• 제목/요약/키워드: bio-enzyme

검색결과 706건 처리시간 0.027초

바이오효소(bio-enzyme)의 엽면시비가 오이, 고추 유묘의 생장에 미치는 영향 (Effects of Foliar Application of Bio-enzyme on the Seedlings Growth of Cucumber and Red Pepper)

  • 김홍기;서범석;정순주
    • 한국유기농업학회지
    • /
    • 제5권2호
    • /
    • pp.141-152
    • /
    • 1997
  • This experiment was conducted to know the effects of foliar applicated bio-enzyme on the early growth of cucumber and red pepper seedlings. Bio-enzyme was manufactured by the culture and proliferation of Bacillus genus and foliar applicated by the concentration of 0.075, 0.15, 0.3 g.$\ell$-1. Foliar application of bio-enzyme had great influenced to the early growth both cucumber and red pepper seedlings. Optimum concentrations of bio-enzyme applicated for the growth of plant height were determined as of 0.075 g.$\ell$-1 in cucumber but in red pepper seedlings 0.15g.$\ell$-1 was more favored. However, foliar application of 0.15g.$\ell$-1 of bio-enzyme was recommended for both cucumber and red pepper seedlings. Especially, leaf area and total dry weight which are main indices of good seedling were highest in the plot of standard concentrations(0.15g.$\ell$-1)of bio-enzyme.

  • PDF

Crystal Structure of (S)-3-Hydroxybutyryl-CoA Dehydrogenase from Clostridium butyricum and Its Mutations that Enhance Reaction Kinetics

  • Kim, Eun-Jung;Kim, Jieun;Ahn, Jae-Woo;Kim, Yeo-Jin;Chang, Jeong Ho;Kim, Kyung-Jin
    • Journal of Microbiology and Biotechnology
    • /
    • 제24권12호
    • /
    • pp.1636-1643
    • /
    • 2014
  • 3-Hydroxybutyryl-CoA dehydrogenase is an enzyme that catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA, in which acetoacetyl-CoA is reduced to 3-hydroxybutyryl-CoA. To understand the molecular mechanisms of n-butanol biosynthesis, we determined the crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Clostridium butyricum (CbHBD). The monomer structure of CbHBD exhibits a two-domain topology, with N- and C-terminal domains, and the dimerization of the enzyme was mostly constituted at the C-terminal domain. The mode of cofactor binding to CbHBD was elucidated by determining the crystal structure of the enzyme in complex with $NAD^+$. We also determined the enzyme's structure in complex with its acetoacetyl-CoA substrate, revealing that the adenosine diphosphate moiety was not highly stabilized compared with the remainder of the acetoacetyl-CoA molecule. Using this structural information, we performed a series of site-directed mutagenesis experiments on the enzyme, such as changing residues located near the substrate-binding site, and finally developed a highly efficient CbHBD K50A/K54A/L232Y triple mutant enzyme that exhibited approximately 5-fold higher enzyme activity than did the wild type. The increased enzyme activity of the mutant was confirmed by enzyme kinetic measurements. The highly efficient mutant enzyme should be useful for increasing the production rate of n-butanol.

Bacillus pseudomycoides로 부터 분리된 alanine racemase 유전자의 발현 및 생화학 특성 (Biochemical Characteristics of a Bacteria (Bacillus pseudomycoides) Alanine Racemase Expressed in Escherichia coli)

  • 강한철;김나현;정유정;윤상홍;이창묵
    • Journal of Applied Biological Chemistry
    • /
    • 제53권3호
    • /
    • pp.132-138
    • /
    • 2010
  • B. pseudomycoides로 부터 alanine racemase로 추정되는 유전자를 분리한 다음 6xHistidine 이 결합된 pET-21 운반체를 이용하여 E. coli BL21(DE3)에서 발현시키고 생화학 특성을 조사하였다. 재조합된 alanine racemase는 affinity chromatography를 이용하여 분리하였으며 SDS-PAGE 분석에서 약 46 kDa의 단일밴드를 나타내었다. 분리된 효소는 여러 아미노산 중에서 L-alanine에 대하여 가장 높은 활성도를 보이고 D-alanine에 대하여 두번째로 높은 활성도를 보였다. 따라서 분리된 효소는 alanine racemase로 판단되었다. 분리된 효소는 D-cysteine에 하여 상당히 저해가 되었다. 효소의 최적 활성도는 pH 9.0 근처에서 관찰되었고 산성의 조건보다는 알칼리의 조건에서 보다 안정하였다. 보효소인 PLP 0.3mM의 첨가에 의해 효소의 활성도는 약 70% 가량 증대되었다.

