Hydrolysis of whey proteins produces highly complex protein hydrolysates that
can contain hundreds of peptide sequences in which the specific bioactive peptide
represents only a single smaller constituent. The identification of these bioactive
peptides requires intense labor of specialized technicians using sophisticated
purification and characterization techniques. Mass spectrometry (MS) is the preferred analytical method for determining their amino acid sequence once identified
the subfractions of protein hydrolysates containing the bioactive peptides [11]. MS
techniques, when combined with other analytical methodologies such as liquid
chromatography (LC/MS), are widely used to isolate and quantify bioactive peptides derived from protein from food, in the food itself, and biological fluids.
Today, in “functional foods” (designer foods/medicinal and therapeutical foods),
the bioactive peptides derived from milk and whey proteins are included as additives functioning as macro/micro essential nutrients or a non-nutritional component,
or component whose nutritional value is not listed as essential [12].
While some of these effects remain putative, a considerable number of bioactive
peptides received scientific scrutiny and have been validated as beneficial by several laboratories around the world in the face of the growing demand by a highly
diverse group of consumers. Nowadays, there are already several bioactive peptides
derived from milk and whey proteins commercialized internationally and identified
by several authors [13, 14]. These peptides are in the market as additives in various
food products but not all with therapeutic effects approved by regulatory agencies
such as the FDA. This fact is associated with the absence of documentation that
validates its functionality and health benefits or has not undergone clinical validation studies with human volunteers that prove the results obtained in vitro and
in vivo testing with animal models [15].
3 Production of Bioactive Peptides
In the global process of industrial production of peptides, it is worth highlighting
the existence of several stages to achieve a concentrated and purified final formulation before its commercialization [16]. These include the pre-treatment of the
protein solution, protein hydrolysis by control mainly of temperature and pH and
the hydrolytic agent concentration, the separation and purification of bioactive
peptides, and drying in the final stage of the formulation [17].
Fermentation processes with dairy starter cultures, i.e., with lactic acid bacteria
(LAB) and hydrolysis with digestive or microbial proteases, are the most widely
used methodologies for releasing bioactive peptides from the primary sequence of
natural proteins. However, chemical processes using acid and alkaline catalytic
agents and even heat in protein-rich food processing can also release some bioactive
peptides [18].
Bioactive peptides for the food industry, rather than those used in the pharmaceutical industry, cannot be characterized at a high cost; otherwise, their use is not
economically viable [19]. For this reason, large-scale production of bioactive
476
A. F. A. Salvado et al.
can contain hundreds of peptide sequences in which the specific bioactive peptide
represents only a single smaller constituent. The identification of these bioactive
peptides requires intense labor of specialized technicians using sophisticated
purification and characterization techniques. Mass spectrometry (MS) is the preferred analytical method for determining their amino acid sequence once identified
the subfractions of protein hydrolysates containing the bioactive peptides [11]. MS
techniques, when combined with other analytical methodologies such as liquid
chromatography (LC/MS), are widely used to isolate and quantify bioactive peptides derived from protein from food, in the food itself, and biological fluids.
Today, in “functional foods” (designer foods/medicinal and therapeutical foods),
the bioactive peptides derived from milk and whey proteins are included as additives functioning as macro/micro essential nutrients or a non-nutritional component,
or component whose nutritional value is not listed as essential [12].
While some of these effects remain putative, a considerable number of bioactive
peptides received scientific scrutiny and have been validated as beneficial by several laboratories around the world in the face of the growing demand by a highly
diverse group of consumers. Nowadays, there are already several bioactive peptides
derived from milk and whey proteins commercialized internationally and identified
by several authors [13, 14]. These peptides are in the market as additives in various
food products but not all with therapeutic effects approved by regulatory agencies
such as the FDA. This fact is associated with the absence of documentation that
validates its functionality and health benefits or has not undergone clinical validation studies with human volunteers that prove the results obtained in vitro and
in vivo testing with animal models [15].
3 Production of Bioactive Peptides
In the global process of industrial production of peptides, it is worth highlighting
the existence of several stages to achieve a concentrated and purified final formulation before its commercialization [16]. These include the pre-treatment of the
protein solution, protein hydrolysis by control mainly of temperature and pH and
the hydrolytic agent concentration, the separation and purification of bioactive
peptides, and drying in the final stage of the formulation [17].
Fermentation processes with dairy starter cultures, i.e., with lactic acid bacteria
(LAB) and hydrolysis with digestive or microbial proteases, are the most widely
used methodologies for releasing bioactive peptides from the primary sequence of
natural proteins. However, chemical processes using acid and alkaline catalytic
agents and even heat in protein-rich food processing can also release some bioactive
peptides [18].
Bioactive peptides for the food industry, rather than those used in the pharmaceutical industry, cannot be characterized at a high cost; otherwise, their use is not
economically viable [19]. For this reason, large-scale production of bioactive
476
A. F. A. Salvado et al.