Introduction

Meat is recognized as a very popular food item worldwide and it is well known as an excellent quality protein source with other nutritional characteristics along with its appealing taste. With the growing rate of the planet's population, the need for food security is rising as well, and to feed this growing population a greater amount of good quality food having proper protein, fat, and other nutrition is required. Meanwhile, increased environmental footprint awareness plays a significant role in meat analogues supply for the sustainable and transparent food security of the planet. Animal is the solitary bioresource of meat protein and with rapid population growth, the need for meat protein is also increasing. Various data show that the demand will be magnified near to twice by 2050 [1]. To cater to this high meat protein demand, more animal husbandry is required, but the scarcity of land, water, and other environmental factors constrain the growth of animal husbandry due to which meat price indices are continuously increasing, which makes it difficult in the adequate meat accessibility to the people of lower and lower-middle class group countries (Fig. 1). One of the major environmental concerns is also emission of greenhouse gases (carbon dioxide (CO2), methane (CH4) and nitrous oxide (N2O)) from livestock farming (Fig. 2). In the search for an alternative to conventional animal-derived meat protein, nowadays search for alternative protein has become very common, where plant-based meat analogues (PBMA) emerge as the most popular alternative [2]. Meat analogues are generally mock meat substitutes or imitation meat having all the structural and nutritional characteristics of meat along with the aesthetic qualities of specific types of meats [3]. The PBMA seems to be a wholesome solution to cater to all the following issues raised by animal meat such as high pricing of meat protein, religious concerns (halal/jhatka), greenhouse gas emissions from animal husbandry farms, and loss of biodiversity due to higher animal husbandry [4]. As people are becoming more aware of the importance of their health and environment, they are inclined to the PBMA [5]. Over a long period, scientists and researchers investigated different protein texturizing techniques to convert different plant-based proteins into meat analogues. The first attempt at texturing plant protein into meat analogues was made with soy protein isolate in 1970 where isolated soy protein was added to increase the protein level and enhance the texture of meatball, wiener, and hamburger compositions [3]. Nowadays to develop PBMA several protein sources like—soy protein, gluten, different legumes, vegetables, seeds, lentils, beans, peas, etc. are used as the main raw material. Plant-based proteins are converted to meat analogues mainly with the extrusion technology process and with time advancements in processing techniques resulting in mimic meats comprising enhanced nutritional qualities and functional meat-like characteristics [6, 7]. Based on moisture content PBMA is mainly two types—low moisture meat analogues that contain moisture content of less than 30% and high moisture content meat analogues that contain moisture content between 50 and 70% [8]. Low moisture content meat analogues are also known as texturized vegetable protein, and it is used with the combination of real meat to get a meat-like texture and qualities. High moisture content meat analogues are gaining rapid attention in the industries for their applicability as a whole meat substitute. In animal meat, one of the major concerns is high saturated fat content and high cholesterol content, which causes severe cardiovascular diseases and also other major problems such as hypertension, weight gain, etc. [9]. Different processed animal meat products like curing meat and smoking meat raised concerns about their possible carcinogenic phenomena [10]. PBMA—as a natural plant-based protein is a primary ingredient that imparts several vitamins, minerals, proteins, fibres, anti-oxidants, and polyphenols into our body system that keeps our body healthy [11]. In animal meat, there is a chance to transfer various animal-borne diseases into the body system through meat intake and this might cause serious illness in the human body, but the chances of similar issues from PBMA are low [2]. Nowadays from a healthy life point of view and different religious concerns, people are moving towards a vegan diet and for them, PBMA gives an excellent option to get meat-like taste, mouthfeel, and nutritional functionalities without meat intake.

Fig. 1
figure 1

Changes in the different meat prices as per FAO meat price index. (Data Source: OECD-FAO Agricultural Outlook 2022–2031)

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Fig. 2
figure 2

Meat Greenhouse gas emissions intensity per region

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This paper collects and synthetizes the available research on plant-based meat analogues. The Scopus database was used to retrieve the data. The Scopus database was searched for data in January 2023 using the following keywords: (plant proteins) AND (meat analogues OR meat alternatives OR meat formulation OR ingredients OR functionalities). The PRISMA guidelines (www.prisma-statement.org) were used for data refinement where the total number of primary searches was 806; after filtering the documents, the final number of relevant articles was 403. For this review, all titles, and abstracts of identified articles were screened by the authors and the full text was evaluated if appropriate. Additional inclusion criteria were that the article should deal specifically with meat analogues using plant proteins, not other sources. No temporal restrictions were applied to the literature search. Figure 3 reported the bibliometric analysis of plant protein-based meat analogues, data were captured from Scopus.

