• Title/Summary/Keyword: ${\beta}$-glucosidase

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Characteristics of Korean Alcoholic Beverages Produced by Using Rice Nuruks Containing Aspergillus oryzae N159-1

  • Kim, Hye Ryun;Lee, Ae Ran;Kim, Jae-Ho
    • Mycobiology
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    • v.45 no.2
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    • pp.119-122
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    • 2017
  • Herein, nuruks derived from non-glutinous and glutinous rice inoculated with Aspergillus oryzae N159-1 (having high alpha-amylase and beta-glucosidase activities) were used to produce Korean alcoholic beverages. The resultant beverages had enhanced fruity (ethyl caproate and isoamyl alcohol) and rose (2-phenethyl acetate and phenethyl alcohol) flavors and high taste scores.

Intergeneric protoplast fusion between Bacillus pumilus and Cellulomonas fimi

  • Kim, D.M.;Lee, K.H.
    • Proceedings of the Korean Society for Applied Microbiology Conference
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    • 1986.12a
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    • pp.528.1-528
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    • 1986
  • Cellulose utilising hybrids between Cellulomonas fimi and Bacillus pumilus were isolated after PEG mediated protoplast fusion. 33% (w/v) PEG #6, 000 and 50mM $Ca^{++}$were optimum concentration. The intergeneric fusion frequency was 3.2$\times$10$^{-7}$ xtracellular CMCase and $\beta$-glucosidase activities were detected from one hydrid unlike only CMCase was detected from Cellulomonas fimi.

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Purification and Characterization of $\beta$-Glucosidase and $\alpha$-Arabinofuranosidase Metabolizing Ginsenoside Rc from Bifidobacterium K-103

  • Park, Sun-Young;Kim, Dong-Hyun
    • Proceedings of the PSK Conference
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    • 2003.04a
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    • pp.224.2-225
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    • 2003
  • Ginsenoside, major components of ginseng have been reported to show various biological activities including an increase of cholesterol metabolism. stimulation of serum protein synthesis, immunomodulatory effects. To explain these pharmacological actions, it is thought that ginseng saponins should be metabolized by human intestinal bacteria after they are orally administered. (omitted)

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Exprission of cellulomonas biazotea cellobiase gene in E. coli (Cellulomonas biazotea cellobiase gene의 대장균에의 형질발현)

  • 박영길;연창석;최영길
    • Korean Journal of Microbiology
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    • v.26 no.1
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    • pp.6-12
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    • 1988
  • Cellobiase ($\beta$-glucosidase) is an enzyme of the cellulase system in cellulolytic microor-ganisms. The chromosomal DNA fragment which include cellobiase gene of Cellulomonas biazotea was cloned in Eschericia coli via plasmid pBR 322 vector. Restriction enzyme Sal I was used to obtain adequate size of fragments from C. biazotea. chromosomal DNA. The transformant of E. coli HB101 with recombinant plasmid pBG101 showed cellobiase activity, which is not ordinary in E. coli HB101. The enzyme activity of the transformant was as of 20% lower than that of C. biazotea.

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Characterization of Cellulases from Schizophyllum commune for Hydrolysis of Cellulosic Biomass (Schizophyllum commune에 의한 Cellulase 생산 및 섬유소계 바이오매스의 당화를 위한 효소적 특성)

  • Kim, Hyun-Jung;Kim, Yoon-Hee;Cho, Moon-Jung;Shin, Keum;Lee, Dong-Heub;Kim, Tae-Jong;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • v.38 no.6
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    • pp.547-560
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    • 2010
  • The optimum culture condition of Schizophyllum commune for the cellulase production and its enzymatic characteristics for saccharification of cellulosic biomass were analyzed. S. commune secrets ${\beta}$-1,4-xylosidase (BXL) and cellulases, including endo-${\beta}$-1,4-glucanase (EG), cellobiohydrolase (CBH), and ${\beta}$-glucosidase (BGL). The optimum reaction temperature for all cellulases was $50^{\circ}C$ and the thermostable range was $30{\sim}40^{\circ}C$C. The optimum reaction pH for all cellulases was 5.5 in a range of temperature from $0^{\circ}C$ to $55^{\circ}C$. The best nutritions for the cellulase production of S. commune among tested nutrients were 2% cellulose for the carbon source and corn steep liquor or peptone/yeast extract for the nitrogen source without vitamins. The environmental culture condition for the cellulase production was 5.5~6.0 for pH at $25{\sim}30^{\circ}C$. The enzyme activities of EG, BGL, CBH, and BXL were 3670.5, 631.9, 398.5, and 15.2 U/$m{\ell}$, respectively, after concentration forty times from the culture broth of S. commune which was grown at the optimized culture condition. Alternative filter paper unit assay showed 11 FPU/$m{\ell}$ enzyme activity. The saccharification tests using cellulase of S. commune showed the low saccharification rate on tested hardwoods but a high value of 50.5% on cellulose, respectively. The saccharification rate (50.5%) of cellulose by cellulase produced in this work is higher than 45.7% in the commercial enzyme (Celluclast 1.5L, 30 FPU/g, glucan).