Improving the Aromatic Profile of Plant-Based Meat Alternatives: Effect of Myoglobin Addition on Volatiles

Abstract

Market demand for palatable plant-based meat alternatives is on the rise. One of the challenges is formulating products with sensorial characteristics similar to conventional meat. In this study, the effect of myoglobin on the aromatic profile of plant-based meat alternatives was assessed. Plant-based burgers were made with soy-textured protein, supplemented with three levels of myoglobin (0, 0.5 and 1.0%, the latter two mimicking endogenous myoglobin levels in meat), and grilled for 12 min at 250 °C. To evaluate the aromatic profile of the compounds, raw and grilled samples were subjected to headspace solid-phase microextraction (HS-SPME) followed by gas chromatography-mass spectrometry (GC-MS). Principal component analysis (PCA) analysis was then performed to visualize the interaction between grilling and myoglobin addition, and the effect exerted on the resulting aromatic profile. Myoglobin significantly affected several classes of volatile compounds, either by itself or in conjunction with grilling. A notable increase in aldehydes and a decrease in hydrocarbons were noted after adding myoglobin. As expected, an increase in pyrazines was observed after grilling. The results suggest myoglobin positively influences the aromatic profile of plant-based meat alternatives, contributing to a profile closer to the one of conventional meat.

Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties

“…The identified and quantified volatile compounds in pulses include aromatic hydrocarbons, aldehydes, alkanes/alkenes, alcohols, ketones, acids, esters (without lactones), pyrazines, terpenes, furans, and lactones (Devaere et al, 2022;Karolkowski et al, 2021). In the present study, the effects of sequential hydrolysis of LPI by…”

“…The identified and quantified volatile compounds in pulses include aromatic hydrocarbons, aldehydes, alkanes/alkenes, alcohols, ketones, acids, esters (without lactones), pyrazines, terpenes, furans, and lactones (Devaere et al., 2022 ; Karolkowski et al., 2021 ). In the present study, the effects of sequential hydrolysis of LPI by Alcalase and Flavourzyme, cross‐linking of LPH by MTGase, grafting through the Maillard reaction (MLPH), and combined cross‐linking and Maillard conjugation (MLPHC) were investigated.…”

Improving Protein Expression, Stability, and Function with ProteinMPNN

“…We first applied our design strategy to the model protein myoglobin. Myoglobin binds heme to carry oxygen in mammalian muscle tissue, and has relevance in clinical applications as a biomarker, as a versatile platform for biocatalytic applications, − and in food science as an ingredient in artificial meat products. − Current efforts to create more stable variants of myoglobin have focused on the stabilization of the globin fold through stapling with cysteine-reactive noncanonical amino acids. , …”

Improving protein expression, stability, and function with ProteinMPNN

“…We first applied our design strategy to the model protein myoglobin. Myoglobin binds heme to carry oxygen in mammalian muscle tissue 16 and has relevance in clinical applications as a biomarker 17 , as a versatile platform for biocatalytic applications [18][19][20] , and in food science as an ingredient in artificial meat products [21][22][23] . Current efforts to create more stable variants of myoglobin have focused on the stabilization of the globin fold through stapling with cysteine-reactive noncanonical amino acids.…”