Fig. 3
figure 3

The bibliometric analysis of plant protein-based meat analogues

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Meat analogues

Potential ingredients for meat analogues

Figures 4 and 5 portray the necessary ingredients needed for develo** PBMA. The specific amount of all the ingredients with accurate formulation will result in the desired mock meat characteristics of the developed meat analogues.

Fig. 4
figure 4

Graphical representation of different ingredients used in PBMA preparation

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Fig. 5
figure 5

Different ingredients and their functions used in PBMA-formulation

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Plant proteins as promising ingredients

Proteins are made up of amino acids that are critical for human health and are mostly used in food processing to create a variety of nutritious diets [12]. Dietary proteins are the basic source of nitrogen, and amino acids serve as construction blocks for human tissue while also requiring physiological enzymes to regulate chemical and biological reactions for the body to function properly [13]. Plant-based proteins (PBP) have gained popularity recently because of the change in particular dietary habits that most people are adopting. There are several PBP, for instance, soy protein, legume-based protein, wheat gluten, and various seed proteins are used in PBMA-develo** (Fig. 6). Soy protein is extensively used in PBMA-develo** due to its low cost, easily available, and superior functionalities. The reason for the increased focus on PBP is a recently discovered link between the intake of animal protein products and an enlarged hazard of chronic diseases [14]. Another reason for the increased prominence of PBP is the environmental issues caused by livestock agriculture. Recently, PBP was used as meat analogues in local and international markets. The global market for meat substitutes was $4,532.6 M in 2019 and is expected to reach $7,106.7 M in 2025. Between 2020 and 2025, this is with an estimated CAGR of 7.7%. Market trends and category development are influenced by regional variations; with 70% each, Europe and North America dominated the global market in 2019. Additionally, Asia Pacific held a significant share and is anticipated to grow at the fastest CAGR. The Middle East and Africa have a small share of the market, so they could be underexplored.

Fig. 6
figure 6

Classification of different types of protein used in the preparation of plant-based meat analogues

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Usage of soy protein for meat analogues

Soybeans are rich in protein and contain water-soluble and insoluble proteins. Based on the dry weight of mature raw seeds, soybeans have ~ 8.5–13% moisture, ~ 33–40% protein, ~ 3–4% ash, ~ 18–20% fats, and ~ 9–12% fibers [15]. The variation in protein content may be due to cultivation environments, variety, and genetic modification. Soy protein has been utilized to create fabricated soy products, including soy protein isolates, soy protein concentrates, and soy-deflated flour [135]. Soluble proteins or aggregates migrate to the interface of the air–water, which reduces surface tension and keeps air bubbles in suspension, thus slowing the rate of coalescence. Recently, Zhu et al. [156] found that wet-separated pea protein had better foaming properties than that of wet-separated one, and the resulting dough of meat analogues was more solid-like with higher hardness. FCI of proteins from bell pepper seed, quinoa seed mung bean, hyacinth bean seed was reported to be 152.67–354.33, 58.37–78.62, 62.50, and 30.33–123.33, respectively, and the corresponding FSI was 113.33 to 119.00, 54.54–83.55 95.20%, and 27.32–84.44%, respectively [135, 136, 140]. The foam foaming property generally depends on protein solubility, as proteins with high solubility can diffuse easily and rapidly into the air–water interface for air bubble encapsulation, leading to improvements in FCI and FSI [136]. At present, the effect of the foaming property of plant protein on the quality of meat analogues is still lacking.

Gel forming ability of plant proteins

Gel-forming ability is the aggregation of unfolded proteins to form a 3D microstructure network through intermolecular interactions [143]. It is usually measured by the least gelation concentration (LGC) and gel strength (GS). Gel property is the foremost indicator for evaluating the usage of plant proteins in meat analogues. The gel-forming ability of plant proteins from diverse sources is significantly different. For example, when the concentration of mung bean protein is above 13%, it can form a gel [157]. The LGC of hyacinth bean seed and soy protein isolate is 16% and 15%, respectively [140, 143]. However, the LGC of rice protein isolate must reach more than 35% to make a gel [143]. The gel strength of plant proteins is significantly lesser as compared to proteins of meat flesh [155]. The nature and concentration of protein, environmental factors, and processing conditions are important influencing factors in the creation of gel [143]. Liu et al. [136] found that the neutral and alkaline environments in mung bean proteins were favoured to denature and unfold the proteins and expose the more embedded functional groups under heating, which improved the molecular interactions and gel texture.

