• Title/Summary/Keyword: soluble stability

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Stabilization of Wheat $\beta$-Amylase by Modification with $IO_4$-Oxidized Starch ($IO_4$-산화전분 변형에 의한 밀 $\beta$-Amylase의 안정성 증가)

  • 안용근
    • The Korean Journal of Food And Nutrition
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    • v.13 no.4
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    • pp.348-352
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    • 2000
  • The stabilization of wheat $\beta$-amylase( Himaltosin GL, Hankyu-Bio) was attained by modification wish periodate-oxidized soluble starch. The specific activities of modified enzyme at pH 9.7 and pH 8.0 were 17% and 96%, respectively, compared with that of native enzyme. The pH stability of modified enzyme was increased at pH 2~5 and 6~12 in the presence of $\alpha$-cyclodextrin( $\alpha$-CD) compared with that of native enzyme, and optimum pH of the enzyme was changed from pH 5.0 to pH 7.0 by the modification. Thermal stability of the modified enzyme was increased. After treatment at 6$0^{\circ}C$ for 10min, the activity remained 8% for the enzyme modified at pH 8.0 in the presence of $\alpha$-CD and tested in the presence of $\alpha$-CD, 5% for the native enzyme. The native enzyme and modified enzyme showed one peak in HPLC. The molecular weight of the modified enzyme was slightly increased in HPLC analysis.

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Chemical Stability and Whitening Activity of Mixture of Functional Ingredients (미백 기능성 성분의 혼합물에 대한 미백 활성 및 안정성에 관한 연구)

  • Lee, Youn-Hee;Lim, Nam-Hoon;Joung, Min-Seok;Kim, Joong-Hoi;Sim, Sang-Soo
    • Journal of the Society of Cosmetic Scientists of Korea
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    • v.31 no.4 s.54
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    • pp.295-304
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    • 2005
  • Recently, arbutin, oil soluble licorice extact (GLY), ascorbyl glucoside (AA2G), and ethyl ascorbyl ether (EAE) have been widely used as functional whitening ingredients. To Investigate which combination between the above agents could be more effective for whitening effect, tyrosinase activity and MSH-induced melanin production in B-16 melanoma cells were investigated. Both GLY and arbutin dose-dependently inhibited purified tyrosinase activity. The inhibitory effects of GLY with AA2A or EAE on Drosinase activity were more potent than those of GLY alone, whereas that of arbutin with other ingreadients did not show those effects. In MSH-induced melanin production in B-16 melanoma cells, the mixture of Gly and EAE more significantly reduced melanin formation than Gly alone. Stability of mixture of GLY, arbutin, AA2A and EAE exposed at the temperature of $25^{\circ}C\;or\;45^{\circ}C$ for 30 days were also investigated. All of the combinations of whitening agents did not show any critical changes in their composition stability. These data suggest that the combination of GLY and vitamin C derivatives such as AA2G and EAE may be useful for the promotion of whitening effect.

Biotransformation of Amides to Acids Using a Co-Cross-Linked Enzyme Aggregate of Rhodococcus erythropolis Amidase

  • Park, Hyun-Joo;Uhm, Ki-Nam;Kim, Hyung-Kwoun
    • Journal of Microbiology and Biotechnology
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    • v.20 no.2
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    • pp.325-331
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    • 2010
  • Rhodococcus erythropolis amidase was expressed in Escherichia coli cells. The crude amidase in the cell-free extract was immobilized using the cross-linked enzyme aggregate (CLEA) method. The crude amidase was mixed with bovine serum albumin and then precipitated with ammonium sulfate. The resultant precipitant was subsequently cross-linked with glutaraldehyde. Scanning electron microscopy revealed that this co-CLEA had a ball-like shape with a diameter of approximately $1\;{\mu}m$. This co-CLEA evidenced hydrolytic activity toward a variety of amide substrates. The amidase co-CLEA evidenced an optimum temperature of $60^{\circ}C$ and an optimum pH of 8.0, results that were similar to those of the soluble amidase. The reaction stability of the co-CLEA was increased. That is, it was stable up to $50^{\circ}C$ and in a pH range of 5.0-12.0. Additionally, the co-CLEA could be recovered by centrifugation, and retained 96% activity after 3 repeated cycles. This amidase co-CLEA may prove useful as a substitute for soluble amidase as a biocatalyst in the pharmaceutical and chemical industries.

Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-Human Immunodeficiency Virus Type lantibodies directed to conformation-dependent epitopes of gp120 (수용성 CD-gp120 결합체의 면역화로 유도된 항 gp120 항체의 특성에 관한 연구)

  • Kang, Chang-Yuil
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.11a
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    • pp.61-67
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    • 1994
  • One fundamental problem in developing an AIDS vaccine is antigenic variation of HIV. Despite a substantial induced immune response in gp120-immunized monkeys and humans, high titers of V3-directed type specific neutralizing antibodies may not be sufficient to neutralize continuously emerging new isolates. Several studies analyzing anti-gp120 antibodies in HIV-infected individuals have clearly indicated that most broadly neutralizing antibodies are directed to conformation-dependent epitopes. Therefore, it seems important to evaluate the potential efficacy of candidate gp120 vaccines at inducing such antibodies, that might be potentially protective against multiple HIV strains. One concern in the development of any recombinant protein as a vaccine is its stability when mixed with an adjuvant. This could be a particularly important factor for recombinant gp120, given the conformational nature of its major, broadly neutralizing, epitopes. We hypothesized that gp120 complexed with recombinant CD4 could stabilize the conformation-dependent epitopes and effectively deliver these epitopes to the immune system. In this study, a soluble gp120-CD4 complex in Syntex Adjuvant Formulation was tested in mice to analyze the anti-gp120 antibody response. With the aim of defining the fine specificity and neutalizing activities of the immune response, 17Mabs were generated and characterized. The studies indicate that the gp120-CD4 complex elicits neutralizing anti-gp120 antibodies, most of which are directed to the conformation dependent epitopes.

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Purification and Characteristics of Amylase from Haloarcular sp. EH-1 (Haloarcular sp. EH-1이 생산하는 Amylase의 정제 및 특성)

  • 정명주;박형숙
    • Microbiology and Biotechnology Letters
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    • v.27 no.2
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    • pp.129-135
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    • 1999
  • EH-1 was highest at 9 days of incubation. This regrowth and enzymatic activity of Haloarcular sp. EH-1 was highest at 9 days of incubation. This amylase was purified by acetone fractionation, DEAG-Cellulose column chromatography, 1st Sephadex G-75 gel filtration, CM-Cellulose column chromatography and 2nd Sephadex G-75 gel filtration. The amylase was purified about 98.64 fold with a yield of 11.75%. The molecular weight of amylase was estimated to be about 43,000and 40,000 by gel filtration and SDS-polyacrylamide gel electrophoresis, respectively, suggesting that the enzyme was a monomer. Amylase had an optimal temperature of 4$0^{\circ}C$, and an optimum pH of 7.0, and the thermal stability was observed the above 50% at 10$0^{\circ}C$ after 1 hour, and the stable range of pH was 6.0 to 8.0. The enzymatic activity was increased in the presence of 10 mM 2-mercaptoethanol, slightly by 10 mM SnCl2.2H2O.FeCl2.4H2O.CuCl2.2H2O.HgCl2.6H2O and SDS. End products from soluble starch were glucose, maltose and maltotriose, and Km value for soluble starch was 2.5mg/ml.

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Production of Fructo-oligosaccharides by the Fructosyltransferase Immobilized onto an lon-exchange Resin (이온교환수지에 고정화된 Fructosyltransferase를 이용한 Fructo-oligosaccharides의 생산)

  • 윤종원;이민규송승구
    • KSBB Journal
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    • v.8 no.4
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    • pp.307-312
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    • 1993
  • A fructosyltransferase from Aureobasidium pullulans was immobilized onto a polystyrene-type anionic ion-exchange resin and the production of fructo-oligosaccharides was Investigated by the immobilized enzyme. The optimum pH and the temperature of immobilized enzyme were found to be pH 5.0, $55^{\circ}C$ respectively. The thermal stability of the enzyme was greatly enhanced after immobilization. The reaction profiles of the immobilized enzyme was almost identical to those of the free cells and the soluble enzyme. The immobilized enzymes were stable up to 20 cycles without loss of initial activity in a repeated-batch operation $50^{\circ}C$.

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Factors Affecting on Protein Stability of Mixed Cow and Soy Milk (콩우유와 우유 혼합유의 단백질 안정성에 미치는 영향인자)

  • 정남용;김우정
    • The Korean Journal of Food And Nutrition
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    • v.7 no.4
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    • pp.345-352
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    • 1994
  • High protein beverage of cow-soy milk was prepared by mixing the soymilk and commercial homogenized cow milk in the various ratios. Effect of heat treatment, pH and addition of calcium and sucrose was studied on the water-soluble nitrogen of cow-soy milk The heat-treated soymilk at 10$0^{\circ}C$ were centrifuged at the range of 830~29,900xg for 30 min and 11,200xg was found to be proper for determination of the degree of protein denaturation by centrifugal method. When soymilk was heated at 70~10$0^{\circ}C$ for 30~240 min, soluble nitrogen (QA SN) in supernatant of protein was decreased to 78.0~56.8% due to protein denaturation. Most of heat denaturation of protein was found to be occurred during Initial heating 10$0^{\circ}C$ for all mixed cow-soy milk. The sedimentation of SN was maximum at pH 4.0 In the range of pH 3~8. Addition of sucrose affected little on oASN while calcium addition reduced %SN significantly to approx. 55% for soymilk(100%). The effect of Ca was less as the ratio of cow milk increased.

