• 한국식품조리과학회지
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• 제16권2호
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• pp.151-159
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• 2000

The effects of bromelain and $\alpha$-chymotrypsin treatments on the functional properties(foaming capacity, foaming stability, emulsifying capacity, and emulsifying stability) of soy protein isolate(SPI) and the addition of various sweeteners(sucrose, sorbitol, xylitol) on the quality attributes(viscosity, overrun ratio, melt-down property, and sensory characteristic) of soy ice cream were studied. SPI was more effectively hydrolyzed with $\alpha$-chymotrypsin than bromelain, resulting in a better foaming and emulsifying capacity. Adding xylitol could significantly improve the viscosity, overrun and melt-down property of soy ice creams while the effect was the lowest in the sucrose addition. Bromelain treatment caused a lower apparent viscosity of SPI suspension compared with $\alpha$-chymotrypsin treatment and untreated. The overrun ratios of the soy ice cream prepared with bromelain and $\alpha$-chymotrypsin treated SPI were 18.9∼25.9% and 24.9∼40.3%, respectively as a result of freezing with agitation for 20 min in an ice cream maker. Comparatively, untreated SPI could bring only 15.8∼21.4% overrun ratios after operating for 15 min. The bromelain treatment caused high melt-down tendency of the product while soy ice cream with untreated SPI showed an opposite trend. In sensory characteristics, no significant differences in the strength of beany flavor were noted among the samples. Sweetness, bitter taste, icy feel, and mouthfeel of the product were greatly affected by the enzyme-treatment of SPI. Soy ice cream added with xylitol after $\alpha$-chymotrypsin treatment was the most acceptable among all samples.

• 한국의류학회지
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• 제33권7호
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• pp.1121-1127
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• 2009

This study presents an eco-friendly and one-step finishing method for modifying fiber property that reduces fiber damage in wool/polyester blend fabrics. Lipase from aspergillus oryzae is used in this experiment. The enzymatic treatment condition is optimized by measuring the relative activity of lipase depending on pH level, temperature, concentration of lipase, and treatment time. The concentration of $CaCl_2$as an activator is determined by the characteristics including whiteness, water contact angle (WCA), and dyeing property. The modified properties of lipase treated fabrics are tested for pill resistance and surface morphology. The results are described as follows: the optimum condions for lipase treatment constitute a pH level of 8.0, treatment temperature of 40$^{\circ}$$_C$, concentration of lipase at 100% (o.w.f), and a treatment time of 90 minutes. $CaCl_2$helps in raising lipase activation, and the optimum concentration is 50mM. The whiteness, wet ability, and pill resistance of lipase treated fabrics improves as compared to the control. The dyeing property of lipase treated fabrics improved by 53.5% after using the one-bath dyeing method. This means that lipase treatment can save time and cost during the dyeing process since lipase treatment modifies wool and polyester fibers. The surface of lipase treated wool fibers do not exhibit any change, however voids and cracks manifest on the surface of lipase treated polyester fibers.

• 한국의류학회지
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• 제33권2호
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• pp.213-221
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• 2009

This study provides the optimum papain treatment method and its effect on wool/polyester blend fabrics. The enzymatic treatment condition is optimized depending on its pH level, temperature, concentration of enzyme, treatment time and concentration of activators. The characteristics of samples treated with the papain are measured using weight loss, tensile strength, whiteness, WCA, dyeing property and surface micrographs. The results are described as follows: According to measuring weight loss, tensile strength and whiteness, a pH level of 7.5, $70^{\circ}C$, 10% papain(o.w.f.) and 60minutes of treatment time are optimized for papain treatment. L-cysteine and sodium sulfite are able to activate the papain. The optimum concentrations of them are 10mM and 50mM respectively. The WCA of fabrics is decreased since papain treatment makes wool/polyester blend fabrics more hydrophilic. Scouring with papain treatment improves whiteness and dyeing property of fabrics. The dyeing property of papain-treated fabrics is enhanced simply by a single step dyeing process using a basic dye. The surface of wool treated with papain in the presence of L-cysteine shows to be descaled. The surface of wool fibers in the presence of sodium sulfite, however, shows it is hydrolyzed evenly instead of being descaled. The surface of papain treated polyester fibers shows cracks and voids.

