Improvement of Laccase Production by Thielavia terrestris Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic TtLacA via Immobilization in Copper Alginate Gel Beads

被引：5

作者：

Gutierrez-Anton, Marina ^{[1
]}

Santiago-Hernandez, Alejandro ^{[1
]}

Rodriguez-Mendoza, Johan ^{[1
]}

Cano-Ramirez, Claudia ^{[2
]}

Bustos-Jaimes, Ismael ^{[3
]}

Aguilar-Osorio, Guillermo ^{[4
]}

Campos, Jorge E. ^{[5
]}

Hidalgo-Lara, Maria Eugenia ^{[1
]}

机构：

[1] CINVESTAV IPN, Dept Biotecnol & Bioingn, Lab Ingn Prot, Ave Inst Politecn Nacl 2508, Mexico City 07360, Mexico

[2] ENCB IPN, Lab Variac Biol & Evoluc, Prol De Carpio & Plan Ayala S-N, Mexico City 11340, Mexico

[3] Univ Nacl Autonoma Mexico, Fac Med, Dept Bioquim, Lab Fisicoquim & Ingn Prot, Ciudad Univ, Mexico City 04510, Mexico

[4] Univ Nacl Autonoma Mexico, Dept Alimentos & Biotecnol, Fac Quim, Grp Fisiol Hongos, Ciudad Univ, Mexico City 04510, Mexico

[5] UNAM, FES Iztacala, UBIPRO, Lab Bioquim Mol, Ave Los Barrios 1, Tlalnepantla De Baz 54090, Mexico

来源：

JOURNAL OF FUNGI | 2023年 / 9卷 / 03期

关键词：

Thielavia terrestris; fungal laccase; alginate immobilization; thermophilic thermostable enzyme; BIOCHEMICAL-CHARACTERIZATION; AROMATIC-COMPOUNDS; SYNTHETIC DYES; METAL-IONS; EXTRACELLULAR LACCASE; PURIFICATION; FUNGUS; DECOLORIZATION; INDUCTION; OPTIMIZATION;

D O I：

10.3390/jof9030308

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A 32-fold increase in laccase activity production by the thermophilic biomass-degrading fungus T. terrestris Co3Bag1 was achieved when the microorganism was grown on a modified medium containing fructose, sodium nitrate, and copper. A 70 kDa laccase (TtLacA), produced under the above conditions, was purified, immobilized in copper alginate gel beads, and characterized. TtLacA, both free and immobilized enzymes, exhibited optimal activity at pH 3.0, at a temperature of 65 and 70 degrees C, respectively, although both displayed 70% of activity from 40 to 70 degrees C. Free and immobilized enzymes retained at least 80% of relative activity in the pH range from 3 to 4.6. Immobilized TtLacA manifested a 2.3-fold higher thermal stability than the free form of the enzyme at 60 and 70 degrees C. Immobilized TtLacA retained 95% initial activity for six consecutive reuse cycles at 60 degrees C, and also retained 86% of initial activity after 12 days of storage at 4 degrees C. Based on the biochemical features, thermophilic TtLacA may be an efficient enzyme for dye decolorization and other industrial applications at high temperatures or acidic conditions. This work represents the first report about the immobilization and biochemical characterization of a thermophilic laccase from a member of the genus Thielavia.

引用

页数：24