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Application of Laser Induced Photoacoustic Spectroscopy in the Investigation of Interaction of Neodymium(III) with Water Soluble Synthetic Polymer

  • Tae Hyung Yoon;Hichung Moon;Seung Min Park;Joong Gill Choi;Paul Joe Chong
    • Bulletin of the Korean Chemical Society
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    • v.14 no.5
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    • pp.574-578
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    • 1993
  • Laser-induced photoacoustic spectroscopy (LIPAS), which utilizes the photothermal effect that results from nonradiative relaxation of excited state molecules, was used in the speciation analysis of the complexes of neodymium(III) and water soluble synthetic polyelectrolyte, poly methacrylic acid (PMAA), in 0.1 M $NaClO_4$ at pH of 6.0. The minimum detection limit of Nd(III) by LIPAS was $5.O{\times}10^{-6}$ M. Experiment was carried out at low concentration ratio of Nd(III) to PMAA to assure that 1 : 1 complexes predominate. The bound and free Nd(III) species were characterized by measuring nonradiative relaxation energy of the excited states $(^2GM{7/2}\;and\;^4G_{5/2})$ to the metastable state $(^4G_{3/2})$. Two species were quantified by deconvolution of the mixed spectrum using their respective reference spectra. The conditional stability constant measured by LIPAS was 5.52 L$mol^{-1}$.

A Novel Synthetic Route to Highly Cross-Linked Poly(alkylvinylether)s. Synthesis and Free Radical Polymerization of a Vinyl Ether Monomer Containing Electron Acceptors in Side Chain

  • 이주연;이현주;김무용
    • Bulletin of the Korean Chemical Society
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    • v.17 no.3
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    • pp.257-262
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    • 1996
  • p-(2-Vinyloxyethoxy)benzylidenemalononitrile 2 and methyl p-(2-vinyloxyethoxy)benzylidenecyanoacetate 3 was prepared by the condensation of p-(2-vinyloxyethoxy)benzaldehyde 1 with malononitrile or methyl cyanoacetate, respectively. Vinyl ether monomers 2 and 3 polymerized quantitatively with radical initiators in γ-butyrolactone solution at 65 ℃. The trisubstituted terminal double bond participated in the vinyl polymerization and radical polymerization of 2 and 3 led to swelling polymers 4 and 5 that were not soluble in common solvents due to cross-linking. Under the same polymerization conditions ethylvinyl ether polymerized well with model compounds of p-methoxybenzylidenemalononitrile 6 and methyl p-methoxybenzylidenecyanoacetate 7, respectively, to give 1:1 alternating copolymers 8 and 9 in high yields. Polymers 4 and 5 showed a thermal stability up to 300 ℃ without any characteristic Tg peaks in DSC thermograms. Alternating copolymers 8 and 9 were soluble in common solvents such as acetone and DMSO, and the inherent viscosities of the polymers were in the range of 0.36-0.74 dL/g. Films cast from acetone solution were cloudy and tough and Tg values obtained from DSC thermograms were in the range of 59-60 ℃.

Techno-functional and rheological properties of Tenebrio molitor larvae protein by different extraction methods

  • Yeeun Kan;Insang Cho;Eunyoung Oh;Ra-Yeong Choi;Jeewon Koh;Yookyung Kim
    • International Journal of Industrial Entomology and Biomaterials
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    • v.48 no.2
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    • pp.86-97
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    • 2024
  • Alkaline- or salt-assisted extractions have been widely used to extract edible insect proteins, however, there is a need for extraction techniques that balance cost-efficient production as well as preserving the protein properties. Mealworm proteins (Tenebrio molitor larvae) were extracted using three different extraction methods-alkali (AMP), salt (SMP), and water (WMP)-and then physicochemical and techno-functional properties were examined. AMP had high yield, protein, and amino acid contents, whereas WMP had high moisture, ash, and fat contents. SDS-PAGE showed a wide range of molecular weights in WMP whereas mostly low molecular weights were observed in AMP and SMP. AMP had poor protein solubilities compared to SMP and WMP across all pHs. AMP had enhanced water-holding capacity and emulsion stability, whereas WMP had improved oil-holding capacity and foaming properties. WMP formed a gel with and without the transglutaminase. The physicochemical and techno-functional properties demonstrated that water-soluble mealworm protein was superior to alkali-and salt-soluble mealworm proteins. Considering the cost efficiency and minimal impact on the environment as well, a cold press juicer could be utilized for mass production of mealworm protein compared to the conventional methods of protein extraction using alkali and salt.