Comparative analysis of β-glucosidase activity in non-conventional yeasts.
Journal
Anais da Academia Brasileira de Ciencias
ISSN: 1678-2690
Titre abrégé: An Acad Bras Cienc
Pays: Brazil
ID NLM: 7503280
Informations de publication
Date de publication:
2023
2023
Historique:
received:
12
12
2022
accepted:
08
05
2022
medline:
11
12
2023
pubmed:
6
12
2023
entrez:
6
12
2023
Statut:
epublish
Résumé
The objective of this study was to evaluate the β-glucosidase activity in the non-conventional yeasts under cellulose, glucose and sucrose substrates. The participation of the enzyme β-glucosidase and its contribution to the enzymatic degradation of tannins is known. Within the classification of tannins are ellagitannins, molecules of gallic acid and ellagic acid, which are considered as nutraceutical compounds due to the properties that they present and that they can be used in the design of food and new drugs, synthesis of materials with antimicrobial capacity. The extracellular β-glucosidase activity was mainly presented in the Candida and Pichia strains, being the glucose and sucrose media the most capable for inducing the activity that showed maximum values with P. pastoris in glucose (0.1682±0.00 µmol/min mg protein), and C. utilis in cellulose (0.1129±0.1349 µmol/min mg of protein), and sucrose (0.0657±0.0214 µmol/min mg protein). Additionally, I. terricola and P. kluyvery stood out in a qualitative cellulose degradation approach measured by Congo red method (9.60±0.04 mm and 9.20±0.05 mm respectively). These indicate that P. pastoris and C. utilis have potential as β-glucosidase producers, especially when growing under complex carbon sources for biomass conversion, new biofuels production and polyphenol degradation with more manageable bioreactor process.
Identifiants
pubmed: 38055563
pii: S0001-37652023000500901
doi: 10.1590/0001-3765202320221118
pii:
doi:
Substances chimiques
Tannins
0
Cellulose
9004-34-6
Glucose
IY9XDZ35W2
Sucrose
57-50-1
Cellulases
EC 3.2.1.-
beta-Glucosidase
EC 3.2.1.21
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM