Sign in
Molecular BiologybioRxiv
Preprint

L-Arginine Hydrochloride Enables Cold-Chain-Free DNA Polymerase Storage

Joseph shenekjiiD, Antonius Al-Daoud, Abduljalil Ghrewati

Abstract

Preserving DNA polymerases under ambient conditions is a critical challenge, particularly in resource-limited settings with minimal cold storage infrastructure. This study introduces a novel, cost-effective approach to polymerase stabilization using L-arginine hydrochloride (LAH), evaluating its efficacy for Pfu polymerase and polymerase mixtures stored in 20 {micro}l aliquots at 4{degrees}C, 25{degrees}C, and 37{degrees}C over three months. Enzyme activity was assessed via polymerase chain reaction (PCR) amplification of a 1250 base pair (bp) DNA fragment. Pfu polymerase maintained enzymatic activity at all tested temperatures with 1 M LAH, whereas activity was lost at 37{degrees}C without the stabilizer. LAH also enhanced the stability of Taq polymerase and Pfu + Taq mixtures, though with reduced efficacy. Mechanistically, LAH prevents protein aggregation, enhances solubility, and stabilizes enzyme structure through electrostatic interactions. These findings position LAH as a robust stabilizer, reducing cold chain dependency and enabling scalable molecular diagnostics in low-resource environments. This study advances enzyme preservation by offering a sustainable alternative to traditional methods, with applications in clinical diagnostics and biotechnology. Future work will optimize LAH concentrations, assess long-term stability beyond three months, and extend the approach to other thermostable polymerases.

PDFDOI

02 /Specification & Classification

Click any tag to browse matching papers

Reproducibility ledger

Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.

Sign in to file a reproducibility report.