Activity and stability of dextransucrase from Leuconostoc mesenteroides NRRL B-512F in the presence of organic solvents

被引:28
作者
Girard, E [1 ]
Legoy, MD [1 ]
机构
[1] Univ La Rochelle, LGPC, Pole Sci & Technol, F-17042 La Rochelle 1, France
关键词
dextransucrase; organic solvent; activity; stability;
D O I
10.1016/S0141-0229(98)00166-5
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The behavior of dextransucrase from Leuconostoc mesenteroides NRRL-B-512F in the presence of organic solvents was investigated The activity and stability of this enzyme were studied in the presence of various concentrations (% v/v) of dimethysulfoxide (DMSO) dimethylformamide (DMF) ethanol, acetone and acetonitrile. The stability was measured at 4 degrees C and 30 degrees C. Generally the initial velocity of dextransucrase decreases proportionally to solvent concentrations except in water-DMSO mixture. Indeed in 25% DMSO (v/v) 45% of the activity in pure wafer was detected whereas 26% was measured in 10% DMSO (v/v). Moreover the loss of activity is much more considerable in the presence of acetonitrile than in the presence of other solvents. In 20% acetonitrile (v/v) only 11% of the activity was measured. Concerning the stability of the enzyme it appears that it is more stable at 4 degrees C than at 30 degrees C. Surprisingly dextransucrase is more active after a period of contact with some solvents, especially DMSO or ethanol, than in acetate buffer. After 2 days in 20% DMSO (v/v) at 4 degrees C, 300% of the initial activity remained and 250% at 30 degrees C. This increase of activity is also observable after 2 days in 20% ethanol (v/v) where 180% of the initial activity is measured. (C) 1999 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:425 / 432
页数:8
相关论文
共 27 条
[1]  
Almarsson O, 1996, BIOTECHNOL BIOENG, V49, P87, DOI 10.1002/(SICI)1097-0290(19960105)49:1<87::AID-BIT11>3.0.CO
[2]  
2-8
[3]   GLYCOSIDASES IN ORGANIC-SOLVENTS .2. TRANSGALACTOSYLATION CATALYZED BY POLYETHYLENE GLYCOL-MODIFIED BETA-GALACTOSIDASE [J].
BEECHER, JE ;
ANDREWS, AT ;
VULFSON, EN .
ENZYME AND MICROBIAL TECHNOLOGY, 1990, 12 (12) :955-959
[4]   INHIBITION-REACTION AND ACCEPTOR-REACTION STUDIES OF STREPTOCOCCUS-MUTANS 6715 GLUCOSYLTRANSFERASES WITH 3-DEOXYSUCROSE, 3-DEOXY-3-FLUOROSUCROSE, AND ALPHA-D-ALLOPYRANOSYL BETA-D-FRUCTOFURANOSIDE [J].
BINDER, TP ;
ROBYT, JF .
CARBOHYDRATE RESEARCH, 1986, 154 :229-238
[5]   KINETICS OF LEUCROSE FORMATION FROM SUCROSE BY DEXTRANSUCRASE [J].
BOKER, M ;
JORDENING, HJ ;
BUCHHOLZ, K .
BIOTECHNOLOGY AND BIOENGINEERING, 1994, 43 (09) :856-864
[6]   BIOCATALYSIS IN ORGANIC MEDIA [J].
BRINK, LES ;
TRAMPER, J ;
LUYBEN, KCAM ;
VANTRIET, K .
ENZYME AND MICROBIAL TECHNOLOGY, 1988, 10 (12) :736-743
[7]  
Griebenow K, 1997, BIOTECHNOL BIOENG, V53, P351, DOI 10.1002/(SICI)1097-0290(19970220)53:4<351::AID-BIT1>3.0.CO
[8]  
2-M
[9]   NEW REACTIONS OF DEXTRANSUCRASE - ALPHA-D-GLUCOSYL TRANSFERS TO AND FROM ANOMERIC SITES OF LACTULOSE AND FRUCTOSE [J].
HEHRE, EJ ;
SUZUKI, H .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1966, 113 (03) :675-&
[10]   SCOPE OF INTERANOMERIC GLYCOSYL TRANSFER REACTIONS - HETERO-DIALDOSIDE SYNTHESIS BY ENZYMIC GLUCOSYLATION OF D-GALACTOSE AND D-MANNOSE [J].
IRIKI, Y ;
HEHRE, EJ .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1969, 134 (01) :130-&