Amino acids and glycine derivatives differently affect refolding of mesophilic and thermophilic like α-amylases: implications in protein refolding and aggregation.

Protein aggregation amino acids osmolytes refolding α-amylase

Journal

Journal of biomolecular structure & dynamics
ISSN: 1538-0254
Titre abrégé: J Biomol Struct Dyn
Pays: England
ID NLM: 8404176

Informations de publication

Date de publication:
14 Mar 2024
Historique:
medline: 15 3 2024
pubmed: 15 3 2024
entrez: 15 3 2024
Statut: aheadofprint

Résumé

α-amylases are industrially important enzymes which are used in different starch-based industries. They are adapted to different environmental conditions like extremes of temperature, pH and salinity. Herein, α-amylases from

Identifiants

pubmed: 38486406
doi: 10.1080/07391102.2024.2327540
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1-14

Auteurs

Aziz Ahmad (A)

School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.

Prachi Joshi (P)

School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.

Rajesh Mishra (R)

School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.

Classifications MeSH