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Transgenic Research

, Volume 27, Issue 2, pp 211–224 | Cite as

Insights into phytase-containing transgenic Lemna minor (L.) as a novel feed additive

  • Mrinmoy Ghosh
  • Neelesh Sharma
  • Meeta Gera
  • Nameun Kim
  • Do Huynh
  • Jiaojiao Zhang
  • Taesun Min
  • Simrinder Singh Sodhi
  • Min Bae Kim
  • V. P. B. Rekha
  • Sukmin Ko
  • Dong Kee Jeong
Original Paper

Abstract

This study assessed the effect of supplementation of novel transgenic phytase on growth performance and bone mineralization in Korean native broiler chickens. The experiment was designed using four dietary groups: those with a diet supplemented with (A) recombinant phytase, (B) transgenic phytase from the plant Lemna minor, (C) or wild-type L. minor as well as (D) a control group that was supplemented with commercially available feed. Three hundred 1-day-old Korean native broiler chicks were used and divided into these four dietary treatment groups having three replicates of 25 birds each (n = 75). The results showed increases in growth performance and bone mineralization in Groups B and C; compared with Groups A and D. Hematological analyses revealed notable contrasts in erythrocyte sedimentation rate, red blood cell count, and hemoglobin levels among the experimental groups, whereas no impacts of dietary treatment were observed on total eosinophil, lymphocyte, heterophil, monocyte, and basophil levels. The relative expression profiling of candidate genes showed that the genes involved in growth response, meat quality, and P–Ca metabolism were significantly highly expressed in the phytase-supplemented groups. Hence, it is suggested that dietary supplementation with transgenic phytase plant L. minor for enhancing growth performance is a promising new approach in the broiler feed industry. To the best of our knowledge, we report here the most comprehensive analysis using a broiler model that provides a workable platform for further research on the cost-effective production of feed with different compositions that might be beneficial in the livestock feed industry.

Keywords

Bioavailability Broiler chicken Growth performance Gene expression Transgenic phytase 

Notes

Acknowledgements

The authors are thankful for support from the Next-Generation Bio-Green 21 Program (No. PJ01117401), Rural Development Administration, Republic of Korea.

Authors’ contributions

DKJ and SK contributed to the design and conception of the project; MG contributed to the design, analysis, and interpretation of data; NS contributed to the evaluation of intellectual content; NK, MG, and DH contributed to the collection, harvesting tissue samples, and mRNA analyses; SSS and JZ contributed to the collection of field samples; TSM, MBK, VPBR, and DKJ contributed to the revision of the manuscript; all authors read and approved the final manuscript.

Compliance with ethical standards

Conflict of interest

The authors do not have any conflict of interest.

Supplementary material

11248_2018_68_MOESM1_ESM.tif (14.9 mb)
Supplementary Fig. 1 Network visualization and a functional module of the selected genes from Gallus gallus domesticus as predicted by the STRING tool. (a) The figure illustrates the co-expression pattern of among COX1, PRDX4 and NOX2 with the partner proteins; (b) prediction of the functional pattern of immunity response genes IL-4 and TLR2; (c) MYBPH does not contribute to POSTN and IGF-I. MYBPH has associated with 10 different protein molecules; (d) the predicted functional pattern of POSTN and IGF-1; (e) the functional pattern of meat quality attribution genes TYRO3 and COL1A2; (f) the string interaction of Ca and P metabolism response genes TRPV6 and FGF23 with the partner proteins. The tool highlights the corresponding nodes in the network (TIFF 15301 kb)
11248_2018_68_MOESM2_ESM.jpg (555 kb)
Supplementary Fig. 2 Schematic representations the MyBPC/H molecules within the sarcomere, cross bridge region, various myofibrillar components (tropomyosin-Tm; hetero-trimeric troponin- TnT, TnI, and TnC) relative to each other and indications of major and functionally significant protein phosphorylation sites. The sites of phosphorylation are indicated by an asterisk. The myosin light chain (MLC) and MyBP-H/C are involved in the radial movement of myosin heads. MyBPC has interaction sites with the neck region via the M domain and with the titin region via C-terminal domains (C8, C9, and C10) (JPEG 555 kb)
11248_2018_68_MOESM3_ESM.docx (66 kb)
Supplementary material 3 (DOCX 66 kb)

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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  • Mrinmoy Ghosh
    • 1
  • Neelesh Sharma
    • 2
  • Meeta Gera
    • 1
  • Nameun Kim
    • 1
  • Do Huynh
    • 1
  • Jiaojiao Zhang
    • 1
  • Taesun Min
    • 1
  • Simrinder Singh Sodhi
    • 3
  • Min Bae Kim
    • 4
  • V. P. B. Rekha
    • 5
  • Sukmin Ko
    • 6
  • Dong Kee Jeong
    • 1
  1. 1.Department of Animal Biotechnology, Faculty of BiotechnologyJeju National UniversityJejuRepublic of Korea
  2. 2.Department of Veterinary Medicine, Faculty of Veterinary Science and Animal HusbandrySher-e-Kashmir University of Agricultural Sciences and Technology of JammuR.S. Pura, JammuIndia
  3. 3.Department of Veterinary and Animal Husbandry Extension EducationGuru Angad Dev Veterinary and Animal Sciences UniversityLudhianaIndia
  4. 4.Department of Agricultural EducationSunchon National UniversitySuncheonRepublic of Korea
  5. 5.School of BiotechnologyGautam Buddha UniversityGautam Buddha Nagar, Greater NoidaIndia
  6. 6.Omicsis. Inc. BVC, Korea Research Institute of Bioscience and BiotechnologyDaejeonRepublic of Korea

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