Evidence map›Paper›PMID 41718352›Full record

ArticleBiotech (Basel (Switzerland))2026

Plant-Derived Hydrolysates Are a Suitable Replacement for Tryptone N1 in Recombinant Protein Expression Using Human Embryonic Kidney (HEK293-6E) Cells.

Shafqat Shabir, Md Shahadat Hossain, Lucie Egly, Gizem Yalkin, Franco H Falcone

Abstract read
In one paragraph

Article in Biotech (Basel (Switzerland)), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Shafqat ShabirInstitute of Parasitology, Justus-Liebig-University Giessen, 35392 Giessen, Germany.ORCID 0000-0003-3794-0373
Md Shahadat HossainInstitute of Parasitology, Justus-Liebig-University Giessen, 35392 Giessen, Germany.ORCID 0000-0002-6176-1036
Lucie EglySpécialité Génie Biologique et Santé, Polytech Angers, 49000 Angers, France.
Gizem YalkinOrganotechnie, 93120 La Courneuve, France.
Franco H FalconeInstitute of Parasitology, Justus-Liebig-University Giessen, 35392 Giessen, Germany.ORCID 0000-0002-1732-9932

Funding

Organotechnie n/a
6 · The paper itself

Abstract

Human embryonic kidney (HEK293) cells are a widespread choice for recombinant protein expression. To optimise yields, the hydrolysate Tryptone N1 (TN1) is commonly added post-transfection. TN1 is obtained by controlled enzymatic digestion of casein. As an animal by-product, TN1 faces stricter regulations during cross-country shipments than plant-based products. This raises the question of whether plant-derived peptides are a suitable alternative to TN1. Using polyethyleneimine (PEI) as a cationic polymer, we transfected HEK293-6E cells grown in suspension in serum-free medium and divided the transfectants into four groups (each in triplicate). Two plant-based hydrolysates each derived from pea and broad bean were compared with TN1 and a no-hydrolysate control group. We monitored the cultures for total cell numbers and viability at days 1, 4, and 5 post-transfection. Both plant-based hydrolysates and TN1 showed similar live cell percentages, in contrast to the no-hydrolysate control, which showed lower viability. Five days post-transfection, the expressed His-tagged protein, a tegumental antigen from the eukaryotic parasite

Indexed as

HEK293hydrolysatesplant-derivedrecombinant expressionTryptone N1

Identifiers

PMID41718352
PMCPMC12922121

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.