• Title/Summary/Keyword: Saprolegnia ferax

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Production and Characteristics of Cellulose from Saprolegnia ferax (미생물 셀룰로오스의 생산 및 특성에 관한 연구)

  • Kang, Jin-Ha;Park, Seong-Cheol
    • Journal of Korea Technical Association of The Pulp and Paper Industry
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    • v.39 no.3
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    • pp.77-83
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    • 2007
  • This study was carried out to examine the optimum culture condition for the production of cellulose from Saprolegnia ferax and its physical characteristics. Conclusions obtained from the results of this study were as follows: In producing the cellulose from S. ferex, optimal pH and temperature were 7.0 and $26{\sim}30^{\circ}C$ with a maximum of $26^{\circ}C$, respectively. And, optimal culture period was 11days. WHC and OHC of biocellulose were 3.2(25.04 g/g) times and 3.5(25.75 g/g) times higher than those of commercial ${\alpha}-cellulose$(7.57, 7.25 g/g) respectively. The viscosity of biocellulose is lower than that of commercial ${\alpha}-cellulose$. And the effect of rpm on the viscosity of biocellulose was more than on the that of ${\alpha}-cellulose$.

Saprolegnia ferax에 의한$\beta$-amylase의 생산 및 특성

  • Bai, Suk;Cho, Nam-Chul;Chun, Soon-Bai
    • Microbiology and Biotechnology Letters
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    • v.25 no.2
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    • pp.109-114
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    • 1997
  • The Oomycete Saprolegnia ferax produces an extracellular $\beta$-amylase, Maximum enzyme yield was attained after 7 days of growth in YNB starch medium (pH 6.5) at 25$\circ$C. The amylase was pu- rified 24-fold by ultrafitration, HPLC DEAE column and HPLC gel filtration. The purfied enzyme was a monomeric glycoprotein with a molecular weight of about 44,000 dalton. The pH and temperature optima were 6.5 and 50$\circ$C, respectively. The enzyme was fairly stable up to 50$\circ$C and at acidic pH region (pH 4.0-7.0). The apparent Km and Vmax values of the enzyme against soluble starch were 0.77 mg/ml and 2,174 $\mu$moles/mg protein, respectively. Amino acid analysis indicated that the enzyme was enriched in alanine, glycine, leucine and acidic amino acid. Starch hydrolysis with the enzyme released maltose but not glucose, whereas maltotriose, Schardinger dextrin ($\alpha$-cyclodextrin) and pullulan were not hydrolysed by the enzyme. The enzyme was inhibited by Schardinger dextrin, p-chloromercuribenzoate(PCMB), CU$^{2+}$' and Hg$^{2+}$. Inhibition of the enzyme by PCMB could be reversed by the addition of cysteine and mercaptoethanol.

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Printability Improvement of Hanji using Microbial Cellulose from Saprolegnia ferax (미생물 셀룰로오스를 이용한 한지의 인쇄적성 개선에 관한 연구)

  • Kang, Jin-Ha;Park, Seong-Cheol
    • Journal of Korea Technical Association of The Pulp and Paper Industry
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    • v.40 no.3
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    • pp.23-29
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    • 2008
  • This study was performed to improve the printability of Hanji using a microbial cellulose from Saprolegnia ferax through investigating the printability of Hanji sized with the mixture of the microbial cellulose and various kinds of sizing agents. Conclusions obtained from the results of this study were as follows. The proper concentration of a microbial cellulose in sizing a printable Hanji with it was 0.5%. In general, there was no remarkable effect but some effect on the opacity and ink density. Hanji was sized with the mixture(5:5) of microbial cellulose(0.5%) and AKD(1.0%). As a result, ink spread was remarkably improved by the girth reduction of ink spot. There was remarkable effect because the mixture(5:5) of a microbial cellulose(0.5%) and CMC(1.0%) improved not only the gloss but also the density and girth of ink spot. Mixing(7:3) with corn starch(3.0%) showed the smallest girth of ink spot among applied sizing agents. Mixing(7:3) with PVA(5.0%) also showed some effect in the density and girth of ink spot.

Regulation of Growth and Metabolic Activities of Chlorella fusca by Release Products of Some Aquatic Fungi (수생균의 분비물질에 의한 Chlorella fusca의 성장 및 대사조절)

  • Hassan, S.K.M.;Fadl-Allah, E.M.;Kobbia, I.A.;Shoulkamy, M.A.
    • The Korean Journal of Mycology
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    • v.18 no.4
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    • pp.181-190
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    • 1990
  • The growth and biochemical activities of Chlorella fusca were studied in the presence of different concentrations of either filtrates or mycelial mats of Saprolegnia ferax and Pythium graminicola. Low concentrations of both fungal filtrates exerted increase in total count, dry weight and in the biosynthesis of photosynthetic pigments, carbohydrates and nitrogen content. High concentrations showed inhibitory effect on both growth and biochemical activities of Chlorella fusca. Supplementation with different concentrations of dry mycelial mats of either fungi the culture of Chlorella showed elevation in biomass, dry weight, and biosynthesis of carbohydrates and nitrogen content especially at low concentrations. The contents of photosynthetic pigment were inhibited only at low concentrations. Neither the culture filtrate of Pythium nor Saprolegnia had cellulolytic activity, although polygalacturonase enzymes were detected, whereas chloroform-extract of both fungal filtrates showed blue spots under long wave light (366 nm).

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A Gene Encoding $\beta$-amylase from Saprolegnia parasitica and Its Expression in Saccharomyces cerevisiae

  • Kim, Hee-Ok;Park, Jeong-Nam;Shin, Dong-Jun;Lee, HwangHee Blaise;Chun, Soon-Bai;Bai, Suk
    • Journal of Microbiology and Biotechnology
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    • v.11 no.3
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    • pp.529-533
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    • 2001
  • The ${\beta}$-Amylase cDNA fragment from the oomcete Saprolegnia parasitica was cloned by reverse transcription-polymerase chain reaction (RT-PCR) using degenerate oligonucleotide primers derived from conserved ${\beta}$-amylase sequences. The 5'and 3'regions of the $\beta$-amylase gene were amplified using the rapid amplification of cDNA ends (rACE) system. It consisted of an open reading frame of 1,350 bp for a protein of 450 amino acids. Comparison between the genomic and cDNA sequences revealed that the intron was not present in the coding region. The deduced amino acid sequence of the ${\beta}$-amylase gene had a 97% similarity to the ${\beta}$-amylase of Saprolegnia ferax, followed by 41% similarity to those of Arabidopsis thaliana, Hordeum vulgare, and Zea mays. The ${\beta}$-amylase gene was also expressed in Saccharomyces cerevisiae by placing it under the control of the alcohol dehydrogenase gene (ADC1) promoter.

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