• Title/Summary/Keyword: lipases

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Preparation of Aliphatic Polyester by Lipase Catalyzed Transesterificatoin in Anhydrous Organic Solvents (유기용매에서 Lipase에 의한 지방족 폴리에스터의 합성)

  • 박현규;장호남
    • KSBB Journal
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    • v.9 no.3
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    • pp.246-252
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    • 1994
  • Enzyme-catalyzed polycondensatlon reaction of aliphatic polyesters with several repeating units was studied using the biocatalytic activities of lipases from different sources. Porcine pancreatic lipase (PPL) was found to be best in utilizing bls(2,2,2-trichloroethyl) glutarate and 1,4-butanediol as substrafes. The reaction was also catalyzed to some extent by the lipases from Humicola lanuginos and Psudomonas sp. In the series of short-chain diols(C2-C4), bis(2,2,2-trichloroethyl) glutarate was iransesterified fastest with 1,4-butanediol and for the long-chain diols (PEG-300-PEG-1000), the reaction was fastest with PEG-400. With PEGs, only monoesterification product was obtained. PPL functioned well in relatively hydrophilic organic solvents such as tetrahydrofuran(THF), ether and acetonitrile. The reaction rate was accelerated as the reaction temperature was raised from $20^{\circ}C$ to $60^{\circ}C$ while Mn values of the reaction products were not affected by the reaction temperature. End group analysis by NMR showed that Mn values of the polymer were in the range of 1500-4000 daltons.

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Lipase를 이용한 피마자유의 methanolysis

  • Yang, Jung-Seok;Jeon, Gyu-Jong;Heo, Byeong-Gi;Yang, Ji-Won
    • 한국생물공학회:학술대회논문집
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    • 2001.11a
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    • pp.621-634
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    • 2001
  • The characteristics of enzymatic methanolysis of castor oil were investigated as a clean technology. Among 16 lipases tested in this study, Novozym 435 showed the highest activity in methanolysis. Solvents had different effects on the methanolysis of castor oil according to weight percent (wt%) of Novozym 435. Heptane showed best activity with 1 wt% of Novozym 435, while isopropyl ether gave the best yield of ricinoleic acid methyl ester with 0.5 wt% of that. Ricinoleic acid methyl ester was obtained in 86% of yield through the methanolysis of castor oil catalyzed by Novozym 435 (1.0 wt%) during 24hr.

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Bacillus stearothermophilus Acetylxylan Esterase 유전자(estI)의 염기 서열 결정

  • 이정숙;최용진
    • Microbiology and Biotechnology Letters
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    • v.25 no.1
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    • pp.23-29
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    • 1997
  • The nucleotide sequence of the estI gene encoding acetylxylan esterase I of Bacillus stearothermophilus was determined and analyzed. The estI gene was found to consist of a 810 base pair open reading frame coding for a polypeptide of 270 amino acids with a deduced molecular weight of 30 kDa. This was in well agreement with the molecular weight (29 kDa) estimated by SDS-PAGE of the purified esterase. The coding sequence was preceded by a putative ribo some binding site 10 bp upsteam of the ATG codon. Further 53 bp upstream, the transcription initiation signals were identified. The putative $_{-}$10 sequence (TCCAAT) and $_{-}$35 seqence (TTGAAT) corresponded closely to the respective consensus sequences for the Bacillus subtiis major RNA polymerase. The G+C content of the coding region of the estI was 51% whereas that of the third position of codone was 60.2%. The N-terminal amino acid sequence of the EstI deduced from the nucleotide sequence perfectly matched the corresponding region of the purified esterase described previously. Comparison with the amino acid sequence of other esterases and lipases reported so far allowed us to identify a sequence, GLSMG at positions 123 to 127 of the EstI which was reported to be the highly conserved active site sequence for those enzymes. The nucleotide sequence of the estI revealed 55.7% homology to that of the xylC coding for the acetylxylan esterase of Caldocellum saccharolyticum.

