• 제목/요약/키워드: addition of enzyme

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

  • 안종호;김연정;김현진
    • Journal of Animal Science and Technology
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    • 제45권1호
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    • pp.131-142
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    • 2003
  • 본 연구는 유우의 생산성 향상을 위하여 유우 사료에 fibrolytic enzyme을 첨가하여 반추위내 발효 성상과 비유중인 젖소의 생산성에 미치는 영향을 평가하였다. 본 실험의 결과를 요약하면 다음과 같다. In vitro 실험을 통하여 NDF 함량 수준이 다른 TMR 사료에 fibrolytic enzyme을 3가지 수준(0, 0.05, 0.1%)으로 달리하여 첨가하였을 때 나타난 NDF 소화율은 효소 첨가시 다소 증가하는 경향을 보였으며 NDF 수준별로는 NDF 38 및 43% 수준보다 NDF 34% 수준에서 NDF 소화율이 낮은 경향을 나타내었는데 이는 본 시험 사료의 조성 성분으로 보아 NDF 성분 구성상 hemicellulose 함량이 높아 이 점이 반추위내 NDF 소화율에 영향을 주었다고 사료된다. 반추위액의 pH는 fibrolytic enzyme의 첨가 수준에 의한 영향보다는 NDF 수준에 의해 영향을 더 받은 것으로 나타났으며(P<0.001) NH3-N 생성도 전체적으로 fibrolytic enzyme 첨가에 따른 효과가 나타나지 않았다. Acetic acid의 생성량은 NDF 수준에 의해 유의한 영향을 받았으나 (P<0.05) propionic acid의 생성량은 처리구간에 큰 차이를 나타내지 않았다. Acetic acid와 propionic acid 생성량 모두 효소 첨가에 의한 영향은 유의하게 나타나지 않았고 A/P ratio는 NDF 34% 수준의 fibrolytic enzyme 첨가구에서 무첨가구에 비해 다소 높은 경향을 나타내었다. CMCase의 효소 활성은 NDF 34 및 43% 수준에서 fibrolytic enzyme 첨가구(0.05, 0.1%)가 무첨가구에 비해 높은 효소 활성을 보였다. Xylanase의 효소 활성은 배양 개시 후 0시간대부터 12시간대까지는 효소 활성이 완만히 감소하였고 24시간 이후부터는 급격히 감소하였다. In vivo 실험을 이용하여 fibrolytic enzyme 첨가에 따른 착유우의 생산성 변화 결과는 다음과 같다. Fibrolytic enzyme 첨가에 의한 산유량은 enzyme 첨가구와 무첨가구에서 각각 25.80 및 23.90kg/d로서 enzyme 첨가구에서 약 8% (1.90kg/d) 증가하는 결과를 나타내었다. 유지방 및 유단백 함량의 경우는 fibrolytic enzyme 첨가구와 무첨가구간 차이가 없었으나 일일 생산량으로 환산하여 평가하면 enzyme 첨가시 유성분 생산량이 유의하게 증가하는 결과를 보였다 (P<0.01). 이상의 결과들로 볼 때, in vitro 실험의 경우 fibrolytic enzyme 첨가시 반추위내 발효성상에 명확한 변화를 보여주지 못했지만 enzyme 첨가에 따라 전반적으로 NDF 소화율이 다소나마 증가하는 경향을 보였다. In vivo 실험 결과를 종합하면 착유우 사료에 fibrolytic enzyme을 첨가시 유성분의 변화보다 유량의 증가 효과가 나타났으며 이는, 사료섭취량을 제한한 본 실험의 특성상, 사료섭취량 증진 효과가 아니라 체내 영양소 이용성 증진에 따르는 효과라고 판단되었다. 반추동물의 생산성 향상을 위한 방안으로서 fibrolytic enzyme 이용 효과는 연구자에 따라 다양한 결과를 나타내므로 효소의 적용 방법에 대한 연구가 더 필요하다고 사료된다.

