Immobilization of fructosyltransferase from Streptococcus mutans on hydroxyapatite surfaces induces the formation of multimeric complexes

M. Bronshteyn; D. Steinberg

doi:10.1046/j.1472-765x.2002.01073.x

Immobilization of fructosyltransferase from Streptococcus mutans on hydroxyapatite surfaces induces the formation of multimeric complexes

M. Bronshteyn, D. Steinberg^*

^*Corresponding author for this work

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

8 Scopus citations

Abstract

Aims: To investigate the formation of fructosyltransferase (FTF) complexes on hydroxyapatite (HA) surfaces. Methods and Results: Cell-free extracellular FTF from Streptococcus mutans, purified from hyperproducing strain V-1995, was adsorbed onto HA and then eluted from the surface by means of a concentration gradient of potassium phosphate buffer. The FTF monomers loaded onto HA formed, upon adsorption, various complexes ranging from 200 to 700 kDa as demonstrated using native PAGE. All these complexes exhibited enzymatic activity. Conclusions: Adsorption of FTF onto HA induced the formation of stable and enzymatically-active complexes. Significance and Impact of the Study: The formation of these complexes may explain the change of FTF catalytic properties after adsorption onto HA. This study is another step in determining the properties of a-cellular constituents of the oral biofilm.

Original language	American English
Pages (from-to)	205-209
Number of pages	5
Journal	Letters in Applied Microbiology
Volume	34
Issue number	3
DOIs	https://doi.org/10.1046/j.1472-765x.2002.01073.x
State	Published - 2002
Externally published	Yes

Access to Document

10.1046/j.1472-765x.2002.01073.x

Cite this

@article{57b186c8c4294ab983ddf9fe9ae8adf4,

title = "Immobilization of fructosyltransferase from Streptococcus mutans on hydroxyapatite surfaces induces the formation of multimeric complexes",

abstract = "Aims: To investigate the formation of fructosyltransferase (FTF) complexes on hydroxyapatite (HA) surfaces. Methods and Results: Cell-free extracellular FTF from Streptococcus mutans, purified from hyperproducing strain V-1995, was adsorbed onto HA and then eluted from the surface by means of a concentration gradient of potassium phosphate buffer. The FTF monomers loaded onto HA formed, upon adsorption, various complexes ranging from 200 to 700 kDa as demonstrated using native PAGE. All these complexes exhibited enzymatic activity. Conclusions: Adsorption of FTF onto HA induced the formation of stable and enzymatically-active complexes. Significance and Impact of the Study: The formation of these complexes may explain the change of FTF catalytic properties after adsorption onto HA. This study is another step in determining the properties of a-cellular constituents of the oral biofilm.",

author = "M. Bronshteyn and D. Steinberg",

year = "2002",

doi = "10.1046/j.1472-765x.2002.01073.x",

language = "American English",

volume = "34",

pages = "205--209",

journal = "Letters in Applied Microbiology",

issn = "0266-8254",

publisher = "Wiley-Blackwell Publishing Ltd",

number = "3",

}

TY - JOUR

T1 - Immobilization of fructosyltransferase from Streptococcus mutans on hydroxyapatite surfaces induces the formation of multimeric complexes

AU - Bronshteyn, M.

AU - Steinberg, D.

PY - 2002

Y1 - 2002

N2 - Aims: To investigate the formation of fructosyltransferase (FTF) complexes on hydroxyapatite (HA) surfaces. Methods and Results: Cell-free extracellular FTF from Streptococcus mutans, purified from hyperproducing strain V-1995, was adsorbed onto HA and then eluted from the surface by means of a concentration gradient of potassium phosphate buffer. The FTF monomers loaded onto HA formed, upon adsorption, various complexes ranging from 200 to 700 kDa as demonstrated using native PAGE. All these complexes exhibited enzymatic activity. Conclusions: Adsorption of FTF onto HA induced the formation of stable and enzymatically-active complexes. Significance and Impact of the Study: The formation of these complexes may explain the change of FTF catalytic properties after adsorption onto HA. This study is another step in determining the properties of a-cellular constituents of the oral biofilm.

AB - Aims: To investigate the formation of fructosyltransferase (FTF) complexes on hydroxyapatite (HA) surfaces. Methods and Results: Cell-free extracellular FTF from Streptococcus mutans, purified from hyperproducing strain V-1995, was adsorbed onto HA and then eluted from the surface by means of a concentration gradient of potassium phosphate buffer. The FTF monomers loaded onto HA formed, upon adsorption, various complexes ranging from 200 to 700 kDa as demonstrated using native PAGE. All these complexes exhibited enzymatic activity. Conclusions: Adsorption of FTF onto HA induced the formation of stable and enzymatically-active complexes. Significance and Impact of the Study: The formation of these complexes may explain the change of FTF catalytic properties after adsorption onto HA. This study is another step in determining the properties of a-cellular constituents of the oral biofilm.

UR - http://www.scopus.com/inward/record.url?scp=0036125422&partnerID=8YFLogxK

U2 - 10.1046/j.1472-765x.2002.01073.x

DO - 10.1046/j.1472-765x.2002.01073.x

M3 - Article

C2 - 11874543

AN - SCOPUS:0036125422

SN - 0266-8254

VL - 34

SP - 205

EP - 209

JO - Letters in Applied Microbiology

JF - Letters in Applied Microbiology

IS - 3

ER -

Immobilization of fructosyltransferase from Streptococcus mutans on hydroxyapatite surfaces induces the formation of multimeric complexes

Abstract

Access to Document

Other files and links

Fingerprint

Cite this