Immobilization of inulinase for sucrose hydrolysis

R. Catana; B. S. Ferreira; J. M.S. Cabral; P. Fernandes

doi:10.1016/j.foodchem.2004.04.041

Immobilization of inulinase for sucrose hydrolysis

R. Catana, B. S. Ferreira, J. M.S. Cabral, P. Fernandes

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

54 Citations (Scopus)

Abstract

A commercial inulinase preparation immobilized on various supports was used for sucrose hydrolysis. Entrapment and encapsulation in Ca-alginate and entrapment in an alginate-silicate sol-gel matrix were evaluated. Best results were obtained with Ca-alginate beads. The influence of sodium-alginate concentration on the immobilization yield was assessed. Inulinase entrapped in Ca-alginate beads displayed high activity in the range 50-60°C, whereas the optimum for the free enzyme was 60°C. The optimum pH of the immobilized enzyme was slightly more acidic (4.0) than the one observed for the free form (4.5). The apparent K_M for sucrose of the immobilized inulinase was 184 mM, as compared to 82 mM for free inulinase, as a result of diffusion resistances.

Original language	English
Pages (from-to)	517-520
Number of pages	4
Journal	Food Chemistry
Volume	91
Issue number	3
DOIs	https://doi.org/10.1016/j.foodchem.2004.04.041
Publication status	Published - Jul 2005

Keywords

Biotransformation
Ca-alginate entrapment
Enzyme immobilization
Inulinase

Access to Document

10.1016/j.foodchem.2004.04.041

Cite this

@article{36a2030e11784a11aefa812f7222026a,

title = "Immobilization of inulinase for sucrose hydrolysis",

abstract = "A commercial inulinase preparation immobilized on various supports was used for sucrose hydrolysis. Entrapment and encapsulation in Ca-alginate and entrapment in an alginate-silicate sol-gel matrix were evaluated. Best results were obtained with Ca-alginate beads. The influence of sodium-alginate concentration on the immobilization yield was assessed. Inulinase entrapped in Ca-alginate beads displayed high activity in the range 50-60°C, whereas the optimum for the free enzyme was 60°C. The optimum pH of the immobilized enzyme was slightly more acidic (4.0) than the one observed for the free form (4.5). The apparent KM for sucrose of the immobilized inulinase was 184 mM, as compared to 82 mM for free inulinase, as a result of diffusion resistances.",

keywords = "Biotransformation, Ca-alginate entrapment, Enzyme immobilization, Inulinase",

author = "R. Catana and Ferreira, {B. S.} and Cabral, {J. M.S.} and P. Fernandes",

year = "2005",

month = jul,

doi = "10.1016/j.foodchem.2004.04.041",

language = "English",

volume = "91",

pages = "517--520",

journal = "Food Chemistry",

issn = "0308-8146",

publisher = "Elsevier Ltd.",

number = "3",

}

TY - JOUR

T1 - Immobilization of inulinase for sucrose hydrolysis

AU - Catana, R.

AU - Ferreira, B. S.

AU - Cabral, J. M.S.

AU - Fernandes, P.

PY - 2005/7

Y1 - 2005/7

N2 - A commercial inulinase preparation immobilized on various supports was used for sucrose hydrolysis. Entrapment and encapsulation in Ca-alginate and entrapment in an alginate-silicate sol-gel matrix were evaluated. Best results were obtained with Ca-alginate beads. The influence of sodium-alginate concentration on the immobilization yield was assessed. Inulinase entrapped in Ca-alginate beads displayed high activity in the range 50-60°C, whereas the optimum for the free enzyme was 60°C. The optimum pH of the immobilized enzyme was slightly more acidic (4.0) than the one observed for the free form (4.5). The apparent KM for sucrose of the immobilized inulinase was 184 mM, as compared to 82 mM for free inulinase, as a result of diffusion resistances.

AB - A commercial inulinase preparation immobilized on various supports was used for sucrose hydrolysis. Entrapment and encapsulation in Ca-alginate and entrapment in an alginate-silicate sol-gel matrix were evaluated. Best results were obtained with Ca-alginate beads. The influence of sodium-alginate concentration on the immobilization yield was assessed. Inulinase entrapped in Ca-alginate beads displayed high activity in the range 50-60°C, whereas the optimum for the free enzyme was 60°C. The optimum pH of the immobilized enzyme was slightly more acidic (4.0) than the one observed for the free form (4.5). The apparent KM for sucrose of the immobilized inulinase was 184 mM, as compared to 82 mM for free inulinase, as a result of diffusion resistances.

KW - Biotransformation

KW - Ca-alginate entrapment

KW - Enzyme immobilization

KW - Inulinase

UR - http://www.scopus.com/inward/record.url?scp=11144317788&partnerID=8YFLogxK

U2 - 10.1016/j.foodchem.2004.04.041

DO - 10.1016/j.foodchem.2004.04.041

M3 - Article

AN - SCOPUS:11144317788

SN - 0308-8146

VL - 91

SP - 517

EP - 520

JO - Food Chemistry

JF - Food Chemistry

IS - 3

ER -

Immobilization of inulinase for sucrose hydrolysis

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this