Film forming property of plant proteins

Water vapour permeability (WVP) and tensile strength (TS) are the two critical parameters of film. The WVP of the film made from quinoa seeds, sesame seeds, and mung bean seeds were reported to be 1.98–4.76, 10.87–13.57, and 10.76 10−7g Pa−1 h−1 m−1, respectively and their TS were 1.88–4.28, 8.29, and 3.33 MPa, respectively [144,145,146]. The film-forming property can be influenced by the properties of proteins used for preparing the film such as solubility, the hydrophobic/hydrophilic nature, purity, free volume, molecular mobility, and flexibility [144,145,146]. Yang et al. [158] used proteins from distiller-dried grains to prepare film incorporating green tea extracts and reported that the film can be utilized as an anti-oxidative packaging material for pork meat. Plant protein film has the potential to be used for packaging meat analogues. However, there are few relevant reports at present.

Binding property of plant proteins

In meat analogues processing, adding flavor (such as vanillin) and nutrients (such as flavonoids) is easy to achieve. Protein contains a variety of functional groups, which can interact with flavonoids, vanillin, quercetin, rutin, and other compounds through covalent (Schiff bases) and non-covalent (hydrogen bond, hydrophobic interaction, electrostatic force, etc.). Therefore, on one side, proteins can bond flavonoids and anthocyanins reversibly and irreversibly to form complexes and improve their stability. Jia et al. [147] stated that 7S/11S soybean protein can bind quercetin and rutin. The binding constant was 0.03–97.43 105 L M−1, and the binding site was 0.77–1.65. Soybean protein isolate was reported to be able to bind to flavonoids, with a binding constant of 0.23–143.88 105 L M−1 and a binding site of 0.98–1.75 [147]. On the other hand, proteins can interact with vanillin, aldehydes, and ketones to cause the loss of flavor intensity or so-called flavor fade. Temthawee et al. [148] found that the binding of vanillin to coconut protein was enthalpy driven, the binding constant was 40.1–122.2 105 L M−1, and the binding site was 0.81–1.48 [148]. The interactions between the compounds and proteins can be influenced by several factors relevant to the functional groups of these compounds and the changes in the protein conformation [147, 148].

Extrusion ability of plant proteins

Extrusion is the most widely used technology to process plant proteins to meat analogues with rich fibrous structures and good springiness like real animal meat. Specific mechanical energy (SME) and fibrous degree (FD) are the most important indicators of extruded meat analogues. SME refers to the mechanical energy absorbed per unit mass of extrudates, which translates into the extent of molecular collapse or disintegration of materials during extrusion. The FD was computed by dividing the crosswise shear force lengthways, which can be used for characterizing the anisotropic structure in the extrudate. Soy protein concentrate, pea protein isolate, and peanut protein powder have been used for extruding into meat analogues [149, 150, 159]. Their SMEs were 1029.03, 985.07660.56–1135.67 kJ, respectively, while TD is 1.03, 1.30, and 1.33, respectively. SME is majorly connected with the contents of moisture and fat, and energy input intensity [151, 160]. Fatty acids, especially those with low unsaturation degrees, have a lubrication effect, which reduces die pressure and contributes to the smooth flow of protein melt in the extruder barrel, consequently reducing the mechanical energy consumption during extrusion processing. TD is related to the protein nature, functional additive, and operation conditions. Dou et al. [149] reported that adding Gums promoted the fibre formation.

Influence of processing on functionalities of proteins

The functional qualities of plant protein depend on processing procedures intrinsic to the chosen extraction processes, modification, heat treatment, etc. in addition to elements inherent to the protein and environmental conditions [161]. These treatments will cause desired and unwanted changes in the functional characteristics of proteins (Table 6). In this way, it is very necessary to explain the changes in protein functional properties during processing operations and the corresponding results from the perspective of chemistry and physics.

