• Title/Summary/Keyword: enzyme hydrolysis

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Enzyme Hydrolysis of Insoluble sericin (불용성 세리신의 효소 가수분해)

  • 김정호;배도규
    • Journal of Sericultural and Entomological Science
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    • v.42 no.2
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    • pp.104-108
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    • 2000
  • To hydrolyze insolule sericin the enzyme hydrolysis was used, and then obtained the results as given belows. When insoluble sericin was hydrolyzed by enzyme treatment, the solubility was best at pH 7, 60$\^{C}$ and was slightly increased both above 2 hours treatment and above 10% of enzyme concentration. As the results of electrophoresis, the distribution of molecular weight of sericin powder obtained by enzyme hydrolysis was very weak and showed in the wide range having no distinguishable band. Average degree of polymerzations (A.D.P.) of sericin hydrolyzed by enzyme were about 4.1∼6.3, average molecular weight were about 470∼730. The whiteness of the sericin powder obtained by enzyme hydrolysis was high and increased slightly with higher treatment concentration of enzyme. As the results of amino acid analysis, the amino acid analysis, the amino acid composition of the sericin powder from the enzyme treatment were similar to which located at near 230$\^{C}$ and 320$\^{C}$. The peak of near 230$\^{C}$ could not been found in the sericin powder obtained by enzyme hydrolysis.

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Cellulose Hydrolysis by Digestive Enzymes of Reticulitermes speratus, a Native Termite from Korea

  • Lee, Young-Min;Kim, Hyun-Jung;Cho, Moon-Jung;Shin, Keum;Kim, Young-Kyoon;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • v.38 no.2
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    • pp.140-148
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    • 2010
  • This study was to investigate the enzymatic hydrolysis of cellulose using the cellulase from whole body of the native termite collected in Milyang-si, Kyungsangnamdo, Korea. In the results, optimal temperature and pH for the enzyme of native termites were $45^{\circ}C$ and pH 5.5 for both endo-${\beta}$-1, 4-glucanase and ${\beta}$-glucosidase. Enzyme activity of the termite enzyme was shown $8.8{\times}10^{-2}\;FPU/m{\ell}$. And the highest glucose hydrolysis rate of cellulose by the digestive enzyme from test termites was 24.5% based on the glucan, comparing 59.7% by commercial enzyme (only celluclast 1.5 L) at 1% (w/v) substrate and 36 hours in hydrolysis time. This hydrolysis rate by the digestive enzyme from test termites was comparatively high value in 41% level of the commercial enzyme. When cellulose was hydrolyzed by the digestive enzyme of the native termite, glucose hydrolysis was almost completed in 12 hours which was the considerably reduced time for cellulose hydrolysis. It was suggested that the quiet short reaction time for cellulose hydrolysis by the enzyme from native termite could be a very high advantage for development of hydrolysis cellulase for lignocellulosic biomass.

Functional Analyses and Application of Microbial Lactonohydrolases

  • Shimizu, Sakayu;Honda, Kohsuke;Kataoka, Michihiko
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.7 no.3
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    • pp.130-137
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    • 2002
  • Microbial lactonohydrolases (intramolecular ester bond-hydrolyzing enzymes) with unique properties were found. The lactonohydrolase from Fusarium oxysporum catalyzes enantiose-lective hydrolysis of aldonate lactones and D-pantoyl lactone (D-PL). This enzyme is useful for the large-scale optical resolution of racemic PL. The Agrobacterium tumefaciens enzyme catalyzes asymmetric hydrolysis of PL, but the stereospecificity is opposite to that of the Fusarium enzyme. Dihydrocoumarin hydrolase (DHase) from Acinetobacter calcoaceticus is a bifunctional enzyme, which catalyzes not only hydrolysis of aromatic lactones but also bromination of monochlorodi-medon in the presence of H$_2$O$_2$and dihydrocoumarin. DHase also hydrolyzes several linear esters, and is useful for enantioselective hydrolysis of methyl DL-$\beta$-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate.