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Proteomic analysis of porcine pancreas development

  • Choi, Jong-Soon;Cho, Young-Keun;Yoon, Sung-Ho;Kwon, Sang-Oh;Koo, Deog-Bon;Yu, Kweon
    • BMB Reports
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    • v.42 no.10
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    • pp.661-666
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    • 2009
  • Porcine pancreas development is not well studied at the molecular level despite being a therapeutic resource for diabetic patients. In this study, we investigated expression of lineage markers and performed proteomic analysis. Expression of the early lineage markers Pdx1 and Ptf1a was developmentally conserved between mice and pigs, whereas expression of the islet differentiation marker Pax4 was delayed in porcine compared with murine pancreas development. Proteomic analysis found that expression levels of chymotrypsinogen were down-regulated during porcine pancreas development while those of digestive enzymes like lipases, elastase and serine protease were up-regulated. In addition, specific isoforms of protein folding assistants such as protein disulfide isomerase and prefoldin were expressed at specific stages during the maturation of digestive enzymes. Taken together, these results show that development of the porcine pancreas is regulated by a concerted interplay of pancreas lineage marker proteins and other specified proteins, resulting in a functional endocrine and exocrine organ.

Morphogenetic Behavior of Tropical Marine Yeast Yarrowia lipolytica in Response to Hydrophobic Substrates

  • Zinjarde, Smita S.;Kale, Bhagyashree V.;Vishwasrao, Paresh V.;Kumar, Ameeta R.
    • Journal of Microbiology and Biotechnology
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    • v.18 no.9
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    • pp.1522-1528
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    • 2008
  • The morphogenetic behavior of a tropical marine Yarrowia lipolytica strain on hydrophobic substrates was studied. Media containing coconut oil or palm kernel oil (rich in lauric and myristic acids) prepared in distilled water or seawater at a neutral pH supported 95% of the cells to undergo a transition from the yeast form to the mycelium form. With potassium laurate, 51 % of the cells were in the mycelium form, whereas with myristate, 32% were in the mycelium form. However, combinations of these two fatty acids in proportions that are present in coconut oil or palm kernel oil enhanced the mycelium formation to 65%. The culture also produced extracellular lipases during the morphogenetic change. The yeast cells were found to attach to the large droplets of the hydrophobic substrates during the transition, while the mycelia were associated with the aqueous phase. The alkane-grown yeast partitioned more efficiently in the hydrophobic phases when compared with the coconut oil-grown mycelia. A fatty acid analysis of the mycelial form revealed the presence of lauric acid in addition to the long-chain saturated and unsaturated fatty acids observed in the yeast form. The mycelia underwent a rapid transition to the yeast form with n-dodecane, a medium-chain aliphatic hydrocarbon. Thus, the fungus displayed a differential behavior towards the two types of saturated hydrophobic substrates.

Screening and Characterization of Psychrotrophic, Lipolytic Bacteria from Deep-Sea Sediments

  • Zeng, Xiang;Xiao, Xiang;Wang, Peng;Wang, Rengping
    • Journal of Microbiology and Biotechnology
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    • v.14 no.5
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    • pp.952-958
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    • 2004
  • Of 23 psychrotrophic bacteria isolated from the west Pacific deep-sea sediments, 19 were assigned to the $\gamma$-Proteobacteria, 3 to the <$\beta$-Proteobacteria, and 1 to the Gram-positive bacteria, as determined by their 16S rDNA sequences. Ten psychrotrophs, affiliated to the Psychrobacter, Pseudoalteromonas, and Pseudomonas genera in the $\gamma$-Proteobacteria group, were screened for lipolytic bacteria. The majority of the lipolytic isolates had growth temperatures between 4-$30^\circ{C}$, and all of them were neutrophilic, aerobic, or facultatively anaerobic, and some were able to produce multiple kinds of ectohydrolytic enzymes. The deep-sea strains Psychrobacter sp. wp37 and Pseudoalteromonas sp. wp27 were chosen for further lipase production analysis. Both strains had the highest lipase production when grown at 10 to $20^\circ{C}$; their highest lipase production occurred at the late-exponential growth stage; and the majority of the enzymes were excreted to the outside of the cells. Lipases from both strains had the same optimal reaction temperature and pH (20-$30^\circ{C}$, pH 7-8) and could retain about 60% of their highest activity at $4^\circ{C}$. Furthermore, SDS-PAGE and an in-gel activity test showed that they had the same high molecular mass of about 85 kDa.

