ArticlePloS one2013
Overexpression of an acidic endo-β-1,3-1,4-glucanase in transgenic maize seed for direct utilization in animal feed.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Genetic engineering of complex feed enzymes into barley seed for direct utilization in animal feedstuff.Plant biotechnology journal · 2023Article
- Physical Exercise Protects Against Endothelial Dysfunction in Cardiovascular and Metabolic Diseases.Journal of cardiovascular translational research · 2022Review
- Designing novel construction for cell surface display of protein E on Escherichia coli using non-classical pathway based on Lpp-OmpA.AMB Express · 2017Article
- Genetic engineering of grass cell wall polysaccharides for biorefining.Plant biotechnology journal · 2017Review
- Strategies for the production of cell wall-deconstructing enzymes in lignocellulosic biomass and their utilization for biofuel production.Plant biotechnology journal · 2016Review
- Nutritionally enhanced food crops; progress and perspectives.International journal of molecular sciences · 2015Review
- Production of a Highly Protease-Resistant Fungal α-Galactosidase in Transgenic Maize Seeds for Simplified Feed Processing.PloS one · 2015Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIncorporation of exogenous glucanase into animal feed is common practice to remove glucan, one of the anti-nutritional factors, for efficient nutrition absorption. The acidic endo-β-1,3-1,4-glucanase (Bgl7A) from Bispora sp. MEY-1 has excellent properties and represents a potential enzyme supplement to animal feed. METHODOLOGY/PRINCIPAL
findingsHere we successfully developed a transgenic maize producing a high level of Bgl7AM (codon modified Bgl7A) by constructing a recombinant vector driven by the embryo-specific promoter ZM-leg1A. Southern and Western blot analysis indicated the stable integration and specific expression of the transgene in maize seeds over four generations. The β-glucanase activity of the transgenic maize seeds reached up to 779,800 U/kg, about 236-fold higher than that of non-transgenic maize. The β-glucanase derived from the transgenic maize seeds had an optimal pH of 4.0 and was stable at pH 1.0-8.0, which is in agreement with the normal environment of digestive tract. CONCLUSION/SIGNIFICANCE: Our study offers a transgenic maize line that could be directly used in animal feed without any glucanase production, purification and supplementation, consequently simplifying the feed enzyme processing procedure.
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