| RRC ID |
50951
|
| Author |
Li Y, Wang Y, Tu T, Zhang D, Ma R, You S, Wang X, Yao B, Luo H, Xu B.
|
| Title |
Two acidic, thermophilic GH28 polygalacturonases from Talaromyces leycettanus JCM 12802 with application potentials for grape juice clarification.
|
| Journal |
Food Chem
|
| Abstract |
Efficient hydrolysis of pectic materials to sugars requires the synergistic action of endo- and exo-polygalacturonases. Two novel polygalacturonases (exo-TePG28a and endo-TePG28b) were identified in Talaromyces leycettanus JCM12802, overexpressed in Pichia pastoris, and characterized in this report. The specific activities of TePG28a and TePG28b towards polygalacturonic acid were 280±9 and 25,900±502U/mg, respectively. Both enzymes exhibited optimal activities at pH 3.5 and retained highly stable over a broad pH range of 2.0-7.0. Distinct from most fungal polygalacturonases that have low temperature optima, TePG28a and TePG28b were optimally active at 70°C. When treated the grape juice with the enzyme combination (the unit ratio of TePG28a:TePG28b was 1:4), higher pectin-degrading efficiency (up to 140%) was achieved, and light transmittance was improved from 14% to 82%. These favorable enzymatic properties make TePG28a and TePG28b attractive for the applications in the juice industry.
|
| Volume |
237
|
| Pages |
997-1003
|
| Published |
2017-12-15
|
| DOI |
10.1016/j.foodchem.2017.06.037
|
| PII |
S0308-8146(17)31019-1
|
| PMID |
28764098
|
| MeSH |
Cloning, Molecular
Enzyme Stability
Polygalacturonase
Talaromyces / enzymology*
Temperature
Vitis
|
| IF |
6.306
|
| Times Cited |
8
|
| Resource |
| General Microbes |
JCM 12802 |
