Levan fructotransferase from Arthrobacter oxydans J17-21 catalyzes the formation of the Di-D-fructose dianhydride IV from levan

Ki Hyo Jang; Eun Ja Ryu; Buem seek Park; Ki bang Song; Soon Ah Kang; Chul Ho Kim; Tai Boong Uhm; Yong Il Park; Sang ki Rhee

doi:10.1021/jf026207o

Levan fructotransferase from Arthrobacter oxydans J17-21 catalyzes the formation of the Di-D-fructose dianhydride IV from levan

Ki Hyo Jang, Eun Ja Ryu, Buem seek Park, Ki bang Song, Soon Ah Kang, Chul Ho Kim, Tai Boong Uhm, Yong Il Park, Sang ki Rhee

Department of Medical and Biological Sciences

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

A new levan fructotransferase (LFTase) isolated from Arthrobacter oxydans J17-21 was characterized for the production of difructose dianhydride IV (DFA IV). LFTase was purified to apparent homogeneity by Q-Sepharose ion exchange chromatography, Mono-Q HR 5/5 column chromatography, and gel permeation chromatography. The enzyme had an apparent molecular mass of 54000 Da. The optimum pH for the enzyme-catalyzed reaction was pH 6.5, and the optimum temperature was observed at 45 °C. The LFTase was activated by the presence of CaCl₂ and EDTA-2Na but inhibited strongly by MnCl₂ and CuSO₄ at 1 mM and completely by FeSO₄ and Ag₂SO₄ at 1 mM. A bacterial levan from Zymomonas mobilis was incubated with an LFTase; final conversion yield from the levan to DFA IV was 35%. Neither inulin, levanbiose, sucrose, dextran, nor starch was hydrolyzed by LFTase. DFA IV was very stable at acidic pH and high temperature, thus indicating that DFA IV may be suitable for the food industry and related areas.

Original language	English
Pages (from-to)	2632-2636
Number of pages	5
Journal	Journal of Agricultural and Food Chemistry
Volume	51
Issue number	9
DOIs	https://doi.org/10.1021/jf026207o
State	Published - 23 Apr 2003

Keywords

Arthrobacter oxydans
DFA IV
Levan fructotransferase
Levan-hydrolyzing enzyme

Access to Document

10.1021/jf026207o

Cite this

@article{251551500e8948d4a7faf4ee1e3f3e5a,

title = "Levan fructotransferase from Arthrobacter oxydans J17-21 catalyzes the formation of the Di-D-fructose dianhydride IV from levan",

abstract = "A new levan fructotransferase (LFTase) isolated from Arthrobacter oxydans J17-21 was characterized for the production of difructose dianhydride IV (DFA IV). LFTase was purified to apparent homogeneity by Q-Sepharose ion exchange chromatography, Mono-Q HR 5/5 column chromatography, and gel permeation chromatography. The enzyme had an apparent molecular mass of 54000 Da. The optimum pH for the enzyme-catalyzed reaction was pH 6.5, and the optimum temperature was observed at 45 °C. The LFTase was activated by the presence of CaCl2 and EDTA-2Na but inhibited strongly by MnCl2 and CuSO4 at 1 mM and completely by FeSO4 and Ag2SO4 at 1 mM. A bacterial levan from Zymomonas mobilis was incubated with an LFTase; final conversion yield from the levan to DFA IV was 35%. Neither inulin, levanbiose, sucrose, dextran, nor starch was hydrolyzed by LFTase. DFA IV was very stable at acidic pH and high temperature, thus indicating that DFA IV may be suitable for the food industry and related areas.",

keywords = "Arthrobacter oxydans, DFA IV, Levan fructotransferase, Levan-hydrolyzing enzyme",

author = "Jang, {Ki Hyo} and Ryu, {Eun Ja} and Park, {Buem seek} and Song, {Ki bang} and Kang, {Soon Ah} and Kim, {Chul Ho} and Uhm, {Tai Boong} and Park, {Yong Il} and Rhee, {Sang ki}",

year = "2003",

month = apr,

day = "23",

doi = "10.1021/jf026207o",

language = "English",

volume = "51",

pages = "2632--2636",

journal = "Journal of Agricultural and Food Chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

number = "9",

}

TY - JOUR

T1 - Levan fructotransferase from Arthrobacter oxydans J17-21 catalyzes the formation of the Di-D-fructose dianhydride IV from levan

AU - Jang, Ki Hyo

AU - Ryu, Eun Ja

AU - Park, Buem seek

AU - Song, Ki bang

AU - Kang, Soon Ah

AU - Kim, Chul Ho

AU - Uhm, Tai Boong

AU - Park, Yong Il

AU - Rhee, Sang ki

PY - 2003/4/23

Y1 - 2003/4/23

N2 - A new levan fructotransferase (LFTase) isolated from Arthrobacter oxydans J17-21 was characterized for the production of difructose dianhydride IV (DFA IV). LFTase was purified to apparent homogeneity by Q-Sepharose ion exchange chromatography, Mono-Q HR 5/5 column chromatography, and gel permeation chromatography. The enzyme had an apparent molecular mass of 54000 Da. The optimum pH for the enzyme-catalyzed reaction was pH 6.5, and the optimum temperature was observed at 45 °C. The LFTase was activated by the presence of CaCl2 and EDTA-2Na but inhibited strongly by MnCl2 and CuSO4 at 1 mM and completely by FeSO4 and Ag2SO4 at 1 mM. A bacterial levan from Zymomonas mobilis was incubated with an LFTase; final conversion yield from the levan to DFA IV was 35%. Neither inulin, levanbiose, sucrose, dextran, nor starch was hydrolyzed by LFTase. DFA IV was very stable at acidic pH and high temperature, thus indicating that DFA IV may be suitable for the food industry and related areas.

AB - A new levan fructotransferase (LFTase) isolated from Arthrobacter oxydans J17-21 was characterized for the production of difructose dianhydride IV (DFA IV). LFTase was purified to apparent homogeneity by Q-Sepharose ion exchange chromatography, Mono-Q HR 5/5 column chromatography, and gel permeation chromatography. The enzyme had an apparent molecular mass of 54000 Da. The optimum pH for the enzyme-catalyzed reaction was pH 6.5, and the optimum temperature was observed at 45 °C. The LFTase was activated by the presence of CaCl2 and EDTA-2Na but inhibited strongly by MnCl2 and CuSO4 at 1 mM and completely by FeSO4 and Ag2SO4 at 1 mM. A bacterial levan from Zymomonas mobilis was incubated with an LFTase; final conversion yield from the levan to DFA IV was 35%. Neither inulin, levanbiose, sucrose, dextran, nor starch was hydrolyzed by LFTase. DFA IV was very stable at acidic pH and high temperature, thus indicating that DFA IV may be suitable for the food industry and related areas.

KW - Arthrobacter oxydans

KW - DFA IV

KW - Levan fructotransferase

KW - Levan-hydrolyzing enzyme

UR - http://www.scopus.com/inward/record.url?scp=0344519748&partnerID=8YFLogxK

U2 - 10.1021/jf026207o

DO - 10.1021/jf026207o

M3 - Article

C2 - 12696949

AN - SCOPUS:0344519748

SN - 0021-8561

VL - 51

SP - 2632

EP - 2636

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 9

ER -

Levan fructotransferase from Arthrobacter oxydans J17-21 catalyzes the formation of the Di-D-fructose dianhydride IV from levan

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this