Xylanase 첨가에 따른 수수의 제빵 적성 변화 (Effects of Xylanase on the Baking Properties of Sorghum)

  • 안지은;고지연;고봉경
    • 한국식품조리과학회지
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    • 제31권1호
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    • pp.18-25
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    • 2015
  • This study investigated the baking properties of sorghum with the addition of xylanase or Pentopan, which is a baking additive containing xylanase. The control bread was made with a 30% substitution for wheat flour and the optimum level of enzyme addition was 0.75 mg/g flour for Pentopan and 5 mg/g flour for xylanase. The water binding capacity of wheat flour increased with the addition of sorghum, but decreased with the addition of either xylanase or Pentopan. The resistance of dough increased while extensibility decreased with the addition of sorghum; however, resistance decreased while extensibility increased with the addition of the enzyme. Specific volume of bread decreased significantly with the addition of sorghum. However, the specific volume was significantly recovered with the addition of enzyme. Crumb firmness was higher in the sorghum-added sample, but crumb firmness of the bread decreased with the addition of the enzyme. The crumb firmness of bread with added xylanase decreased significantly in 24 hours. These results demonstrated that adding sorghum with either xylanase or Pentopan that included xylanase increased specific volume and decreased crumb firmness whereas sorghum decreased the quality of fermented bread when added to wheat flour. The firmness rate of fermented bread particularly decreased with the addition of pure xylanase.

Enhanced Enzyme Activities of Inclusion Bodies of Recombinant ${\beta}$-Galactosidase via the Addition of Inducer Analog after L-Arabinose Induction in the araBAD Promoter System of Escherichia coli

  • Jung, Kyung-Hwan
    • Journal of Microbiology and Biotechnology
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    • 제18권3호
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    • pp.434-442
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    • 2008
  • We observed that an inclusion body (IB) of recombinant ${\beta}$-galactosidase that was produced by the araBAD promoter system in Escherichia coli (E. coil) showed enzyme activity. In order to improve its activity, the lowering of the transcription rate of the ${\beta}$-galactosidase structural gene was attempted through competition between an inducer (L-arabinose) and an inducer analog (D-fucose). In the deep-well microtiter plate culture and lab-scale fermentor culture, it was demonstrated that the addition of D-fucose caused an improvement in specific ${\beta}$-galactosidase production, although ${\beta}$-galactosidase was produced as an IB. In particular, the addition of D-fucose after induction led to an increase in the specific activity of ${\beta}$-galactosidase IB. Finally, we confirmed that the addition of D-fucose after induction caused changes in the structure of ${\beta}$-galactosidase IB, with higher enzyme activity. Based on these results, we expect that an improved enzyme IB will be used as a biocatalyst of the enzyme bioprocess, because an enzyme IB can be purified easily and has physical durability.

The Response of Nitrogen Deposition to Methane Oxidation Availability and Microbial Enzyme Activities in Forest Soils

  • Jang, In-Young;Lee, Hyoung-Min;Kang, Ho-Jeong
    • Environmental Engineering Research
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    • 제15권3호
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    • pp.157-161
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    • 2010
  • Forest soils are often nitrogen-limited, and nitrogen input to forest soils can cause substantial changes in the structure and functions of a soil ecosystem. To determine the effects of nitrogen input on methane oxidation and the microbial enzyme activities, manipulation experiments were conducted using nitrogen addition to soil samples from Mt. Jumbong. Our findings suggested that the addition of nitrogen to the soil system of Mt. Jumbong did not affect the microbial enzyme activities. Conversely, the addition of nitrogen affected the rate of methane oxidation. Inorganic nitrogen in soils can inhibit methane oxidation via several mechanisms, such as substrate competition, toxic effects, and competition with other microbes, but the inhibitory effects are not always the same. In this research, seasonal changes were found to produce different inhibitory factors, and these different responses may be caused from differences in the methantrophic bacteria community structure.