Effects of Supplementing Different Levels of a Commercial Enzyme Complex on Performance, Nutrient Availability, Enzyme Activity and Gut Morphology of Broilers

  • Yuan, Jiu;Yao, Junhu;Yang, Fengxia;Yang, Xiaodan;Wan, Xinjie;Han, Jincheng;Wang, Yaojie;Chen, Xinke;Liu, Yurui;Zhou, Zhenfeng;Zhou, Ningbo;Feng, Xinyu
    • Asian-Australasian Journal of Animal Sciences
    • /
    • 제21권5호
    • /
    • pp.692-700
    • /
    • 2008
  • A trial was conducted to study the influence of different levels of a commercial enzyme complex on performance, nutrient availability, blood parameters, digestive tract measurements, amylase and trypsin activity of the digestive tract and gut morphology in broilers fed the typical diets in north China. There were four treatments: the control diet and the other three enzyme complex supplemented diets which were 180 mg/kg, 360 mg/kg and 720 mg/kg enzyme complex supplemented to the control diet, respectively. The birds fed the diets supplemented with 180 mg/kg and 360 mg/kg enzyme complex had better performance and nutrient availability, the activities of amylase and trypsin in the digestive tract in the two treatments were improved, the villus height and surface area of villus in the small intestine increased and the crypt depth and epithelial thickness of small intestine decreased. Relative weights of pancreas and relative weights and lengths of small intestine decreased. However, the addition of 720 mg/kg enzyme complex had no effects on these parameters and increased crypt depth and epithelial thickness of the small intestine. The data suggested that suitable supplementation of enzyme complex was beneficial for the birds, while excess enzyme complex inhibited secretion of endogenous enzyme and destroyed the structure of the small intestine.

Isolation and Characterization of a Novel Bacterium Burkholderia gladioli Bsp-1 Producing Alkaline Lipase

  • Zhu, Jing;Liu, Yanjing;Yanqin, Yanqin;Pan, Lixia;Li, Yi;Liang, Ge;Wang, Qingyan
    • Journal of Microbiology and Biotechnology
    • /
    • 제29권7호
    • /
    • pp.1043-1052
    • /
    • 2019
  • Active lipase-producing bacterium Burkholderia gladioli Bps-1 was rapidly isolated using a modified trypan blue and tetracycline, ampicillin plate. The electro-phoretically pure enzyme was obtained by purification using ethanol precipitation, ion-exchange chromatography, and gel filtration chromatography. The molecular weight was 34.6 kDa and the specific activity was determined to be 443.9 U/mg. The purified lipase showed the highest activity after hydrolysis with $p-NPC_{16}$ at a pH of 8.5 and $50^{\circ}C$, and the $K_m$, $k_{cat}$, and $k_{cat}/K_m$ values were 1.05 mM, $292.95s^{-1}$ and $279s^{-1}mM^{-1}$, respectively. The lipase was highly stable at $7.5{\leq}pH{\leq}10.0$. $K^+$ and $Na^+$ exerted activation effects on the lipase which had favorable tolerance to short-chain alcohols with its residual enzyme activity being 110% after being maintained in 30% ethanol for 1 h. The results demonstrated that the lipase produced by the strain B. gladioli Bps-1 has high enzyme activity and is an alkaline lipase. The lipase has promising chemical properties for a range of applications in the food-processing and detergent industries, and has particularly high potential for use in the manufacture of biodiesel.

