• Journal of Microbiology and Biotechnology
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• v.1 no.1
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• pp.50-53
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• 1991

The reaction steps involved in the bioconversion of a chemically synthesized precursor, $D,L-2-amino-{\Delta}^2-thiazoline-4-carboxylic$ acid (D,L-ATC), to L-cysteine and the properties of the involved enzymes were investigated. It was found that the conversion consisted of two steps, i. e., D,L-ATC to S-carbamyl-L-cysteine (S-C-L-cysteine) and S-C-L-cysteine to L-cysteine, and the S-C-L-cysteine was an intermediate between them. While the enzymes involved in the reactions were induced by the addition of D,L-ATC as an inducer, S-C-L-cysteine induced only the enzyme involved in the latter step. The conversion of S-C-L-cysteine to L-cysteine could be also carried out in the presence of hydroxylamine and its rate was much faster than that by the corresponding enzyme. On the other hand, L-cysteine (or L-cystine) was decomposed to evolve $H_2S$ by the enzyme considered to be a kind of desulfhydrase. However, hydroxylamine was a perfect inhibitor for this enzyme.

• Microbiology and Biotechnology Letters
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• v.2 no.1
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• pp.45-50
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• 1974

1 With cysteinedesulfhydrase (E. C.4.4.1.1.) from Aerobactor aerogenes, an enzyme which catalyzes the stoichiometric conversion of L-cysteine to pyruvate, ammonia and sulfide, reversibility of the degradation of L-cysteine was investigated. It was found that the enzyme also catalized the reverse reaction of $\alpha$, $\beta$-elimination to synthesize L-cysteine derivatives from pyruvate, ammonia and sulfides when large amounts of substrates were added to the reaction mixtures. 2. The synthetic reaction by cysteinedesulfhydrase proceeded linearly with incubation time and enzyme concentrations. The optimal pH for the synthetic reaction was 10.0. 3. The results of the isolation and identification of the products showed that the L-cysteine derivatives synthesized by this enzymatic method were identical with S-methyl-L-cysteine and S-ethyl-L-cysteine respectively.

• Microbiology and Biotechnology Letters
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• v.18 no.1
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• pp.49-55
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• 1990

The bioconversion of D, L-20aminothiazoline-4-carboxylic acid (D, L-ATC) to L-cysteine was investigated. After the intracelluar enzyme of a Pseudomonas species was inducibly formed by addition of D, L-ATC in the middle of culture, the cells were isolated and treated with sonication to prepare the crude enzyme solution. The results indicated that the cysteine was produced only in the form of L-isomer from D,L-ATC and its production could be enhanced several tens times by addition of managanese ions which were required as a cofactor in this enzymatic reaction. Bedies, this reaction suffered from the feedback inhibition of L-cysteine. On the other hand, since L-cysteine-decomposing enzyme coexisted in the crude enzyme solution, most of the L-cyseine formed disappeared in the absence of its inhibitor. However, hydroxylamine was found to be a potent inhibitor which could successfully prevent the decomposition of L-cyseine.

• Bulletin of the Korean Chemical Society
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• v.2 no.4
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• pp.125-129
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• 1981