헤이즐넛 첨가에 따른 청국장의 품질 특성 변화 (Changes in the Quality Characteristics of Cheonggukjang prepared with Hazelnut)

  • 김종덕;이영현;이난희;김대현;최웅규
    • 한국식품영양학회지
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    • 제31권6호
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    • pp.926-932
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    • 2018
  • This research was conducted to investigate the changes in quality characteristics of cheonggukjang fermented with the addition of hazelnut (10, 20, 30 and 40%) including; water content, pH, hydrophilic and lipophilic substances, color, viscosity and angiotensin converting enzyme inhibition activity. There was no significant change in pH with the addition of hazelnut. The water content significantly decreased with the addition of hazelnut. Hazelnut was also found to brighten the color of cheonggukjang. L-value and b-value increased with the addition of cheonggjuang. There was an insignificant change in the a-value. There was a slight decrease in the content of hydrophilic with addition of hazelnuts. Where there was more than 20% addition of hazelnut to soybean, the viscous substance content in cheonggukjang decreased significantly. Angiotensin converting enzyme inhibitory activity increased proportionally to the amount of hazelnut added. It was identified that the addition of 40% of hazelnut made its angiotensin converting enzyme inhibitory activity 10% point higher than that of control. These results suggests that the addition of hazelnut makes it possible to produce cheongkukjang of excellent angiotensin converting enzyme inhibitory activity.

Effect of Enzyme Supplementation on the Performance of Growing-Finishing Pigs Fed Barley-Based Diets Supplemented with Soybean Mealor Canola Meal

  • Thacker, P.A.
    • Asian-Australasian Journal of Animal Sciences
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    • 제14권7호
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    • pp.1008-1013
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    • 2001
  • This experiment was conducted to determine the effects of enzyme supplementation on the performance of 80 growing-finishing pigs (26.2 kg) fed diets containing either soybean or canola meal. Barley-based diets formulated using either soybean meal or canola meal were fed with or without enzyme (Allzyme Vegpro, Alltech Biotechnology Centre). Eight castrates and twelve gilts were fed each diet. Digestibility of dry matter, crude protein and gross energy was 8.0 (p=0.0001), 7.9 (p=0.0005) and 7.9 (p=0.0003) percent lower for pigs fed diets containing canola meal compared with soybean meal. Enzyme supplementation had no effect on nutrient digestibility (p>0.05). There was a significant interaction between protein source and enzyme for all three nutrients. Over the entire experimental period (26.2 to 77.9 kg), pigs fed canola meal consumed 9.4% less feed (p=0.001), gained weight 20.4% slower (p=0.001) and had a 12.9% poorer feed conversion (p=0.001) than pigs fed soybean meal. Weight gain, feed intake and feed conversion were unaffected by enzyme addition (p>0.05). Castrates gained weight 11.4% faster (p=0.001), consumed 9.3% more feed (p=0.001) and had a 2.6% better feed conversion (p=0.026) than gilts. There was a significant interaction between protein source and sex of pig for feed conversion. Pigs fed diets based on canola meal had a significantly lower carcass value index (p=0.01), lower lean yield (p=0.007) and lower lean depth over the loin (p=0.001) than pigs fed diets based on soybean meal. Enzyme addition significantly increased lean depth over the loin (p=0.01). There was a significant interaction between protein source and enzyme for carcass value index (p=0.04), estimated lean yield (p=0.05) and fat depth over the loin (p=0.05). These results confirm previous studies which have demonstrated poorer pig performance when canola meal completely replaces soybean meal in diets fed to growing-finishing pigs. In addition, the results provide little justification for the inclusion of the Vegpro enzyme in diets fed to pigs of this weight range.

