• Title, Summary, Keyword: Enzyme

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Effect of Enzyme Retting on the Fiber Separation of Kenaf Bast - influence of chelator - (효소 레팅에 의한 케냐프 섬유의 분리 -킬레이터의 영향-)

  • 이혜자;안춘순;김정희;유혜자;한영숙;송경헌
    • Journal of the Korean Society of Clothing and Textiles
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    • v.28 no.7
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    • pp.873-881
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    • 2004
  • This research was aimed to investigate the effect of enzyme and the addition of chelators on rotting of the Kenaf bast. Enzyme rotting was effective only when the chelators were added with the enzyme. EDTA was a more effective chelator than oxalic acid under 1% concentration. There was no difference in the rotting effect under different enzyme concentration levels, and under different treatment time and temperature. Therefore, it was found that enzyme rotting can be carried out with low enzyme concentration(0.125%) at room temperature. Retting time can be shortened when higher enzyme concentration and higher temperature are applied. Cellulose I structure of kenaf fiber did not change after enzyme rotting, and different enzyme concentration did not affect the crytallinity structure. Non-cellulosic matters such as hemicellulose, lignin, and pectin were present in the descending order in the enzyme rotted kenaf fiber, and there were no differences in their amounts due to enzyme concentration levels. There was no difference in the dyeabilities of kenaf fiber rotted with different enzyme concentration levels. Enzyme rotted kenaf fiber showed better cyeability when pectin, lignin, and hemicellulose were removed.

Effects of Water and Silica Gel on Enzyme Agglomeration in Organic Solvents

  • Keehoon Won;Lee, Sun-Bik
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.6 no.2
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    • pp.150-155
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    • 2001
  • It has been observed that water, which is absolutely essential for enzyme activity, can induce the agglomeration of enzyme particles in organic media. Although enzyme agglomeration is significant in that it usually reduces enzyme activity and stability, little attention has been paid to the quantitative analysis of enzyme agglomeration behavior in nonaqueous biocatalytic systems. In this study, the effect of water and silica gel on enzyme agglomeration were investigated using Candida rugosa lipase and cyclohexane as a model enzyme and an organic medium. The extent of enzyme agglomeration was quantified by sieve analysis of freeze-dried agglomerates. Increasing the water content of the medium increased the size of the enzyme agglomerates, and it was found that water produced during the esterification reaction could also promote the agglomeration of enzyme particles suspended in organic media. On the other hand, the size of the enzyme agglomerates was remarkably reduced in the presence of silica gel at the same water content. We also show that this increase in the size of enzyme agglomerates results in lower reaction rates in organic solvents.

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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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Understanding Enzyme Structure and Function in Terms of the Shifting Specificity Model

  • Britt, Billy Mark
    • BMB Reports
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    • v.37 no.4
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    • pp.394-401
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    • 2004
  • The purpose of this paper is to suggest that the prominence of Haldane's explanation for enzyme catalysis significantly hinders investigations in understanding enzyme structure and function. This occurs despite the existence of much evidence that the Haldane model cannot embrace. Some of the evidence, in fact, disproves the model. A brief history of the explanation of enzyme catalysis is presented. The currently accepted view of enzyme catalysis -- the Haldane model -- is examined in terms of its strengths and weaknesses. An alternate model for general enzyme catalysis (the Shifting Specificity model) is reintroduced and an assessment of why it may be superior to the Haldane model is presented. Finally, it is proposed that a re-examination of many current aspects in enzyme structure and function (specifically, protein folding, x-ray and NMR structure analyses, enzyme stability curves, enzyme mimics, catalytic antibodies, and the loose packing of enzyme folded forms) in terms of the new model may offer crucial insights.

Purification and Biochemical Analysis of Rice Bran Lipase Enzyme

  • Kim, Young Hee
    • Journal of Plant Biotechnology
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    • v.6 no.1
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    • pp.63-67
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    • 2004
  • A simple procedure for the extraction of the lipolytic enzyme from rice bran has been developed. High activity of lipolytic enzyme was obtained by first defatting the rice bran to remove lipid components with various extraction conditions. Then, after rove cycles of aqueous extraction, rice bran lipolytic enzyme was purified using micro- and ultrafiltration apparatus. Lipolytic enzyme activity was estimated by its hydrolytic action of tributyrin. The result indicated that the standard activity curve of butyric acid showed that the potential rice bran enzyme is a hydrolytic lipase enzyme. In addition, it showed higher lipolytic activity and specific enzyme activity with further purification by micro- and ultrafiltration. The size of rice bran lipase enzyme was identified through 15 % SDS-PAGE. The molecular weight of the rice bran lipase enzyme was 41 kDa.