Effect of physical operations on proteins

Effect of high-pressure homogenization, micro-fluidization, and high hydrostatic pressure treatments

In recent years, high-pressure processing has received attention from both industry and academia and has smeared extensively to amend the functional characteristics of plant proteins. During the high-pressure homogenization process, a continuous flowing fluid or suspension is pushed through a narrow gap that is usually controlled by a valve, which leads to high turbulence and shear stress [85]. Micro-streams with high velocity are generated in the micro-fluidization process, as fluid is accelerated into a Y-type interaction chamber by a high-pressure pump, resulting in high shear and impact forces [152]. In high-pressure homogenization, the fluid circulates in the equipment for a period, whereas the fluid passes through the micro-fluidization device in a fleeting time. As for the high hydrostatic pressure treatment, protein isolate or concentrate is placed in a closed ultra-high-pressure container statically, and water is used as the medium to apply a pressure of 200 ~ 600 MPa usually, which is higher than that (typically in a range of 50–200 MPa) in the micro-fluidization and high hydrostatic pressure treatment [165].

Those pressure effects can induce significant modifications of the functional characteristics of plant proteins (Table 6). Regardless of the method and protein source, moderate pressure (50 ~ 200 MPa) treatment can significantly increase the solubility, emulsification property, foaming property, and gel-forming ability. The improvement of solubility can be attributed to the fact that moderate pressure treatment causes the proper dissociation of the quaternary structure, the diminution of protein particle size, and the swelling of the molecule, leading to an increase in solvent-protein interaction [166]. At the same time, moderate pressure treatment unfolds the protein conformational structure, which led to the disclosure of internal hydrophobic groups and the increase of molecular flexibility, thereby enhancing the intermolecular interactions and protein adsorption at the air–water and oil–water interfaces. Therefore, the foaming property, gel-forming ability, emulsification property, and film-forming property are improved. However, excessive pressure (> 300 MPa) treatment induces the creation of bigger protein aggregates, causing declined solubility and other functional characteristics [162,163,133, 143]. The exposure of hydrophobic groups induced by sonication facilitates the diffusion of protein molecules toward air–water or oil–water interfaces and their adsorption on them. Consequently, the foaming property and emulsification properties are remarkably improved on the condition that the structural changes have been balanced in terms of hydrophilicity and hydrophobicity after sonication [143, 153]. Although the hydrophobicity increases, the foaming property, and emulsification properties may decrease due to the decline in the solubility under the excessive sonication [133, 143]. Under moderate sonication conditions, gel-forming ability film-forming property, and extrudability increase, as indicated in the increase of TS while the decrease of WVP, a decrease of LGC, and an increase of TD, correspondingly [143, 144, 168]. The reason might be assigned to the partial unfolding of their three-dimensional molecular structures, resulting in the exposing of hydrophobic and/or sulfhydryl groups, thereby promoting the formation of more interconnected gel networks due to the presence of more junction zone per particle [143, 168].

Effect of water bath incubation, autoclaving, ohmic heating, microwave heating, and extrusion cooking

Heat treatment is a traditional processing method, including water bath incubation, autoclaving, ohmic heating, microwave heating, extrusion cooking, etc. These heating methods have distinct characteristics. For example, water bath incubation is easy to apply in industrial production. Autoclaving can make the material temperature reach over 100 ℃. Ohmic and microwave heating can quickly generate heat by utilizing the friction movement of polar molecules and the conductivity of ions, respectively, thus shortening the heating time. Extrusion cooking combines the functions of mixing, sterilization, heating, drying, and forming. Heat treatment affects the functional characteristics of plant proteins.

Generally, the solubility of protein decreased after thermal treatment, which is mainly due to the creation of insoluble aggregates [139, 165]. However, Hu et al. [166] reported that extrusion increased the solubility of Baijiu vinasse proteins and suggested that the changes in solubility during extrusion are primarily due to an interplay of shearing, temperature, and pressure, which led to the formation of the small particle size, porous structure, and air voids of proteins. Water bath incubation, ohmic heating, and extrusion cooking affect the foaming property and emulsification properties of proteins, which rely on the operation conditions. The changes in the foaming property and emulsification properties can be explained by the changes in solubility and conformational structure [139, 166]. After water bath incubation (90 °C), the gel-forming ability of cowpea protein isolates decreased. It could be due to the formation of aggregates that had a lower ability to realign and form the protein network [165]. Guo et al. [169] examined that the binding capacities of soy protein isolate for HxAc and HpAc decreased as the temperature increased in the protein aqueous solution. It was related to the formation of an additional hydrophobic surface because of the thermal denaturation (unfolding) of protein, which declined the affinity of primary binding sites. Whereas the binding capacities of soy protein isolate for LiFo, LiAc, linalool, and geraniol increased, the reason was that heat treatment increased the number of lower affinity secondary binding sites on the hydrophobic surface of soy protein isolate. TD showed a tendency to significantly decrease after autoclaving [170]. The result was thought to be related to the movement and redistribution of moisture caused by the vacuum-heat treatment process.

