash of commercial Nuruk and citric lactic and suc-cinic acid in mash of rice koji. The contents of total organic acids were 5,146mg/L, 1,706mg/L and 1, 388 mg/L in mash of commercial Nuruk rice koji and modified Nuruk respectively. The major free amino acids were glutamic acid alanine proline and histidine in mash of modified Nuruk and glutamic acid proline leucine and histidine in mash of commercial Nuruk and arginine proline and glutamic acid in mash of rice koji. The contents of total free amino acids were 14,090mg/L 12,202mg/L and 7,152 mg/L in mash of modified Nuruk commercial Nurcuk and rice koji respectively. Therefore it seemed that the Takju mash of modified Nuruk was better than that of commercial Nuruk or rice koji.

• 대한화학회지
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• 제5권1호
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• pp.33-37
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• 1961

We have shown that carboxy-peptidase destroys the biological activity of angiotensin octa-and deca-peptides. Since Proline occurs as the seventh amino acid from the amino end of the chain and since carboxypeptidase does not cleave proline from a peptid chain, it is evident that the heptapeptid H.asp-arg-val-tyr-ileu-his-pro.OH is formed by this hydrolysis. This peptide must then be biologically inactive. In order to determine whether the phenyl group of the C-terminal amino acid was the necessary requirement for biological activity of the octapeptide, $ala^8$ angiotensin octapeptide(amino acids of peptides numbered from amino end) was synthesized. For this synthesis the four dipeptides were prepared: carbobenzoxy-L-prolyl-L-alanine-P-nitrobenzyl-ester, m.p. $134-135^{\circ}C,$ carbobenzoxy-L-isoleucyl-imidazole benzyl-L-histidine methyl ester, m.p. $114-116^{\circ}C,$ carbobenzoxy-L-valyl-L-tyrosine hydrazide and carbobenzoxy B-benzyl-L-aspartyl-nitro-L-arginine. The first three dipeptides were obtained as crystalline compounds. Imidazole-benzyl-L-histidine was used in the hope that it would block the histidine imidazole against side reactions in steps subsequent to the formation of the C-terminal tetrapeptide. Also, it was through that the imidazole benzylated peptides would be easier to crystallize. This, however, was not the case. The tetrapeptide, carbobenzoxy-L-isoleucyl-L-im, benzyl-histidyl, L-prolyl-L-alanine-nitrobenzyl ester was not obtained in a crystalline form. Neither could the mono-or dihydrobromide of the tetrapeptide free base be induced to crystallize. Carbobenzoxy-L-valyl-L-tyrosine azide was condensed with the tetrapeptide free base to yield the protected hexapeptide; carbobenzoxy-L-valyl-L-tyrosyl-L-isoleucyl-L-im, benzyl, histidyl-L-Prolyl-L-alanine-nitrobenzyl ester. Upon removal of the carbobenzoxy group with hydrogen bromide in acetic acid an amorphous free base hexapeptide ester was obtained. This compound gave the correct C, H, N analysis and contained the six amino acids in the correct ratio. The octapeptide was obtained by condensing this hexapeptide with carbobenzoxy-B-benzyl-L-aspartyl-nitro, L-arginine using the mixed anhydride method of condensation. This amorphous product was proven to be homogenous by chromatography in two solvent systems and upon hydrolysis yielded the eight amino acids in correct ratio. The five protecting groups were removed from the octapeptide by hydrogenolysis over palladium black catalyst. Biological assay of the free peptide indicated that it possessed less than 0.1 per cent of both pressor and oxytocic activity of the phenylalanine8 angiotensin. This suggests that the phenyl group is a point of attachment between angiotensin and its biological receptor site.

• Toxicological Research
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• 제15권1호
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• pp.109-115
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• 1999

The antiosidant activity of carnosine and related compounds such as anserine, homo-carnosine, histidine, and $\beta$-alanine which are found in most mammalian tissues, was investigated using hypochlorite (HOCl)-induced oxidant systems. Carnosine and related compounds were protective against HOCl-induced ascorbic acid oxidation, as determined by UV absorbance at 265nm. L-histidine was the most effective among them. The inhibitory effect of these compounds was strongly associated with a decrease in HOCl. It was also found that carnosine and related compounds significantly protected against the HOCl-mediated erythrocyte damage, as determined by hemoglobin release and gemolysis (p<0.05). Carnosine and anserine also inhibited of $\alpha$-antiprotease($\alpha$-AP) by HOCl, thereby inactivating porcine elastase. The inhibitory effect of carnosine on inactivation of $\alpha$-AP by HOCl depended on the concentration of carnosine and on the time preincubated with HOCl. Homocarnosine, histidine, and $\beta$-alanine did not inhibit the reaction. These results indicate that carnosine and related compounds can neutralize or scavenge HOCl. Thus, these compounds may play an important role in protecting against HOCl-mediated damage of biomolecules in vivo.