Optical Resolution of Hexanol Derivatives, Synthesis of Optically Active Systhane from Them and Its Biological Activity (Hexanol 유도체의 순수이성질체로의 분할, 이를 이용한 광학활성 시스탄의 합성 및 생물학적 활성)

  • Im, Dai-Sig;Lee, So-Ha;Cheong, Chan-Seong
    • Applied Biological Chemistry
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    • v.46 no.3
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    • pp.240-245
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    • 2003
  • $({\pm})-2-(4-Chlorophenyl)-2-cyano-2-phenyl-1-hexanol$ (2) and acetate ester (3) were resolved by various lipases. (R) and (S)-systhane were synthesized by the resolved compound 2. The antifungal screening of (R), (S)-systhane and $({\pm})-systhane$ against wheat leaf rust and barley powdery mildew gave activity over 92% in concentration of 2 ppm, but (R)- and (S)-systhane were not more active than $({\pm})-systhane$.

USE OF ENZYMES FOR MODIFICATION OF DISSOLVED AND COLLOIDAL SUBSTANCES IN PROCESS WATERS OF MECHANICAL PULPING

  • Johanna Buchert;Annikka Mustrnata;Peter Spetz;Rainer Ekman;Kari Luukko
    • Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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    • 1999.11b
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    • pp.115-119
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    • 1999
  • During mechanical pulp production and blcaching wood components, such as extractives, carbohydrates and lignin are dissolved and dispersed into the process waters. These components are called dissolved and colloidal substances(DCS). DCS can accumulate during water circulation and can in turn affect paper machine runnability and also the strength and optical properties of the paper. In this work DCS fraction origination from TMP process were treated with enzymes acting on triglycerides. glucomannans, and lignin and the effect of enzymatic treatments on the water composition as well as sheet properies were evaluated. Lipases were found to modify the chemical structure of the extractives resulting in more hydrophilic fibre surface and subsequent improvement in the sheet strength properties. Mannanase treatment, on the other hand, destabilized pitch. As a result, aggregation of pitch to the fibres was observed which in turn resulted in impaired strength properties. Laccase could effectively polymerize lignans and the reaction products seemed to be sorbed onto the fibres.

Quality of Milk and Psychrotophic Bacteria (우유의 품질과 저온성균)

  • Chung, Chung-Il
    • Journal of Dairy Science and Biotechnology
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    • v.18 no.1
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    • pp.38-46
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    • 2000
  • Since generalization of cold storage of raw and processed milk, psychrotrophic bacteria has become more important. The number present in raw milk is related to sanitary conditions during pro-duction and to length and temperature of storage before pasteurization. Growth of psychrotrophs In raw milk often reduces the quality of pasteurized products. Recently, some pathogenic bacteria like Listeria monocytogenes, Yersinia enterocolitica, Bacillus cereus are reported to grow at low temperature and cause food poisoning. The presence of gram positive psychrotrophic bacteria which can survive pasteurization can limit the shelf life of pasteurized milk during extended storage and the survival of heat stable proteases and lipases produced by gram negative psychrotrophic bacteria often brings about proteolytic damage to milk protein in the products. Therefore, in order to prevent the deteorioration of milk and milk products by the growth of psychrotrophs, it is necessary to cool down the temperature of raw milk as soon as possible after milking and to keep the temperature below 5t during storage at farm. As psychrotrophic bacteria become readily predominant in raw milk under refregeration, it can be considered to change the traditional incubating temperature for SPC from 30${\sim}$32$^{\circ}C$ to 25${\sim}$27$^{\circ}C$ at which the psychrotrophs prefer to grow. The psychrotrophic bacterial count(PBC) is of limited use in dairy industry, because of the 10 days incubation period. Although estimates of psychrotrophic bacteria may provide an acceptable shelf-life prediction, there is no single, generally acceptable rapid method for replacing the PBC at the moment. Consequently, faster method for esmating psychrotrophic bacteria has to be developed.

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Thermal Inactivation of Lipase from Geotrichum candidum (Geotrichum candidum Lipase의 열불활성(熱不活性)에 관(關)하여)

  • Park, K.H.
    • Applied Biological Chemistry
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    • v.20 no.1
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    • pp.101-104
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    • 1977
  • Lipase from Geotrichum candidum was heat inactivated in 0.1M phosphate buffer solution. The thermal inactivation followed first order kinetics for the range of temperatures $50^{\circ}-80^{\circ}C$ except at $50^{\circ}C$. The changes in enthalpy, entropy and Gibbs free energy at $60^{\circ}C$ were 120.4 kJ/mol, 73.0 J/mol K and 96.9 kJ/mol respectively a value of $19^{\circ}C$(Geotrichum candidum lipase) is greater than that of lipases from milk and pancreas. The effect of detergents, lecithin and linoleic acid or the thermal inactivation of lipase was found to be negligible.

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