Production of levan using recombinant levansucrase immobilized on hydroxyapatite

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dc.contributor.authorKi Hyo Jang-
dc.contributor.authorKi Bang Song-
dc.contributor.authorJ S Kim-
dc.contributor.authorChul Ho Kim-
dc.contributor.authorBong Hyun Chung-
dc.contributor.authorSang Ki Rhee-
dc.date.accessioned2017-04-19T08:57:12Z-
dc.date.available2017-04-19T08:57:12Z-
dc.date.issued2000-
dc.identifier.issn0178-515X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5148-
dc.description.abstractLevansucrase of Zymomonas mobilis was immobilized onto the surface of hydroxyapatite by ionic binding. Optimum conditions for the immobilization were: pH 6.0, 4 h of immobilization reaction time, and 20 U of enzyme/g of matrix. The enzymatic and biochemical properties of the immobilized enzyme were similar to those of the native enzyme, especially towards the effect of salts and detergents. The immobilized enzyme showed sucrose hydrolysis activity higher as that of the native enzyme, but levan formation activity was 70% of the native enzyme. HPLC analysis of levan produced by immobilized enzyme showed the presence of two different types of levan: high-molecular-weight levan and low-molecular-weight levan. The proportion of low-molecular-weight levan to total levan produced by the immobilized enzyme was much higher than that with the native enzyme, indicating that immobilized levansucrase could be applied to produce low-molecular-weight levan. Immobilized levansucrase retained 65% of the original activity after 6 times of repeated uses and 67% of the initial activity after 40 d when stored at 4°C.-
dc.publisherSpringer-
dc.titleProduction of levan using recombinant levansucrase immobilized on hydroxyapatite-
dc.title.alternativeProduction of levan using recombinant levansucrase immobilized on hydroxyapatite-
dc.typeArticle-
dc.citation.titleBioprocess Engineering-
dc.citation.number1-
dc.citation.endPage93-
dc.citation.startPage89-
dc.citation.volume23-
dc.contributor.affiliatedAuthorKi Bang Song-
dc.contributor.affiliatedAuthorChul Ho Kim-
dc.contributor.affiliatedAuthorBong Hyun Chung-
dc.contributor.affiliatedAuthorSang Ki Rhee-
dc.contributor.alternativeName장기효-
dc.contributor.alternativeName송기방-
dc.contributor.alternativeName김종수-
dc.contributor.alternativeName김철호-
dc.contributor.alternativeName정봉현-
dc.contributor.alternativeName이상기-
dc.identifier.bibliographicCitationBioprocess Engineering, vol. 23, no. 1, pp. 89-93-
dc.identifier.doi10.1007/s004499900153-
dc.subject.keywordhydroxyapatite-
dc.subject.keywordlevan-
dc.subject.keywordlevansucrase-
dc.subject.keywordrecombinant enzyme-
dc.subject.localhydroxyapatite-
dc.subject.localLevan-
dc.subject.locallevan-
dc.subject.localLevansucrase-
dc.subject.locallevansucrase-
dc.subject.localRecombinant enzyme-
dc.subject.localrecombinant enzyme-
dc.description.journalClassY-
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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