Effect of atmospheric cold plasma, ultraviolet radiation

In recent years, non-thermal technology, a potential alternative to traditional thermal processing for microbial inactivation to extend the shelf life, including atmospheric cold plasma and ultraviolet irradiation, etc., were pertained to improve the functional characteristics of plant proteins regarding solubility, gel-forming ability, film-forming properties, and foaming property [145, 172,

Data availability

There is no data available for this article.

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Funding

Open Access funding enabled and organized by Projekt DEAL. The open access publishing fee is covered under the agreement between the DEAL Consortium and Springer and Springer Nature upon acceptance due to Shahida Anusha Siddiqui being affiliated with the Technical University of Munich.

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Authors and Affiliations

  1. Campus Straubing for Biotechnology and Sustainability, Technical University of Munich, Essigberg 3, 94315, Straubing, Germany

    Shahida Anusha Siddiqui

  2. German Institute of Food Technologies (DIL e.V.), Prof.-Von-Klitzing Str. 7, 49610 D, Quakenbrück, Germany

    Shahida Anusha Siddiqui

  3. Department of Food Technology, Faculty of Agriculture, Benha University, Qaluobia, 13736, Egypt

    Ibrahim Khalifa & Mohamed K. Morsy

  4. College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province, 430070, People’s Republic of China

    Tao Yin & Ramy M. Khoder

  5. National R & D Branch Center for Conventional Freshwater Fish Processing, Wuhan, Hubei Province, 430070, People’s Republic of China

    Tao Yin

  6. Key Laboratory of Environment Correlative Dietology, Ministry of Education, Hubei Province, Wuhan, People’s Republic of China

    Tao Yin

  7. Mirmadan Mohanlal Government Polytechnic, West Bengal State Council of Technical Education, Plassey, Nadia, 741156, India

    Molla Salauddin

  8. Department of Food Processing Technology, Karunya Institute of Technology and Sciences, Coimbatore, 641114, India

    Wasiya Farzana

  9. AICRP (PHET), University of Agricultural Sciences, Gandhi Krishi Vignana Kendra, Bangalore, 560 065, India

    Wasiya Farzana

  10. School of Engineering, University of Guelph, Guelph, ON, N1G 2W1, Canada

    Sonu Sharma

  11. Department of Food Science and Technology, School of Food and Agricultural Sciences, University of Management and Technology, Lahore, 54000, Pakistan

    Nauman Khalid

  12. College of Health Sciences, Abu Dhabi University, 59911, Abu Dhabi, United Arab Emirates

    Nauman Khalid

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  1. Shahida Anusha Siddiqui
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  2. Ibrahim Khalifa
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  3. Tao Yin
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  5. Ramy M. Khoder
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  6. Molla Salauddin
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  7. Wasiya Farzana
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Contributions

Shahida Anusha Siddiqui—Conceptualization, Methodology, Writing—Original Draft, Writing—Review and Editing, Validation, Formal Analysis, Investigation, Software, Data Curation, Visualization, Resources, Project administration, Funding Acquisition, Supervision. Ibrahim Khalifa—Writing—Original Draft, Resources, Visualization. Tao Yin—Writing—Original Draft, Visualization. Mohamed K. Morsy—Writing—Original Draft, Visualization. Ramy M. Khoder—Writing—Original Draft, Visualization. Molla Salauddin—Writing—Original Draft, Visualization. Wasiya Farzana—Writing—Original Draft, Visualization. Sonu Sharma—Writing—Review and Editing, Visualization, Validation. Nauman Khalid—Conceptualization, Review and Editing, Supervision.

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Correspondence to Shahida Anusha Siddiqui.

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Siddiqui, S.A., Khalifa, I., Yin, T. et al. Valorization of plant proteins for meat analogues design—a comprehensive review. Eur Food Res Technol (2024). https://doi.org/10.1007/s00217-024-04565-1

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