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Contribution of Quasifibrillar Properties of Collagen Hydrolysates Towards Lowering of Interface Tension in Emulsion-Based Food Leading to Shelf-Life Enhancement

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Abstract

This study was conducted to decipher the mechanism of emulsion-based food stabilization by fish-derived collagen hydrolysate. Collagen type I was isolated from seven fish processing by-products with yields ranging from 9.15 to 92.38%. The isolated samples had a mass of 110–120kDa and eluted at 30.44% NaCl in ion-exchange chromatography. The collagen samples were enzymatically digested to obtain collagen hydrolysate (CH) with mass <6kDa. The seven CH samples were subsequently screened for surface activity. CH obtained from Pacu skin and Tilapia bones exhibited more than 80% solubility over a wide pH range, zeta potential greater than +50mV, moisture retention up to 92–96%, emulsification activity of 53–70 m2g−1, and emulsion stability of 62–85min, and successfully increased the emulsion stability of a drug by 14 times. Both CH samples were able to retain the emulsion properties of butter and chocolate sauce for 25 weeks and did not show any cytotoxic effect on leukocytes and Vero cells. Structural studies revealed that the CH peptides existed in polyproline-II conformation that assembled to form a vast quasifibrillar network. Sequence analysis through tandem mass spectroscopy revealed that the peptides could be classified into multiple groups depending on the distribution of hydrophilic/lipophilic residues (H/L). The surface activity of the CH was found to be dependent on (1) small size and a wide array of H/L ratio, (2) abundance of hydroxyproline, and (3) assembly of the peptides in the emulsion interface to form a mimic-helix–based quasifibrillar network which ensured optimal orientation and subsequent interaction with multiple phases.

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Acknowledgements

The authors express their gratitude to the LCMS facility, Indian Institute of Science, Bangalore, India, for helping with the sequence identification. The authors are also thankful to Ms. Manjushree Kupendra, INSPIRE fellow at Dayananda Sagar University, for her help in collecting the mass spectrometry data. Some of the components of Fig.9 have been used from Servier Medical Art.

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Not applicable. All the relevant data have been displayed in the manuscript figures.

Funding

The authors are thankful to the Centre of Innovation in Science and Engineering in Dayananda Sagar Institution, funded by the Vision Group on Science and Technology, Government of Karnataka (grant number GRD 316) for the partial funding of this study.

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Authors and Affiliations

  1. Department of Biochemistry, Dayananda Sagar Institutions, Bangalore, Karnataka, 560111, India

    Pritha Dey, Saleem Kadharbasha, Jayashree Das & Tanuj Chakraborty

  2. School of Basic and Applied Sciences, Dayananda Sagar University, Bangalore, Karnataka, 560111, India

    Mayur Bajaj, Chetna Bhat & Pradipta Banerjee

Authors
  1. Pritha Dey

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  2. Saleem Kadharbasha

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  3. Mayur Bajaj

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  4. Jayashree Das

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  5. Tanuj Chakraborty

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  6. Chetna Bhat

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  7. Pradipta Banerjee

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Contributions

Pritha Dey and Saleem Kadharbasha were involved in the isolation of the collagen samples from fish waste, their characterization, hydrolysis, and performing the assays. Mayur Bajaj helped in the characterization of hydrolysates, structural studies, and assays. Jayashree Das and Tanuj Chakraborty offered their help during the several assays performed in the study. Chetna Bhat helped during the purification of the hydrolysate and was primarily responsible for mass spectroscopy data analysis. Pradipta Banerjee was responsible for designing the study, obtaining funds, designing the experiments, statistical analysis of results, figure drawing, and manuscript writing. All the authors contributed toward data interpretation, manuscript preparation, and subsequent editing.

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Correspondence toPradipta Banerjee.

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Dey, P., Kadharbasha, S., Bajaj, M.et al. Contribution of Quasifibrillar Properties of Collagen Hydrolysates Towards Lowering of Interface Tension in Emulsion-Based Food Leading to Shelf-Life Enhancement.Food Bioprocess Technol14, 1566–1586 (2021). https://doi.org/10.1007/s11947-021-02640-z

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