Two fractional model for evaluating the activity of glucoamylase from Aspergillus niger under combined pressure and temperature conditions

被引：15

作者：

Buckow, R ^{[1
]}

Heinz, V ^{[1
]}

Knorr, D ^{[1
]}

机构：

[1] Berlin Univ Technol, Dept Food Biotechnol & Food Proc Engn, D-14195 Berlin, Germany

来源：

FOOD AND BIOPRODUCTS PROCESSING | 2005年 / 83卷 / C3期

关键词：

glucoamylase; Aspergillus niger; high pressure; inactivation; conversion rate; optimization;

D O I：

10.1205/fbp.04250

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 impact of high pressure and temperatures on the conversion reaction of glucoamylase has been assessed by the kinetic rate constants. Hydrostatic pressure up to 1400 MPa in a temperature range from 40 to 95 degrees C has been investigated. A two fractional model is suggested to describe the inactivation behaviour of the enzyme over all tested pT-combinations. It was supposed that the two isoforms of glucoamylase (GA1 and GA2) responded differently to high hydrostatic pressure. The pressure labile form of glucoamylase (GA2) was inactivated quickly at pressures above 850 MPa whereas the stable form (GA1) showed slower inactivation at pressure levels up to 1400 MPa at 50 degrees C. A significant stabilization against heat inactivation has been observed at 400 MPa for GA2 and at 550 MPa for GAL In addition it was observed that high pressure also impedes the enzymatic cleavage of maltose. A reduction of the conversion rate constants with increasing pressures (up to 600 MPa) has been found within the temperature range investigated (40-80 degrees C). For the overall reaction of glucose liberation from maltose monohydrate in ACES buffer at pH 4.5 the optimum was identified at 318 MPa and 84 degrees C for a 30 min process. Compared to the maximum observed at ambient pressure (approximately 62 degrees C) the glucose production was doubled.

引用

页码：220 / 228

页数：9

共 41 条

[1] Purification and properties of two forms of glucoamylase from Aspergillus niger [J].

Amirul, AA ;

Khoo, SL ;

Nazalan, MN ;

Razip, MS ;

Azizan, MN .

FOLIA MICROBIOLOGICA, 1996, 41 (02) :165-174

[2]

ARABAS J, 1999, ADV HIGH PRESSURE BI

[3]

ARDIA A, 2004, DEP FOOD BIOTECHNOLO, P102

[4] Immobilization of glucoamylase onto activated pHEMA/EGDMA microspheres: properties and application to a packed-bed reactor [J].

Arica, MY ;

Alaeddinoglu, NG ;

Hasirci, V .

ENZYME AND MICROBIAL TECHNOLOGY, 1998, 22 (03) :152-157

[5] Pressure effects on intra- and intermolecular interactions within proteins [J].

Boonyaratanakornkit, BB ;

Park, CB ;

Clark, DS .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 2002, 1595 (1-2) :235-249

[6]

CHEFTEL JC, 1992, COLLOQ INSE, V224, P195

[7] Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry [J].

Christensen, T ;

Svensson, B ;

Sigurskjold, BW .

BIOCHEMISTRY, 1999, 38 (19) :6300-6310

[8] Physicochemical characterisation of the two active site mutants Trp52→Phe and Asp55→Val of glucoamylase from Aspergillus niger [J].

Christensen, T ;

Frandsen, TP ;

Kaarsholm, NC ;

Svensson, B ;

Sigurskjold, BW .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2002, 1601 (02) :163-171

[9] Substrate binding mechanism of Glu180->Gln, Asp176->Asn, and wild-type glucoamylases from Aspergillus niger [J].

Christensen, U ;

Olsen, K ;

Stoffer, BB ;

Svensson, B .

BIOCHEMISTRY, 1996, 35 (47) :15009-15018

[10] PURIFICATION AND PROPERTIES OF A THERMOPHILIC AMYLOGLUCOSIDASE FROM ASPERGILLUS-NIGER [J].

FOGARTY, WM ;

BENSON, CP .

EUROPEAN JOURNAL OF APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1983, 18 (05) :271-278

← 1 2 3 4 5 →