• Title/Summary/Keyword: agarase

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Erratum to: Identification of a New Agar-hydrolyzing Bacterium Vibrio sp. S4 from the Seawater of Jeju Island and the Biochemical Characterization of Thermostable Agarose (Erratum to: 제주도 연안 해양에서 분리한 한천분해 미생물 Vibrio sp. S4의 동정 및 내열성 agarase의 생화학적 특성)

Purification and Characterization of Neoagarotetraose from Hydrolyzed Agar

  • Jang, Min-Kyung;Lee, Dong-Guen;Kim, Nam-Young;Yu, Ki-Hwan;Jang, Hye-Ji;Lee, Seung-Woo;Jang, Hyo-Jung;Lee, Ye-Ji;Lee, Sang-Hyeon
    • Journal of Microbiology and Biotechnology
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    • v.19 no.10
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    • pp.1197-1200
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    • 2009
  • The whitening effect, tyrosinase inhibition, and cytotoxicity of neoagarotetraose were measured after its purification from hydrolyzed agar by gel filtration chromatography. In melanoma B16F10 cells, the melanin content of neoagarotetraose-treated cells was the same as that treated by kojic acid or arbutin. In addition, tyrosinase of melanoma cells was strongly inhibited by neoagarotetraose at a concentration of $1{\mu}g/ml$ and similarly inhibited at 10 and $100{\mu}g/ml$ compared with those by arbutin or kojic acid. The activity of mushroom tyrosinase showed a 38% inhibition by neoagarotetraose at $1{\mu}g/ml$, and this inhibitory effect was more efficient than that by kojic acid. Neoagarotetraose revealed a similar $IC_{50}$ (50% inhibition concentration) value for mushroom tyrosinase as that by kojic acid. These data suggest that the neoagarotetraose generated from agar by recombinant $\beta$-agarase might be a good candidate as a cosmetic additive for the whitening effect.

Chemical Composition and Rheological Properties of Enzymatic Hydrolysate of Porphyran Isolated from Pyropia yezoensis (김(Pyropia yezoensis)에서 분리한 포피란 효소가수분해물의 화학적 및 유동 특성)

  • In, Seo-Kyoung;Koo, Jae-Geun
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.48 no.1
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    • pp.58-63
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    • 2015
  • The chemical and rheological properties of natural and enzymatically hydrolyzed porphyran isolated from Pyropia yezoensis were investigated. The enzymatic hydrolysate was prepared by hydrolysis of porphyran using ${\beta}$-agarase followed by fractionation based on molecular weight (>300 kDa (Fr-1), 100-300 kDa (Fr-2), 10-100 kDa (Fr-3) and 1-10 kDa (Fr-4) using an ultrafiltration membrane. Each hydrolysate fraction consisted mainly of galactose (42.7-57.5%), 3,6-anhydro galactose (6.5-15.1%) and ester sulfate (8.6-14.1%). The sulfate content of the enzymatically hydrolyzed fractions decreased with an increase in molecular weight, whereas the 3,6-anhydro galactose content increased significantly. The rheological behavior of porphyran and enzymatically hydrolyzed porphyran solutions demonstrated a pseudoplastic behavior, which agrees with the Herschel-Bulkley model. The effect of temperature on the viscosity of the porphyrans and hydolysate fractions were measured and modeled using the Arrhenius equation. The activation energy of the porphyrans and enzymatically hydrolyzed porphyran (Fr-1) increased from 12.30 to 20.29 kJ/mol and 9.06 to 23.84 kJ/mol, respectively with increasing concentrations from 3% to 7%. These data indicate that the extent of the apparent viscosity of porphyran and enzymatically hydrolyzed porphyran are influenced by both temperature and concentration.

Complete genome sequence of Microbulbifer agarilyticus GP101 possessing genes coding for diverse polysaccharide-degrading enzymes (다양한 다당류를 분해하는 세균 Microbulbifer agarilyticus GP101의 완전한 유전체 서열)

  • Jung, Jaejoon;Bae, Seung Seob;Chung, Dawoon;Baek, Kyunghwa
    • Korean Journal of Microbiology
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    • v.54 no.3
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    • pp.299-301
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    • 2018
  • Microbulbifer agarilyticus GP101 was isolated from the gut of a marine invertebrate Turbo cornutus and capable of degrading polysaccharide such as agar, alginate, and ${\kappa}$-carrageenan constituting algal cell wall. To obtain genomic basis of polysaccharide-degrading activity, we sequenced genome of strain GP101. The genome consists of 4,255,625 bp, 3,458 coding sequences with 55.4% G + C contents. BLASTP search revealed the presence of seven agarases, five alginate lyases, ten glucanases, four chitinases, two xylanases, one ${\kappa}$-carrageenase, and one laminarinase. The genomic data of strain GP101 will provide potential uses in the bioconversion process of diverse polysaccharide into bioenergy and biochemicals.

Production of Ethanol from Agarose by Unified Enzymatic Saccharification and Fermentation in Recombinant Yeast

  • Lee, Ji-Soo;Hong, Soon-Kwang;Lee, Chang-Ro;Nam, Soo-Wan;Jeon, Sung-Jong;Kim, Yeon-Hee
    • Journal of Microbiology and Biotechnology
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    • v.29 no.4
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    • pp.625-632
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    • 2019
  • The unified saccharification and fermentation (USF) system was developed for direct production of ethanol from agarose. This system contains an enzymatic saccharification process that uses three types of agarases and a fermentation process by recombinant yeast. The $pGMF{\alpha}-HGN$ plasmid harboring AGAH71 and AGAG1 genes encoding ${\beta}-agarase$ and the NABH558 gene encoding neoagarobiose hydrolase was constructed and transformed into the Saccharomyces cerevisiae 2805 strain. Three secretory agarases were produced by introducing an S. cerevisiae signal sequence, and they efficiently degraded agarose to galactose, 3,6-anhydro-L-galactose (AHG), neoagarobiose, and neoagarohexose. To directly produce ethanol from agarose, the S. cerevisiae $2805/pGMF{\alpha}-HGN$ strain was cultivated into YP-containing agarose medium at $40^{\circ}C$ for 48 h (for saccharification) and then $30^{\circ}C$ for 72 h (for fermentation). During the united cultivation process for 120 h, a maximum of 1.97 g/l ethanol from 10 g/l agarose was produced. This is the first report on a single process containing enzymatic saccharification and fermentation for direct production of ethanol without chemical liquefaction (pretreatment) of agarose.