The addition reactions of cysteine without blocking amino and carboxyl groups to substituted and unsubstituted ${\beta}$-nitro-styrene derivatives were investigated. ${\beta}$-Nitrostyrene(1a), p-methyl-${\beta}$-nitrostyrene(1b), 3,4,5-trimethoxy-$[\beta}$ -nitrostyrene(1c), $[\varpi}$-3,4-methylenedioxy-${\beta}$ -nitrostyrene(1d), o-, m- and p-chloro-${\beta}$ -nitrostyrene (1e, 1f, 1g) and o-, m- and p-methoxy-${\beta}$-nitrostyrene (1h, 1i, 1j) easily undergo addition reactions with cysteine to form S-(2-nitro-1-phenylethyl)-L-cysteine(3a), S-[2-nitro-1-(p-methyl)phenyl-ethyl]-L-cysteine(3b), S-[2-nitro-1-(3',4',5'-trimethoxy) phenylethyl]-L-cysteine(3c), S-[2-nitro-1-($[\vatpi}$ -3',4'-methylenedioxy)phenylethyl]-L-cysteine(3d), S-[2-nitro-1-(o-chloro)phenylethyl]-L-cysteine(3e), S-[2-nitro-1-(m-chloro)-phenylethyl]-L-cysteine(3f), S-[2-nitro-1-(p-chloro)phenylethyl]-L-cysteine(3g), S-[2-nitro-1-(o-methoxy)phenylethyl]-L-cysteine(3h), S-[2-nitro-1-(m-methoxy)phenylethyl]-L-cysteine(3i) and S-[2-nitro-1-(p-methoxy)phenylethyl]-L-cysteine(3j), respectively. The structure of adducts were confirmed by means of UV-spectrum, IR-spectrum, molecular weight measurement and elemental analysis. The various factors effecting the yield of cysteine adducts to ${\beta}$-nitrostyrene derivatives were also studied.

• Food Science and Preservation
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• v.20 no.2
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• pp.173-181
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• 2013

This study investigated that anti-browning effects of Atractylodis Rhizoma Alba extract and L-cysteine combination. Mushrooms were dipped in solutions (0.1% Atractylodis Rhizoma Alba extract containing 0.05% L-cysteine) for 3 min. The dipped mushrooms were packaged in a polystyrene (PS) tray and wrapped with a polyvinyl chloride (PVC) film, and stored for 14 days at $10^{\circ}C$. The browning inhibition activity (Hunter L, a, b color scale and tyrosinase inhibition activity) and quality changes (weight loss rate, gas composition, firmness and sensory evaluation) were analyzed during storage period. After 14 days, the Hunter L and ${\Delta}E$ value of mushrooms treated in 0.1% Atractylodis Rhizoma Alba extract containing 0.05% L-cysteine were 87.24 and 5.56, respectively. The mushrooms treated with 0.1% Atractylodis Rhizoma Alba extract containing 0.05% L-cysteine also showed higher firmness (13.31 N) and smaller weight loss rate (2.87%) than the untreated mushroom (11.42 N, 3.04%) on storage day 14. During storage period, the sensory evaluation showed that overall acceptability of mushrooms treated with 0.1% Atractylodis Rhizoma Alba extract containing 0.05% L-cysteine were higher than those of the untreated mushrooms, except those that were stored for five days. Overall, the mushrooms treated with 0.1% Atractylodis Rhizoma Alba extract containing 0.05% L-cysteine had a higher tyrosinase inhibition activity than the untreated mushrooms during storage period. This study suggests that the browning of the mushrooms treated with 0.1% Atractylodis Rhizoma Alba extract containing 0.05% L-cysteine solution were inhibited, and the that their shelf life was extended.

• Food preservation and processing industry
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• v.7 no.1
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• pp.33-44
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• 2008

마늘의 저장 중 생리활성과 향미에 중요한 영향을 미치는 성분의 변화를 발표된 논문을 중심으로 정리하여 살펴보았다. 또한 마늘의 냄새를 최소화하고 생리활성을 극대화할 수 있는 기능성식품의 소재개발 타당성을 살펴보기 위하여 열처리(blanching)로 마늘 중의 효소를 모두 불활성화 시킨 후, 이에 마늘로부터 추출한 alliinase를 가하여 반응조건에 따른 alk(en)yl thiosulfinates 생성 및 이들의 분해산물인 휘발성 황함유화합물의 함량변화를 측정하였다. 수확한 마늘의 최종 저장물질로 알려진 -glutamyl-S-alk(en)yl-L-cysteines는 마늘중에 존재하는 -glutamyl-transpeptidase 및 oxidase의 작용에 의하여 감소한 반면 S-alk(en)yl cysteine sulfoxide는 감소한 만큼 증가하였으며, 이는 $-3^{\circ}C$ 및 실온($23^{\circ}C$)에서 보다도 냉장온도($4^{\circ}C$)에서 가장 많이 변화하는 것으로 나타났다. 이러한 감소 및 증가현상은 -glutamyl-S-(2-popenyl)-L-cysteine이 -glutamyl-S-(trans-1-propenyl)-L- cysteine이나 -glutamyl-S-methyl-L-cysteine보다 더 컸다. -glutamyl-S-(2-propen yl)-L-cysteine은 $4^{\circ}C$에서 저장 60일 만에 66%가 감소한 반면 이로부터 생성된 S-(2- popenyl)-L-cysteine sulfoxide는 그 만큼 증가하였다. -glutamyl-S-(trans-1-propenyl)-L-cysteine 및 -glutamyl-S-methyl-L-cysteine도 $4^{\circ}C$에서 150일간 저장한 경우 각각 81% 및 39%가 감소하고, 이들로부터 각각 생성된 S-(trans-1- propenyl)-L-cysteine sulfoxides 및 S-methyl-L-cysteine sulfoxide는 증가하였다. 한편 열처리 마늘에 alliinase를 가하여 함황화합물을 재생성 시킨 결과 8종의 S-alk(en)yl cysteine sulfoxides를 확인할 수 있었다. S-(2-propenyl)-L-cysteine sulfoxide은 전체 thiosulfinates함량의 약 60%를 차지하는 것으로 나타났다. 100, 200, 300 및 400 unit의 alliinase를 첨가하여 15분간 반응시킨 결과 총 thiosulfinates는 생마늘(대조구)에 비하여 각각 37, 68, 77 및 80%가 생성되는 것으로 나타났다. GC/MSD를 이용하여 대조구 및 효소를 첨가하여 반응시킨 시료의 휘발성 향기성분을 분석한 결과 alliinase를 100, 200, 300 및 400 unit 첨가하여 15분간 반응시키면 각각 마늘의 휘발성 향기성분이 25, 36, 66및 76% 씩 재 생성되는 것으로 나타났다. 이상의 결과를 종합해 볼 때 마늘을 이용한 제품개발이나 연구를 할 경우 마늘의 저장조건에 따른 생리활성물질의 분석결과를 근거로 하여 이루어져야 하며, 또한 효소를 이용하여 적절히 반응시키면 마늘 냄새를 $30{\sim}80%$ 범위 내에서 조절이 가능한 것으로 나타났다.

• Bulletin of the Korean Chemical Society
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• v.9 no.3
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• pp.115-117
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• 1988

The addition of L-cysteine without blocking amino and carboxyl groups to${\beta},{\beta}$-dinitrostyrene derivatives(11a-e) were investigated. ${\beta},{\beta}$ -Dinitrostyrene derivatives(11a-e) easily undergo addition reactions with L-cysteine to from s-(2,2-dinitro-1-phenylethyl)-L-cysteine(12a), s-[2,2-dinitro-1-(p-methyl)phenylethyl]-L-cysteine (12b), s-[2,2-dinitro-1-(p-methoxy)phenylethyl]-L-cystein e(12c), s-[2,2-dinitro-1-(p-chloro)phenylethyl]-L-cysteine (12d) and s-[2,2-dinitro-1-(p-nitro)phenylethyl]-L-cysteine( 12a), respectively. The structure of adducts were confirmed by means of spectral data, molecular weight measurement and elemental analysis.