Angiotensin I Converting Enzyme Inhibitory Activity of Krill (Euphausia superba) Hydrolysate

  • Kim Dong-Soo;Park Douck-Choun;Do Jeong-Ryong
    • Fisheries and Aquatic Sciences
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    • v.5 no.1
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    • pp.21-27
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    • 2002
  • Angiotensin I converting enzyme inhibitory activities of shelled krill (Euphausia superba) hydrolysates by autolysis and by hydrolysis with commercial proteases were analyzed. Among the proteases, Alcalase was the most effective protease for the hydrolysis of krill considering the degree of hydrolysis $(87.5\%)$ and the ACE inhibitory activity $(60\%)$. Four hour hydrolysis suggested as the most suitable and economic. In order to establish the optimum hydrolysis condition of krill, degree of hydrolysis and ACE inhibitory activity as affected by Alcalase concentration and water amount added were statistically analyzed by response surface methodology (RSM). The optimum hydrolysis condition was $2.0\%$ Alcalase hydrolysis in 2 volumes (v/w) of water at $55\% for 4 hr. The hydrolysate prepared from the optimum hydrolysis condition was fractionated by molecular weight. The lower molecular weight fraction showed the higher ACE inhibitory activity. $IC_{50}$ of the fraction under 500 Da was 0.57mg protein/mL.

Kinetic Studies on Enzymatic Hydrolysis of Cellulose(I) -Effect of Structural Features of Cellulose on Enzyme Adsorption- (섬유소 가수분해반응에 관한 연구(I) -효소흡착에 대한 섬유소의 구조적 특성-)

  • Lee, Yong-Hun;Kim, Chul
    • KSBB Journal
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    • v.6 no.2
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    • pp.157-166
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    • 1991
  • The structural properties of cellulose are significantly changed with the progress of hydrolysis reaction. The effects of changes on such properties of cellulosic substrate as crystallinity, amicessibility of enzyme to the active site of cellulose surface, and particle size on the kinetics of enzymatic hydrolysis have been studied. Among those physical studies, the apparent surface active site of cellulose particle was found to have the most significant effect on the hydrolysis kinetics. Based on the experimental results, the adsorption affinity of enzyme and hydrolysis rate were mainly influenced by the surface roughness of cellulose particle. The extent of accesssible active site may be expressed as the change of particle diameter. The Langmuir isotherm was proposed in terms of enzyme activity to explain the actual action of enzyme protein.

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Biodegradability of Polylactic Acid Fabrics by Enzyme Hydrolysis and Soil Degradation

  • Lee, So Hee
    • Textile Coloration and Finishing
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    • v.29 no.4
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    • pp.181-194
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    • 2017
  • The biodegradability of polylactic acid(PLA) fabrics was evaluated by two methods: enzyme and soil degradation. Three different enzymes were selected to evaluate. Degradation times were measured at optimal enzyme treatment conditions. Biodegradation by enzymatic hydrolysis was compared with soil degradation. As a result, biodegradation created cracks on the fiber surface, which led to fiber thickening and shortening. In addition, new peak was observed at $18.5^{\circ}$ by degradation. Moreover, cracks indicating biofragmentation were confirmed by enzyme and soil degradation. By enzyme and soil degradation, the weight loss of PLA fabrics was occurred, there through, the tensile strength decreased about 25% by enzyme hydrolysis when 21 days after, and 21.67% by soil degradation when 60 days after. Furthermore, the biodegradability of PLA fabrics by enzymatic and soil degradation was investigated and enzymatic degradation was found to be superior to soil degradation of PLA fabrics. Among the three enzymes evaluated for enzymatic degradation, alcalase was the most efficient enzymes. This study established the mechanism of biodegradation of PLA nonwovens, which might prove useful in the textile industry.