• 폴리머
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• 제33권2호
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• pp.111-117
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• 2009

본 연구를 통해 역이온 영동(reverse iontophoresis)을 이용한 무채혈 혈당 측정시스템의 patch sensor에 사용되는 효소 고정형 수화젤의 생체적합성 여부를 확인하고자 하였다. 아크릴레이트 계열의 단량체를 사용하여 일정한 unit의 효소가 고정된 수화젤을 합성하였다. 합성된 수화젤의 물성분석을 위해 FT-IR spectrometer를 이용하여 구조분석을 하고 DSC를 이용하여 열적 안정성을 확인하였다. 또한, UV-Vis spoctrophotometer를 이용하여 표준품 대비 50% 이상의 효소 활성도를 확인하였다. 표면의 효소 고정화 확인을 위해 SEM을 이용하여 확인한 결과 효소가 고정화되어 있음을 확인하였다. 수화젤은 환자의 피부에 직접적으로 접촉됨으로써 접촉 시 무해성을 평가하기 위하여, ISO-10993에 의하여 세포독성(cytotoxicity), 피내반응(intracutaneous reactivity), 피부자극(skin irritation) 및 감작성(maximization sensitization) 시험을 실시하였고 이를 통해 생체적합성이 우수하다는 것을 확인하였다.

• 미생물학회지
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• 제20권4호
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• pp.189-194
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• 1982

Acid protease produced from Aspergillus tubingensis was pruified by ethanol fractionation, dialysis, and DEAE cellulose column chromatography. As a result of purification its specific activity increased to 5.4 times, and percent recovery was 39. The kinetic constants of the enzyme were studied. Km and Vmax was $1.5{\times}10^{-7}M\;and\;0.11{\Delta}O.D/min$ , respectively, when casein was used as substrate. The order of Km value of several proteins is : casein

• Journal of Microbiology and Biotechnology
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• 제25권11호
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• pp.1810-1818
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• 2015

For the synthesis of various pharmaceuticals, chiral alcohols are useful intermediates. Among them, (R)-ethyl-4-chloro-3-hydroxybutanoate ((R)-ECHB) is an important building block for the synthesis of L-carnitine. (R)-ECHB is produced from ethyl-4-chloro-3-oxobutanoate (ECOB) by a reductase-mediated, enantioselective reduction reaction. The Saccharomyces cerevisiae YOL151W reductase that is expressed in Escherichia coli cells exhibited an enantioselective reduction reaction toward ECOB. By virtue of the C-terminal His-tag, the YOL151W reductase was purified from the cell-free extract using Ni²⁺-NTA column chromatography and immobilized onto Ni²⁺-magnetic microparticles. The physical properties of the immobilized reductase (Imm-Red) were measured using electron microscopy, a magnetic property measurement system, and a zeta potential system; the average size of the particles was approximately 1 μm and the saturated magnetic value was 31.76 emu/g. A neodymium magnet was used to recover the immobilized enzyme within 2 min. The Imm-Red showed an optimum temperature at 45℃ and an optimum pH at 6.0. In addition, Bacillus megaterium glucose dehydrogenase (GDH) was produced in the E. coli cells and was used in the coupling reaction to regenerate the NADPH cofactor. The reduction/oxidation coupling reaction composed of the Imm-Red and GDH converted 20 mM ECOB exclusively into (R)-ECHB with an e.e._p value of 98%.

• 한국미생물·생명공학회지
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• 제30권4호
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• pp.332-338
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• 2002

토양으로부터 세포외로 $\alpha$-galactosidase를 분비 생산하는 방선균 YB-4가 분리되었으며, 분리균의 배양ㆍ형태ㆍ생리적 특성을 조사한 결과 Streptomyces 속 균주로 확인되었다. 분리균의 배양상등액으로부터 부분정제된 $\alpha$-galactosidase를 조효소액으로 사용하였을 때 para-nitrophenyl-$\alpha$-D-galacto-pyranoside는 pH 6.0과 6$0^{\circ}C$의 반응조건에서 가장 잘 분해되었으며, 조효소액을 pH 4.0에서 pH 10.0범위에서 1시간 이상 방치한 후에도 약 90% 이상의 $\alpha$-galactosidase 활성을 유지하였다. 또한 분리균이 생산하는 $\alpha$-galactosidase는 melibiose, raffinose와 stachyose와 같은 저당류를 가수분해 할 수 있으며 분해산물로 galactose를 방출하는 것으로 보아 $\alpha$-1,6 결합을 분해한 것으로 확인되었다.