호알카리성 목질분해 효소를 이용한 폐지재생(제1보) -목질분해 효소의 단리 및 특성- (Recycling of Waste Paper with Alkaline Cellulolytic Enzymes(I) - Preparation and characteristics of cullulolytic enzymes-)

  • 강석현;이중명;박성배;엄태진
    • 펄프종이기술
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    • 제35권3호
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    • pp.66-73
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    • 2003
  • Alkaline cellulolytic enzymes are prepared from Coprinus cinereus 2249. Recovery method of enzyme protein from cultured medium and effect factors on enzyme activity of protein were investigated. The results could summarized as follows, \circled1 Amount of enzyme protein from cultured medium was highest in incubation with shaking and addition of skim milk. \circled2 Protein from cultured medium was alkaline enzymatic protein which shows the highest activity at pH 9.0. \circled3 The most effective recovery method of enzyme protein was the precipitation of protein by addition of cultured medium of protein in ethanol. \circled4 The enzyme activity was enhanced by tween-80 and decreased with $Al_2(SO_4)_3$, $H_2O_2$et al, and was little changed with metal ions except $Hg^{++}$.

한국산 무 Peroxidase의 열변성 및 재활성화에 미치는 요인 (Factors Affecting Thermal Inactivation and Reactivation of Korean-Radish Peroxidase)

  • 이경아;홍정민;김기남;박인식
    • 한국식품영양과학회지
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    • 제19권4호
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    • pp.301-304
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    • 1990
  • Factors affecting thermal inactivation and reactivation of korean radish peroxidase were inves-tigated,. The enzyme was stable below pH4.0 and above pH 8.0 The thermostablity of the enzyme was increased by addition of glucose sodium chloride and albuminl The inactivated enzyme by heat treatment was reactivated at room temperaturem The optimal pH for reactivation of the enzyme was pH of 9.0 The reactivation rate of the enyme was not afected by addition of glucose sodium chloride and albumin, The reactivation was completely inhibited by addition of sulfhydryl reagent such as dithiothreitol.

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Aspergillus niger SFN-416으로부터 생산한 $\beta$-Glucosidase의 정제 및 특성

  • 성찬기;이상원;박석규;박정로;문일식
    • 한국미생물·생명공학회지
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    • 제25권1호
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    • pp.44-50
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    • 1997
  • $\beta $-Glucosidase (EC 3.2.1.21) was purified from Aspergillus niger SFN-416 by a sequential process of ammonium sulfate precipitation, Sepadex G-100 and DEAE-Sephacel column chromatography. Molecular weight of the enzyme was 46, 000 daltons. The K$_{m}$ and V$_{max}$ values for PNPG were 0.67 mM and 25 moles/ml $\cdot $min., respectively. The optimum pH and temperature of the enzyme activity were 3.5 and 58$\circ $C, respectively. The enzyme activity was decreased by addition of metal ions, and increased by addition of metanol, ethanol, isopropanol and 1-butanol at a concentration of 10% (v/v). Stability of the enzyme was increased by addition of isopropanol and 1-butanol at a concentration of 10% (v/v).

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다발구멍장이버섯으로부터 분리한 혈전용해 세린분해효소의 특성 연구 (Characterization of a Fibrinolytic Serine Protease from an Edible Mushroom, Albatrellus confluens)

  • 김준호
    • 한국균학회지
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    • 제36권2호
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    • pp.183-188
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    • 2008
  • 3단계를 거처 식용 가능한 다발구멍장이버섯으로부터 분리한 혈전용해효소의 비활성은 30.49 U/mg이었으며, MALDI-TOF/MS로부터 분자량이 30086.41 Da이었다. 일차 아미노산 구조는 Glu-Thr-Val-Thr-Glu-Thr-Thr-Ala-Pro-Trp-Gly-Leu-Ser-Arg-Ile으로 밝혀졌으며, pH 8.0에서 pH 10.0의 넓은 범위에서 큰 활성을 나타내는 alkaline protease로, 최적온도는 $50^{\circ}C$이며, $30^{\circ}C$까지는 대체로 열에 안정한 효소였다. 이 효소는 합성 기질 N-Suc-Ala-Ala-Pro-Phe pNA을 강하게 분해하였으며, $Hg^{2+}$ 금속이온의 첨가로 효소 활성이 완전히 사라졌다. 효소저해제인 PMSF의 첨가로 혈전용해활성이 사라지는 결과로부터 serine 분해효소임을 알 수 있었다.