Abstract

Objective: To differentiate porcine gelatin and bovine gelatins using specific peptide markers as determined by liquid chromatography-mass spectrometry tandem with mass spectrometry (LC-MS/MS) and classify both gelatins using retention time and m/z as variables in principal component analysis (PCA).
 Methods: Porcine and bovine gelatins were digested using trypsin enzyme and then subjected to LC-MS/MS analysis. The specific peptides were identified. The classification between porcine and bovine gelatins was carried out using chemometrics of PCA using retention times and mass to charge ratio (m/z) as variables.
 Results: PCA using singvariables retention times (tR) and m/z could successfully classify porcine gelatin and bovine gelatin based on score plots of first principle component (PC1) and second principle component (PC2). The loading plot analysis showed that variable of tR32 and m/z32 contributed for the separation of both gelatins.
 Conclusion: The chromatograms of LC-MS/MS combined with PCA offered reliable method for differentiation between porcine and bovine gelatins. The developed method could be extended for halal authentication of food and pharmaceutical products via detection of porcine gelatin, non-halal gelatin.

Highlights

  • Gelatin, a mixture of polypeptides obtained from hydrolysis of collagen with high molecular weight (MW), is commonly used in the food industry because of its gelling and thickening properties and pharmaceutical industry to prepare hard and soft capsule shells as well as in cosmetics products [1,2,3]

  • The Muslim societies following certain scholars of thought did not allow the consumption of any products containing porcine gelatine (PG) and considered PG as non-halal materials [5], while bovine gelatine (BG) carrying prion proteins is associated with certain diseases like bovine spongiform encephalopathy [6]

  • The previous study reported that profiling of peptides in gelatin samples was accomplished within 120 min

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Summary

Introduction

A mixture of polypeptides obtained from hydrolysis of collagen with high molecular weight (MW), is commonly used in the food industry because of its gelling and thickening properties and pharmaceutical industry to prepare hard and soft capsule shells as well as in cosmetics products [1,2,3]. High MW of gelatines affected gel strength and viscosity of products [4]. Numerous sources for extraction of collagen have been reported, most ones are porcine, bovine, and fish. The Muslim societies following certain scholars of thought did not allow the consumption of any products containing porcine gelatine (PG) and considered PG as non-halal materials [5], while bovine gelatine (BG) carrying prion proteins is associated with certain diseases like bovine spongiform encephalopathy [6]. There is a need to develop reliable methods for identifying gelatine sources in any products

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