KOPRI Repository

Characterization of cold-active β-N-acetylglucosaminidase from Arctic bacterium Pseudoalteromonas issachenkonii KOPRI 22718

Metadata Downloads
Title
Characterization of cold-active β-N-acetylglucosaminidase from Arctic bacterium Pseudoalteromonas issachenkonii KOPRI 22718
Other Titles
북극 해양세균 Pseudoalteromonas issachenkonii KOPRI 22718이 생산하는 베타-N-acetylglucosaminidase 특성연구
Authors
Park, Ha Ju
Lee, Hong Kum
Kim, Dockyu
Yim, Joung Han
Kim, Sung Jin
Kim, Il-Chan
Keywords
Arctic; cold-active; endochitinase; psychrotolerant; β-N-acetylglucosaminidase
Issue Date
2010
Citation
Park, Ha Ju, et al. 2010. Characterization of cold-active β-N-acetylglucosaminidase from Arctic bacterium Pseudoalteromonas issachenkonii KOPRI 22718. 극지연구소. 극지연구소. 2010.05.26~.
Abstract
One hundred thirty-six marine bacteria showing chitinolytic activity were isolated from 47 sediment samples of the Kara Sea, Arctic. Among them, a psychrotolerant strain (KOPRI 22718) was selected for its high exo-acting chitinase activity. The 16S rRNA sequence identifies KOPRI 22718 as Pseudoalteromonas issachenkonii. An exo-acting chitinase was homogeneously purified from the culture supernatant of KOPRI 22718 through ion exchange and gel filtration chromatography, and the molecular weight of purified chitinase was estimated to be approximately 112 kDa. Due to its β-N-acetylglucosaminidase activity, W-Chi22718 was able to produce N-acetyl-D-glucosamine monomers from chitin oligosaccharide substrates. W-Chi22718 displayed chitinase activity from 0-37°C (optimal temperature of 30°C), and maintained activity from pH 6.0-9.0 (optimal pH of 7.6). Interestingly, W-Chi22718 exhibited a relative activity of 13 and 35% of maximal activity at 0 and 10°C, respectively, which is comparable to the activities of previously characterized, cold-adapted, bacterial chitinases. W-Chi22718 activity was enhanced by K+, Ca2+, and Fe2+, but completely inhibited by Cu2+and SDS. We found that W-Chi22718 can produce much more N-acetyl-D-glucosamines from colloidal chitin, working together with, previously characterized, cold-active endochitinase W-Chi21702.
URI
http://repository.kopri.re.kr/handle/201206/8073
Conference Name
극지연구소
Conference Place
극지연구소
Conference Date
2010.05.26~
Files in This Item
There are no files associated with this item.
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    qrcode

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

    Browse