Pretreatment and enzymatic saccharification process of rapeseed straw for production of bioethanol

  • Lee, Heon-Hak;Jeon, Min-Ki;Yoon, Min-Ho
    • 농업과학연구
    • /
    • 제43권4호
    • /
    • pp.641-649
    • /
    • 2016
  • This study was conducted to evaluate the yield of bio-ethanol produced by separate hydrolysis and fermentation (SHF) with the pretreated rapeseed straw (RS) using crude enzyme of Cellulomonas flavigena and Saccharomyces cereviase. Crude enzyme of C. flavigena showed enzymatic activity of 14.02 U/mL for CMC 133.40 U/mL, for xylan 15.21 U/mL, for locust gum and 15.73 U/mL for rapeseed straw at pH 5.0 and $40^{\circ}C$, respectively. The hemicellulose contents of RS was estimated to compromise 36.62% of glucan, 43.20% of XMG (xylan + mannan + galactan), and 2.73% of arabinan by HPLC analysis. The recovering ratio of rapeseed straw were investigated to remain only glucan 75.2% after 1% $H_2SO_4$ pretreatment, glucan 45.44% and XMG 32.13% after NaOH, glucan 44.75% and XMG 5.47% after $NH_4OH$, and glucan 41.29% and XMG 41.04% after hot water. Glucan in the pretreatments of RS was saccharified to glucose of 45.42 - 64.81% by crude enzyme of C. flavigena while XMG was made into to xylose + mannose + galactose of 58.46 - 78.59%. Moreover, about 52.88 - 58.06 % of bio-ethanol were obtained from four kinds of saccharified solutions by SHF using S. cerevisiae. Furthermore, NaOH pretreatment was determined to show the highest mass balance, in which 21.22 g of bio-ethanol was produced from 100 g of RS. Conclusively, the utilization of NaOH pretreatment and crude enzyme of Cellulomonas flavigena was estimated to be the best efficient saccharification process for the production of bio-ethanol with rapeseed straw by SHF.

면사의 효소가공 및 실켓 가공 (Bio-polishing and Silket Treatment of Cotton Yarns)

  • 배영환;이지완;손영아;김주혜;권미연;김의화;이승구
    • 한국염색가공학회지
    • /
    • 제20권4호
    • /
    • pp.15-20
    • /
    • 2008
  • The cotton yarn was subjected to bio-polishing treatment with three commercial enzymes(Cellusoft L, Denimax-991L and Denimax-acid) to remove the fuzz on the cotton yarn. Also, enzyme treated cotton yarns were compared with singeing cotton yarns. Experimental variables of enzyme treated cotton yarn were as follow: concentration of enzyme solution and NaOH, dipping time, and processing temperature. The enzymatic treatments were evaluated by analyzing the effect on yarn count, twist contraction, evenness and tenacity. As the results, enzymatic treatment on cotton yarn induced same effects as the traditional singeing treatment. Also, silket treatment of cotton yarn after bio-polishing enhanced the tensile properties of the cotton yarn.

Computational identification of significantly regulated metabolic reactions by integration of data on enzyme activity and gene expression

  • Nam, Ho-Jung;Ryu, Tae-Woo;Lee, Ki-Young;Kim, Sang-Woo;Lee, Do-Heon
    • BMB Reports
    • /
    • 제41권8호
    • /
    • pp.609-614
    • /
    • 2008
  • The concentrations and catalytic activities of enzymes control metabolic rates. Previous studies have focused on enzyme concentrations because there are no genome-wide techniques used for the measurement of enzyme activity. We propose a method for evaluating the significance of enzyme activity by integrating metabolic network topologies and genome-wide microarray gene expression profiles. We quantified the enzymatic activity of reactions and report the 388 significant reactions in five perturbation datasets. For the 388 enzymatic reactions, we identified 70 that were significantly regulated (P-value < 0.001). Thirty-one of these reactions were part of anaerobic metabolism, 23 were part of low-pH aerobic metabolism, 8 were part of high-pH anaerobic metabolism, 3 were part of low-pH aerobic reactions, and 5 were part of high-pH anaerobic metabolism.

Production of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Malassezia pachydermatis G-14

  • Jeong, Seung-Chan;Kim, Jae-Ho;Kim, Na-Mi;Lee, Jong-Soo
    • Mycobiology
    • /
    • 제33권3호
    • /
    • pp.142-146
    • /
    • 2005
  • To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.