Production, characterization, and application of novel fungal pullulanase for fruit juice processing.
Pullulanase fermentation
Pullulanase production
Pullulanase purification
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Sep 2023
01 Sep 2023
Historique:
received:
09
06
2023
revised:
13
07
2023
accepted:
20
07
2023
medline:
22
9
2023
pubmed:
24
7
2023
entrez:
23
7
2023
Statut:
ppublish
Résumé
The present study aimed to produce, characterize, and apply pullulanase from Aspergillus flavus (BHU-46) for fruit juice processing, assessing its enzymatic properties and impact on juice quality. Pullulanase was produced via solid-state fermentation using wheat bran as the substrate. Purification and characterization included specific activity, molecular weight, pH and temperature optima, and substrate specificity. The enzyme was immobilized in sodium alginate beads and used for clarifying mosambi, apple, and mango juices. Parameters such as yield, clarity, reducing sugar, total soluble solids (TSS), total phenol, and enzymatic browning were evaluated pre-and post-treatment. The purified pullulanase had a specific activity of 652.2 U/mg and a molecular weight of 135 kDa. Optimal pH values were 6.5 and 10, with maximum activity at 50 °C. Pullulanase showed a high affinity for pullulan and starch, indicating Pullulanase type II classification. Immobilized pullulanase improved yield, clarity, reducing sugar, TSS, and total phenol in fruit juices. The highest yield and clarity were observed in mosambi juice. Additionally, the enzyme reduced enzymatic browning, increasing the lightness of the juice. This study provides a significant contribution to the juice processing industry and represents the first report on the application of pullulanase for fruit juice processing.
Identifiants
pubmed: 37482156
pii: S0141-8130(23)02831-3
doi: 10.1016/j.ijbiomac.2023.125936
pii:
doi:
Substances chimiques
pullulanase
EC 3.2.1.41
Glycoside Hydrolases
EC 3.2.1.-
Phenols
0
Sugars
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
125936Informations de copyright
Copyright © 2023. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper