• Biotechnology and Bioprocess Engineering:BBE
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• 제8권3호
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• pp.167-172
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• 2003

Foam fractionation can be used to enrich a hydrophobic protein such as bromelain from an aerated dilute protein solution because the protein foams. On the other hand, a protein such as invertase, which is hydrophilic, is not likely to foam under similar aerated conditions. While a foam fractionation process may not be appropriate for recovering a hydrophilic protein alone, it is of interest to see how that non-foaming protein affects the foaming protein when the two are together in a mixture. The bromelain enrichment, activity and mass recovery were observed as a function of the solution pH in order to explore how invertase can affect the recovery of bromelain in a foam fractionation process.

• 한국환경농학회지
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• 제41권3호
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• pp.206-216
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• 2022

BACKGROUND: Dithiocarbamate fungicide propineb can be analyzed quantitatively by derivatization reaction followed by HPLC/UVD, which has high reproducibility and stability. However, the presence of high protein in soybeans and peas affects the derivatization process resulting in extremely low recoveries. Therefore, this study was conducted to improve the analytical method for analysis of propineb in soybeans and peas by applying a deproteinization process using chloroform-gel method. METHODS AND RESULTS: The deproteinization process was carried out up to 6 times for soybeans and 5 times for peas using 50 mL chloroform. After 4 times of deproteinization process followed by a derivatization reaction with methyl iodide, the recovery yields of propineb in both pulses were >90%. However, the recovery yield tended to decrease when the deproteinization process was performed more than 5 times. The method limit of quantification (LOQ) was 0.04 mg/L. The recovery conducted in triplicate at 10 times and 50 times of the LOQ ranged from 87.2 to 95.0 % with a coefficient of variation <10%. CONCLUSION(S): This study confirmed that 4 times of deproteinization process using the chloroform-gel method was effective when derivatizing and analyzing dithiocarbamate fungicides in pulses with high protein content. However, depending on the initial protein content present in the pulses, there was a difference in the recovery: the lower the protein content, the higher the recovery rate of propineb. It is expected that the method proposed in this study could be applied to remove high content of protein as analytical interference substance from agricultural samples.

• BMB Reports
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• 제29권5호
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• pp.398-404
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• 1996

Light-chilling effects were investigated in chilling-sensitive cucumber (Cucumis sativus L. cv. Ilmichungjang) and chilling-resistant pea (Pisum sativum L. cv. Giant) leaf discs in relation to possible damage in D1 protein. In both plants, dark-chilling did not cause any noticeable changes in (Fv)m/Fm and lincomycin did not affect the decrease in (Fv)m/Fm caused by light-chilling. This result suggests that the de novo synthesis of D1 protein did not occur actively during light-chilling. In pea light-chilled for 6 h. the decreased (Fv)m/Fm was partly recovered in the dark, and almost complete recovery was observed in the light. In cucumber light-chilled for 3 h. the reduced (Fv)m/Fm decreased further for the initial 2 h recovery process in the light regardless of the treatment of lincomycin and recovered very slowly. In both plant species, the treatment of lincomycin inhibited the recovery process in the light, but did not significantly inhibit the process in the dark. In cucumber leaves pulse-labeled with $[^{35}S]Met$, the labeled band intensities of isolated pigment-protein complexes were almost the same during the 6 h light-chilling, but significant decreases in band intensities were observed during the 3 h recovery period. This result suggests that the irreversibly damaged D1 protein was degraded during the recovery period. However, no noticeable changes were observed in the pea leaves during the 12 h chilling and 3 h recovery period. The polyacrylamide gel electrophoresis of the pigment-protein complexes showed that the principal lesion sites of light-chilling were different from those of room temperature photoinhibition.

• Journal of Microbiology and Biotechnology
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• 제6권4호
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• pp.225-231
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• 1996

The production of recombinant proteins in Escherichia coli often leads to the formation of an intracellular inclusion body. Key process steps that can determine the economics of large-scale protein production from inclusion bodies are fermentation, inclusion body recovery, and protein refolding. Compared with protein refolding and fermentation, inclusion body recovery has received scant research attention. Nevertheless, it can control the final product yield and hence process cost for some products. Optimal separation of inclusion bodies and cell debris can also aid subsequent operations by removing contaminant particulates that foul chromatographic resins and contain antigenic pyrogens. In this review, the properties of inclusion bodies and cellular debris are therefore examined. Attempts to optimise the centrifugal separation of inclusion bodies and debris are also discussed.

• Journal of Plant Biology
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• 제38권1호
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• pp.1-10
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• 1995

Photoinhibition and its recovery of spectrally adapted Anacystis nidulans were studied. Phycocyanin and Chl content and phycocyanin/Chl ratio were increased in cells grown under blue-green light compared with those grown in white light. Photosynthetic activities of white light and blue-green light grown cells were reduced by 50% after 15 min and 10 min of photoinhibitory light treatment (1.2 mmol·m-2s-1), respectively, largely due to the decline of PSII activities. However, their activities were recovered fully after 30 min incubation under weak light. Treatment of rifampicin and chloramphenicol magnified the photoinhibitory effects and suppressed the recovery with disappearance of susceptibility to photoinhibition and delayed the recovery process, indicating no significant differences in phosphorylation, dephosphorylation and protease activity between two cells. Therefore, it is suggested that the increased sensitivity of blue-green adapted cells might be attributed to the decline of protein synthesis, and phosphorylation-dephosphorylation of protein and protease activity might be involved in the recovery process.