Enzyme Activity and Beating Properties for Preparation of MicroFibrillated Cellulose(MFC) (MicroFibrillated Cellulose(MFC) 제조를 위한 전처리 효소의 활성 및 고해 특성)

  • Kim, Kang-Jae;Jung, Jin-Dong;Jung, Soo-Eune;Ahn, Eun-Byeoul;Eom, Tae-Jin
    • Journal of Korea Technical Association of The Pulp and Paper Industry
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    • v.47 no.1
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    • pp.59-65
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    • 2015
  • In this study, we evaluated optimum condition of enzyme with pH and temperature for preparation of microfibillated cellulose(MFC). Well-known endo-glucanase, three enzymes were used and CMC was used for substrate. Enzyme activity was evaluated using DNS method and absorbance with UV/VIS spectrophotometer. The enzyme shown the greatest activity was reacted with pulps at optimum condition for 1 hour and treated pulps beated until 100 mL CSF. Enzyme B and Enzyme L was the higher enzyme activity below 0.1% concentration and Enzyme N was the lowest enzyme activity. At various pH and temperature conditions, enzyme activity of Enzyme B was higher than the others at the same concentration. Especially enzyme activity at $50^{\circ}C$ of Enzyme B was almost not changed over pH 6.0. Optimum condition of three enzyme was pH 6 or pH 7 and $50^{\circ}C$ or $60^{\circ}C$. Also beating efficiency of enzyme treated pulps with Enzyme B is 55.6%.

Effects of Enzyme Application Method and Levels and Pre-treatment Times on Rumen Fermentation, Nutrient Degradation and Digestion in Goats and Steers

  • Hong, S.H.;Lee, B.K.;Choi, N.J.;Lee, Sang S.;Yun, S.G.;Ha, J.K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.3
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    • pp.389-393
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    • 2003
  • Present study investigate the effect of enzyme supplementation, methods (applied to rumen or enzyme treated diet) compared with no enzyme diet, on rumen fermentation and apparent nutrient digestibility in a $3{\times}3$ Latin square design with three rumen cannulated Korean Native goats. In situ rumen degradation kinetics was studied in three rumen cannulated Holstein steers. Three diets were, no enzyme, 1% enzyme in rumen and 1% enzyme in diet. The enzyme was sprayed onto forage, and the forage: concentrate ratio was 30:70. Degradation kinetics was studied with three enzyme levels (0, 1 and 2%, w/w) and four pre-treatment times (0, 1, 12 and 24 h). Results suggested that enzyme application method did not affect rumen fermentation, ruminal enzyme activity and total tract apparent digestibility. Nutrient degradation rate and effective degradability of DM, NDF and ADF increased with increasing enzyme level and pre-treatment times. Degradation of nutrients was affected by enzymes levels or pre-treatment times. Therefore, it is probable that the improved degradation may be due to the supplemented exogenous hydrolytic enzymes under a certain condition.

Effects of Fibrolytic Enzyme Addition on Ruminal Fermentation, Milk Yield and Milk Composition of Dairy Cows (Fibrolytic Enzyme 첨가가 반추위 발효 성상 및 착유우의 유량 및 유성분에 미치는 영향)

  • Ahn, J. H.;Kim, Y. J.;Kim, H. J.
    • Journal of Animal Science and Technology
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    • v.45 no.1
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    • pp.131-142
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    • 2003
  • We evaluated the effects of adding fibrolytic enzyme into ruminant diets on ruminal fermentation (in vitro) and lactational performances of dairy cows (in vivo). Through the in vitro experiment that was carried out with different contents of NDF (34, 38, 43%) in diets, digestibilities of NDF in the rumen appeared not significantly different by the addition of enzyme but were different by NDF content in diets showing higher digestibility in NDF 43% diet. It could be attributed by the relatively higher amount of hemicellulose in the current experimental diets than in conventional diets that might have been digested easily by the addition of fibrolytic enzyme in the rumen. The addition of fibrolytic enzyme tended to increase NDF digestibilities to a little extent both in 0.05 and 0.1% enzyme levels. Ruminal pH, NH3-N concentrations and VFA production in the rumen were not affected by the addition of fibrolytic enzyme. Activities of CMCase and xylanase were higher in enzyme treated diets of both NDF 34 and 38%. In particular, the activities of xylanase that slowly decreased from 0 to 12 hr but rapidly after 24 hr indicates that the major action of the enzyme in the rumen occurs in early period of incubation. Through an in vivo experiment, fibrolytic enzyme addition into the diets of dairy cows indeed affected lactational performance of milk yield. The cows fed enzyme treated diets produced 8% (1.9kg/d) more amounts of milk than with no enzyme addition. Milk composition of milk fat and protein was not affected by enzyme addition. Overall, the results of this in vivo study indicates that fibrolytic enzyme can be used to improve milk production in lactating cows. In respect that animals in different treatments of this study had the same amounts of intake, the increased milk yield with enzyme addition may be attributed to the improved utilization of nutrients in the digestive tract.