Optimization of Enzymatic Hydrolysis Conditions for Production of Angiotensin-I Converting Enzyme Inhibitory Peptide from Casein

  • Do, Jeong-Ryong;Kim, Ki-Ju;Kim, Hyun-Ku;Kim, Young-Myoung;Park, Yeung-Beom;Lee, Yang-Bong;Kim, Seon-Bong
    • Food Science and Biotechnology
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    • v.16 no.4
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    • pp.565-571
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    • 2007
  • This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

Evaluation of Secondary Acid and Enzymatic Hydrolysis of Hemicellulose in Hot Water Pre-Pulping Extract of Mixed Hardwoods

  • Um, Byung-Hwan
    • Journal of the Korean Wood Science and Technology
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    • v.40 no.2
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    • pp.123-132
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    • 2012
  • Pre-pulping extracts were found to contain a dilute amount of xylo-oligosaccharides and acetic acid as the major components, and many minor components including other organic acids, lignin-derived phenolics, and sugar degradation products. Once separated from the pulp, a secondary hydrolysis step was required to hydrolyze oligomeric hemicellulose sugars into monomeric sugars before fermentation. The following study detailed the extent of hemicellulose recovery by pre-pulping using hot water extraction and characterized the hydrolysis of the extract with respect to comparing acid and enzymatic hydrolysis. The secondaryhydrolysis of hot water extracts made at an H-Factor of 800 was tested for a variety of acid and enzyme loading levels using the sulfuric acid and xylanases. The maximum fermentable sugar yield from acid and enzyme hydrolysis of the extract was 18.7 g/${\ell}$ and 17.7 g/${\ell}$ representing 84.6% and 80.1% of the maximum possible yield, respectively.

A Study on Improvement of Oriental Drugs Preparation by Enzyme (효소(酵素)를 이용한 한약(韓藥) 전탕법(煎蕩法)의 개선(改善)에 관한 연구(硏究))

  • Ko, Byoung-Seob;Park, Kap-Joo;Hong, Won-Sik;Choi, Mi-Kyeong;Kim, Mung-Hee
    • The Journal of Korean Medicine
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    • v.18 no.1
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    • pp.506-514
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    • 1997
  • This study was conducted to improve preparations of oriental drugs by enzyme. Total sugar, reduced sugar, hydrolysis rate, and amylose content were compared in Korean yam starch and some oriental drugs treated different enzyme levels and treatment times. The results were as follows. Reduced sugar and hydrolysis rate by enzyme of yam starch were significantly increased according to increments of enzyme level and treatment time. Amylose content in yam starch was significantly decreased to increment of enzyme level and treatment time. Total sugar content in some oriental drugs of Sangmaeksan, Yukmigiwhang, Yukshinsan, Manbungsarungsan, and Sanyaksogalum were 46.08, 44.87, 11.15, 10.67, and $6.l6mg/m{\ell}$, respectively. There was no significant difference in hydrolysis rate by enzyme of Sangmaeksan, Yukmigiwhang, Manbungsarungsan. However, hydrolysis rates of Yukshinsan and Sanyaksogalum were significantly highest in 0.2% enzyme and 0.5% enzyme groups, respectively.

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Studies on the Enzymatic Hydrolysis of Lignocellulosic Materials for the Alternative Fuels(III) - Quantitative Recycling of Cellulase Enzyme in the Enzymatic Hydrolysis of Steam-Exploded Woods - (대체연료(代替燃料) 생산(生産)을 위한 목질재료(木質材料)의 가수분해(加水分解)에 관한 연구(硏究) (III) - 폭쇄(爆碎)처리재의 산소분해시(酸素分解時) Cellulase 산소(酸素)의 정량적(定量的) 회수(回收)에 관하여 -)

  • Cho, Nam-Seok;Lim, Chang-Suk;Lee, Jae-Sung;Park, Shin
    • Journal of the Korean Wood Science and Technology
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    • v.19 no.1
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    • pp.14-21
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    • 1991
  • Steam-exploded woods were delignified by two-stage with a 0.3% NaOH extraction and oxygen-alkali bleaching and were subjected to the enzymatic hydrolysis with cellulase enzyme. Also, an improved almost quantitative recycle process of cellulase enzyme was discussed. In enzyme recovery by affinity method, The first recycling showed relatively high hydrolysis rate of 96.4%. Even at the third recycle, hydrolysis rate was 87.0 percents. In the case of cellulase recovery by ultrafiltration method, first 2 recycling treatments resulted in very high hydrolysis rates, 96.8% and 95.0%, respectively. Even the third recycling showed about 93.6%. Steam-explosion treatment of oak wood followed by 2-stage delignification with alkali and oxygen-alkali produced a excellant substrate for the enzymatic hydrolysis that allowed almost quantitative recycle of cellulase.

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