• Journal of Embryo Transfer
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• v.29 no.2
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• pp.163-169
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• 2014

The objective of this study was to evaluate the characteristics of Korean Native Cattle sperm frozen-thawed with L-cysteine and/or catalase. The semen from bulls was collected by the artificial vagina method, and Triladyl containing 20% egg-yolk and/or L-cysteine (L), catalase (C) and L-cysteine + catalase was added to the diluted semen for cryopreservation. The results showed that sperm viability was significantly higher in the L-cysteine + catalase ($69.49{\pm}3.16%$) group than in the control ($60.5{\pm}3.94%$) group (p<0.05). Acrosome damage was significantly lower in the L-cysteine ($17.12{\pm}1.08%$) group than in the control ($21.46{\pm}1.14%$), catalase ($20.54{\pm}0.76%$), and L-cysteine + catalase ($19.29{\pm}0.65%$) groups (p<0.05). In addition, the level of intact mitochondria in the spermatozoa was significantly higher in the L-cysteine ($58.65{\pm}1.39%$) group than in the control ($50.63{\pm}2.37%$) group (p<0.05). The hydrogen peroxide level in the frozen-thawed sperm was significantly lower in the L-cysteine ($3.74{\pm}1.66%$), catalase ($4.65{\pm}1.87%$), and L-cysteine + catalase ($8.11{\pm}2.15%$) groups than in the control ($13.22{\pm}1.6%$) group (p<0.05). The glutathione level was significantly higher in the L-cysteine ($1.33{\pm}0.03%$) group than in the control ($1.08{\pm}0.06%$), catalase ($1.05{\pm}0.02%$) and L-cysteine + catalase ($1.11{\pm}0.03%$) groups (p<0.05). In conclusion, L-cysteine and catalase could protect the membrane of Korean Native Cattle sperm from damage during sperm cryopreservation. Especially, L-cysteine was more effective for keeping acrosomes and mitochondria intactness during sperm cryopreservation.

• Textile Coloration and Finishing
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• v.20 no.2
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• pp.9-18
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• 2008

Wool has excellent properties, such as heat retention, absorbency, and elasticity, but it has a disadvantage in washability because the fabric will felt and shrink greatly. Felting causes the interlocking of the fiber surface scales with one another. Therefore, the studies on wool finishing have been focused on shrink proofing. Precedent researches on wool shrink proofing are mostly on eco-friendly method. using enzyme. The purpose of this study is to examine the effect of L-cysteine, EDTA in papain treatment of wool fabrics. The specific contents of study are as follows. Depending on pH, temperature, treatment time, enzyme concentration and L-cysteine, EDTA concentration, weight loss, tensile strength, whiteness, SEM were examined. Each papain treatment conditions depending on L-cysteine, EDTA were optimized from these properties. Papain had very low activation without activators. The optimum conditions of papain treatment were pH 7.5, temperature $75^{\circ}C$, time 30minutes(L-cysteine), 180minutes(EDTA) and papain concentration 5%(o.w.f.). In the use of papain 5%(o.w.f.), the activators optimum concentration was L-cysteine 2%(o.w.f.), EDTA 7%(o.w.f.)

• Bulletin of the Korean Chemical Society
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• v.5 no.6
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• pp.215-218
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• 1984

A series of S-(2,2-diethoxycarbonyl-1-phenylethyl)-L-cysteine derivatives (10a-e) were synthesized from the reaction of $\beta$$\beta$-diethoxycarbonylstyrene with L-cysteine in 1:1 aqueous methanol. Thus, S-(2,2-diethoxycarbonyl-1-phenylethyl)-L-cysteine( 10a), S-[2,2-diethoxycarbonyl-1-(3',4'-methylendioxy)ph enylethyl]-L-cysteine (10b), S-[2,2-diethoxycarbonyl-1-(3',4',5'-trimethoxy)phe nylethyl]-L-cyseine (10c), S-[2,2-diethoxycarbonyl-1-(p-hydroxy)phenylethyl] -L-cysteine (10d), S-[2,2-diethoxycarbonyl-1-(p-methoxy)phenylethyl] -L-cysteine (10e) were obtained in moderate to excellent yields. The structure of the adducts was characterized by analytical and spectral data. The effects of pH upon the product yields were also briefly examined.