Influences of Enzyme Complex Supplementation on Growth, Ileal and Apparent Fecal Digestibility and Morphology of Small Intestine in Pigs

  • Kim, B.G.;Tian, J.Z.;Lim, J.S.;Kil, D.Y.;Jeon, H.Y.;Chung, Y.K.;Kim, Y.Y.
    • Asian-Australasian Journal of Animal Sciences
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    • v.17 no.12
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    • pp.1729-1735
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    • 2004
  • A total of 140 weaning pigs were used to determine the effects of digestive enzyme supplementation to corn-soybean meal diets on growth performance, physiological changes of small intestine, microorganisms and pH in the gastrointestinal tract. Two kinds of enzyme complex (A, B) were used in this experiment. Pigs were allotted in a completely random design (CRD) to five replicates with four pigs per pen. Diets and water were provided for ad libitum consumption. Treatments included 1) Control: without enzyme supplementation, 2) Enzyme A 0.05%, 3) Enzyme A 0.10%, 4) Enzyme A 0.15%, 5) Enzyme B 0.05%, 6) Enzyme B 0.10%, 7) Enzyme B 0.15% in the diets. A total of 24 crossbred barrows 25.78${\pm}$0.55 kg BW fitted with simple ileal T-cannulas were used to evaluate the effect the enzyme addition on the nutrient digstibility. Pigs were allotted 4 treatments (No enzyme, enzyme A 0.05%, enzyme A 0.1%, enzyme A 0.15%), 6 replicates according to a completely random design (CRD). Another digestibility trial was followed for enzyme complex B. Twenty pigs, average 31.92${\pm}$0.37 kg BW, fitted with simple ileal T-cannulas for digestibility trial. Neither enzyme A nor enzyme B affected on fecal or ileal digestibility of dry matter, gross energy, crude protein, crude fat and crude ash (p>0.05). The apparent fecal digestibilities of all the nutrients were higher in total feces collection method than in indirect method. At the end of feeding trial, 21 pigs were slaughtered for examining the morphological changes of small intestine and the concentration of microorganisms in the ileum and the colon. Growth performance, intestinal morphology and pH of ileum and colon were not affected by the either enzyme complex supplementation (p>0.05). These results suggested that enzyme complex A and enzyme complex B were of no benefit to early-weaned pigs when corn-soybean meal based diet was provided.

Physical and catalytic properties of CMCase encoded by Bacillus subtilis gene in B. megaterium

  • Kim, Hoon;Kim, Ha-Geun;Park, Moo-Young
    • Proceedings of the Korean Society for Applied Microbiology Conference
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    • pp.524.3-524
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    • 1986
  • Carboxymethyl cellulase (CMCase) produced by cloned B. megaterium was found to contain 5.2% carbohydrate but no metal ion. The enzyme was isoelectric at pH 7.23 and was high is basic amino acids. The N-terminal of the enzyme was glutamic acid. The cellulolytic activity of this enzyme was extended to the small molecular substrates such as from cellotriose to cellopentaose. In additon, the enzyme showed transglycoslation activity. The pK values of the enzyme we estimated to be 4.4 and 6.7, andthat of the enzyme-substrate complex were 4.2 and 7.2, respectively. The enzyme was not affected by the treatment with iodoacetic acid, but the modification of enzyme with carbodiimide and diethyl pyrocarbonate resulted in a marked loss of the enzyme activity. These results suggest that the active site of enzyme essentially contains carboxylic and imidazole group of amino acid residues.

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