Solubilization of myofibrillar proteins in water or low ionic strength media: Classical techniques, basic principles, and novel functionalities

Abstract

The qualitative characteristics of meat products are closely related to the functionality of muscle proteins. Myofibrillar proteins (MPs), comprising approximately 50% of total muscle proteins, are generally considered to be insoluble in solutions of low ionic strength (< 0.2 M), requiring high concentrations of salt (> 0.3 M) for solubilization. These soluble proteins are the ones which determine many functional properties of meat products, including emulsification and thermal gelation. In order to increase the utilization of meat and meat products, many studies have investigated the solubilization of MPs in water or low ionic strength media and determining their functionality. However, there still remains a lack of systematic information on the functional properties of MPs solubilized in this manner. Hence, this review will explore some typical techniques that have been used. The main procedures used for their solubilization, the fundamental principles and their functionalities in water (low ionic strength medium) are comprehensively discussed. In addition, advantages and disadvantages of each technique are summarized. Finally, future considerations are presented to facilitate progress in this new area and to enable water soluble muscle MPs to be utilized as novel meat ingredients in the food industry.

Methods for Extraction of Muscle Proteins from Meat and Fish Using Denaturing and Nondenaturing Solutions

“…Protein Extractability. Solubility is an indicator of protein extractability; indeed, a solubilized protein could be easily extracted into a solution from muscle fibers or myofibrils [9]. e amount of myofibrillar proteins extracted using denaturing and nondenaturing solutions from beef, lamb, chicken, sole, European hake, and sea bass is reported in Figure 2.…”

“…However, it has to be considered that the use of these reagents is regarded as toxic and highly polluting and require proper disposer procedures. Chen et al [9] reported the use of water or low ionic strength media for the extraction and solubilization of myo brillar proteins from skeletal muscle. To the best of our knowledge, no research is available on the comparison of the extraction capacity of denaturing and nondenaturing solutions.…”

l‐histidine improves water retention of heat‐induced gel of chicken breast myofibrillar proteins in low ionic strength solution

“…Thermal gelation of MPs involves partial denaturation of protein followed by irreversible aggregation, which forms a multidimensional network that holds water and thus produces a gel (Sun & Holley, ). It is generally accepted that a high concentration (2% to 3% or >0.3 m ) of sodium chloride (NaCl) is required to solubilise the MPs to form a good gel, improving textural properties and water‐holding capacity (WHC) (Lee et al ., ; Cando et al ., ; Chen et al ., ).…”

Functional protein rich extracts from bovine and porcine hearts using acid or alkali solubilisation and isoelectric precipitation

“…However, many meat by-products are rich in proteins and if processed correctly can be used for the production of extracts with desirable functional properties (Chernukha et al, 2015;Lynch et al, 2018). It is well known that myofibrillar proteins are mainly responsible for the gelling properties of meat products (Chen et al, 2015). The production of protein rich extracts from meat by-products represents a good valorisation opportunity for the meat industry, and at the same time can improve consumer acceptance.…”