鶹Ժ


Broad-specificity enzyme targets glycans from across the kingdoms of life

Broad-specificity enzyme targets glycans from across the kingdoms of life
Structures of eukaryotic types of N-glycans. The N-glycan core structure is indicated by the orange box and α-linkages are labeled. Credit: Royal Society Open Science (2025). DOI: 10.1098/rsos.251012

Researchers have found a new enzyme, taken from Flavobacterium akiainvivens, that has a much broader specificity than the current leading alternatives.

This analysis resulted in the identification of the PNGaseL taken from Flavobacterium akiainvivens, which is a microbe isolated from decaying wood of the Hawai'ian plant Wikstroemia oahuensis (ākia), as well as being the state microbe of Hawai'i.

The identification of this new enzyme, PNGaseL, is described in a paper in The Royal Society Open Science New Talent Collection. This discovery follows on from new research conducted by an international team of scientists from the University of Birmingham, in collaboration with industrial partners.

Using a technique called bioprospecting—the process used to find biological resources that can be used to create commercially valuable products, such as pharmaceuticals, cosmetics, or industrial enzymes—the team studied six previously uncharacterized PNGases, which are used in a range of research contexts to remove N-glycans from glycoproteins.

PNGaseL was found to work in a broader range of contexts to remove sugars from proteins, showing its greater utility in glycobiological settings and wide research applications compared to the capabilities of two other widely used enzymes, PNGaseF and PNGaseA.

Dr. Lucy Crouch, a Sir Henry Dale Fellow at the University of Birmingham and senior author of the paper, said, "Our study exemplifies the successful translation of fundamental discovery biology into practical applications. Unlike its predecessors, PNGaseL exhibits a significantly broader substrate specificity, meaning it can target glycans from mammalian, insect and plant-derived proteins in parallel.

"We're very excited by the potential for further discoveries in this space and the impact they may have on both future research and industry-led projects."

More information: Cassie R. Bakshani et al, PNGaseL from Flavobacterium akiainvivens targets a diverse range of N-glycan structures, Royal Society Open Science (2025).

This enzyme is already available to buy through and can be readily integrated into current protocols.

Journal information: Royal Society Open Science

Citation: Broad-specificity enzyme targets glycans from across the kingdoms of life (2025, August 29) retrieved 29 August 2025 from /news/2025-08-broad-specificity-enzyme-glycans-kingdoms.html
This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no part may be reproduced without the written permission. The content is provided for information purposes only.

Explore further

Healthy gut bacteria that feed on sugar analyzed for the first time

0 shares

Feedback to editors