• Journal of Photoscience
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• 제9권2호
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• pp.130-133
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• 2002

The last step in the photocycle of photoactive yellow protein (PYP) is a spontaneous recovery of the dark state from the active state in which the p-coumaric acid chromophore is thermally isomerized, concomitantly with the deprotona- tion of the chtomophore and the refolding of the protein moicty. For the purpose of understanding the mechanism of the thermal back-isomerization, we have investigated the rate-determining step by analyzing mutant PYPs of Met100, which was previously shown to play a major role in facilitating the reaction (1). The mutation to Lys, Leu, Ala, or Glu decelerated the dark state recovery by 1 to 3 three orders of magnitude. By evaluating temperature-dependence and pH-dependence of the kinetics of the dark state recovery, it was found that the retardation by mutations resulted from elevation of the activation enthalpy ( H$\^$┿/) and that the pKa of the chromophore, which was affected by the mutation, is in a linier correlation with the amplitude of the rate constants. It was, therefore, deduced from the correlation that the free energy for crossing the activated state in the dark recovery process is proportional to the free energy for the deprotonation of the chromophore, identifying the rate-determining step as the deprotonation of the chromophore. (1) Devanathan, S. Genick, U. K. Canestrelli, I. L. Meyer, T. E. Cusanovich, M. A. Getzoff, E. D. Tollin, G., Biochemistry 1998, 37, 11563 - 11568

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2002년도 생물공학의 동향 (X)
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• pp.515-518
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• 2002

The method of foam fractionation can be applied to enrich proteins from a dilute protein solution if the proteins are hydrophobic and foam. If a protein, such as invertase, is hydrophilic, a dilute solution containing this protein may not foam. In that case, a batch foam fractionation process may not be appropriate for recovering a concentrated solution of that protein. In this paper, various concentrations of invertase were added to a dilute solution containing bromelain (a hydrophobic protein), in order to determine how the presence of a hydrophilic protein can affect the recovery of the desired hydrophobic protein. The effect of invertase on bromelain recovery was studied here at an initial bulk solution pH of 5 and an air superficial velocity of 4.6 cm/s.

• 멤브레인
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• 제12권3호
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• pp.165-170
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• 2002

씻어나온 쌀(무세미) 생산공정 중 발생하는 쌀뜨물 중 함유된 유효성분, 특히 단백질 회수를 위한 분리막 공정에 관하여 검토하였다. 먼저 dead-end형 Amicon 여과셀을 이용하여 단백질 농축에 적절한 분리막을 선정하였으며 이를 토대로 중공사형 한외여과 모듈 또는 가정용 정수기에 사용되는 나권형 나노여과 및 역삼투 모듈을 이용한 투과실험을 행하였다. 그 결과, 분획분자량이 10,000 dalton인 한외여과막은 쌀뜨물내 유효성분 내지는 단백q질을 농축하기에 적절하지 않았다. 그러나 역삼투 또는 나노여과 모듈에 9% 가량의 단백질이 함유된 원료용액을 250%까지 농축할 경우, 역삼투 모듈 농축액중에 단백질의 농도는 22%로서 약 2.4배가 농축되었으며 나노여과 모듈의 경우는 약 2배까지 단백질을 농축할 수 있었다.

• 한국염색가공학회지
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• 제14권4호
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• pp.249-258
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• 2002

Natural silk is formed by two proteins : the crystalline fibroin (inside the silk thread) and amorphous sericin (as a tube outside the thread). The degumming process is used to eliminate the external sericin prior to dyeing ; generally it makes use of soaps at about pH 10. Sericin is the protein constituent that "gums"together the fibroin filaments of cocoon silk. It constitutes about 25% of the weight of the cocoon, is soluble in hot water and "gels" on cooling. The removal of sericin from raw silk, known as degumming, is a simple but important process usually employing hot dilute soap or alkaline solution and occasionally dilute acids or enzymic methods. During degumming, alkali is taken up by the sericin and the free acid from the soap is formed ; this may be deposited on the fiber, reducing the rate of degumming and protecting it from hydrolysis. Alkali is often added to maintain or restore the pH of the baths, but it is rarely used alone, since it leaves the silk rather harsh in handle. If complete sericin removal is required as for printing, sodium carbonate may be added. If the pH of the bath exceeds 11, the fibroin is attacked. Recently, According to the development of electrolysis, we can be obtained the electrolytic reduction water(above pH 11.5) and electrolytic oxidation water (below pH 3). The aim of this work was to study a degumming process using electrolytic water and a possibility of sericin recovery. The new degumming process used electrolytic water operates at $95^\circ{C}$ for 2hr. without any reagents. The wastewater of this process are formed by a solution of sericin in water. This conditions suggest the study of a possible recovery of this protein (sericin) which has an amino acid composition suitable for many used in cosmetics, textile finishing agents, animal feeding, etc. The degumming process using electrolytic water is available to reduce treatment costs and pollute and at the same time to recover sericin.

• 한국응용과학기술학회지
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• 제24권4호
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• pp.347-353
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• 2007

Fleshing scrap is a kind of wastes produced during leather making process and used in the test of manufacturing biodiesel. The early step of manufacturing biodiesel is fat recovery from fleshing scrap. Hence, we investigated the influence of the way of fat recovery on the fatty acid composition. We used three different recovery ways, that is chemical method by protein decomposition with acid/fat recovering, physical method by protein denaturalization with heat and vacuum/fat pressing, and biodiesel method by protein decomposition/fat recovering. The biological method yielded the best results in terms of appearance transparency. It was most effective to lower acid value. Also the recovered fat by biological method would be favorable methyl-ester reaction raw material for biodiesel because it contains more than 5% of oleic acid among unsaturated fatty acid.