• 한국미생물·생명공학회지
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• 제27권4호
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• pp.298-303
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• 1999

An $\alpha$-D-galactosidase ($\alpha$-D-galactoside galactohydrolase, EC 3. 2. 1. 22) from earthworm was purified by affinity chromatography using N-$\varepsilon$-aminocaproyl-$\alpha$-D-galactopyranosylamine coupled to sepharose and its properties were examined. The specific activity of the purified enzyme, tested with p-nitrophenyl-$\alpha$-D-galactopyranoside as substrate, was 314 units/mg protein, representing an 122-fold purification of the original crude extract. The final preparation obtained from by Sephadex G-25 chromatography showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 48,000 by SDS-polyacrylamide gel electrophoresis. The purified galactosidase was showed maximum activity at pH 4.5 and 4$0^{\circ}C$, and was stable in the pH and temperature ranges from 4.0 to 5.5 and 30 to 5$0^{\circ}C$, respectively. The enzyme activity was inhibited by Zn2+, Hg2+ and Co2+. When the purified $\alpha$-galactosidase treated to guar gum for 6 hour, gel-promoting property was increased. It was clear that enzymatic elimination of galactose from guar gum by purified $\alpha$-galactosidase would lead to a significant increase in gelation ability.

• Journal of Microbiology
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• 제35권2호
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• pp.141-148
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• 1997

Alcaligenes xylosoxydans strain SMN3 capable of utilizing biphenyl grew not only on phenol, and benzoate, but also on salicylate. Catabolisms of biphenyl and salicylate appear to be interrelated since benzoate is a common metabolic intermediate of these compounds. Enzyme levels in the excatechol 2. 3-dioxygenas which is meta-cleavage enzyme of catechol, but did not induce catechol 1, 2-dioxygenase. All the oxidative enzymes of biphenyl and 2, 3,-dihydroxybiphenyl (23DHBP) were induced when the cells were grown on biphenyl and salicylate, respectively. Biphenyl and salicylate could be a good inducer in the oxidation of biphenyl and 2, 3-dihydroxybiphenyl. The two enzymes for the degradation of biphenyl and salicylate were induced after growth on either biphenyl or salicylate, suggesting the presence of a common regulatory element. However, benzoate could not induce the enzymes responsible for the oxidation of these compounds. Biphenyl and salicylate were good inducers for indigo formation due to the activity of biphenyl dioxygenase. These results suggested that indole oxidation is a property of bacterial dioxygenase that form cis-dihydrodiols from aromatic hydrocarbon including biphenyl.

• Parasites, Hosts and Diseases
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• 제41권3호
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• pp.165-169
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• 2003

This study describes the characterization of 80 kDa pretense showing gelationlytic property among three pretenses in the excretory/secretory proteins (ESP) from Toxoplasma gondii. The pretense activity was detected in the ESP but not in the somatic extract of RH tachyzoites. This pretense was active only in the presence of calcium ion but not other divalent cationic ions such as $Cu^{2+},{\;}Zn^{2+},{\;}Mg^{2+},{\;}and{\;}$Mn^{2+}$, implying that $Ca^{2+}$ is critical factor for the activation of the protease. The 80 kDa pretense was optimally active at pH 7.5. Its gelatinolytic activity was maximal at $37^{\circ}C$, and significant level of enzyme activity of the pretense remained after heat treatment at $56^{\circ}C$ for 30 min or $100^{\circ}C$ for 10 min, This thermostable enzyme was strongly inhibited by metal chelators, i.e., EDTA, EGTA, and 11 10-phenanthroline. Thus, the 80 kDa pretense in the ESP secreted by T. gondii was classified as a calcium dependent neutral metalloprotease.