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Gluten: digestibility

by luciano

Gluten which is a compound formed by gliadin and glutenin which is the basis of baked products (bread and other) is not, as such, assimilable by the intestine but must be reduced to the amino acids components or small series (peptides) of them. The reduction occurs by different enzymes such as trypsin in the stomach, pepsin in the small intestine and other enzymes [1]. In normal health the intestine expels the parts of gluten that are not digested because they are too large to be assimilated. The digestibility of gluten is not only, however, dependent on the “strength of the gluten”, that is on the strength of the different types of bonds that “connect” the proteins of gluten but also on the type of enzymes that hydrolyse “break” the gluten and from the environment in which these processes take place. For example, trypsin in the stomach is activated (ie works), only in an acid environment. Furthermore, all digestive enzymes have the possibility of working better if directly in contact with gluten: something that can only occur in laboratory experiments, since these enzymes will have to “work” on in the stomach and intestines a “complex” of foods and not on gluten [2]. Knowledge of the digestibility of gluten is therefore extremely complex being affected by multiple factors, not least the variability of the conditions of the environment where it occurs (stomach and intestine).

The method of preparation of the finished product should not be overlooked. Indeed the digestibility of gluten, and more specifically, of the finished product is greatly influenced by the preparation method and the ingredients used [3]. Among these a primary role is played by the type of flour and the use of sour dough and / or yeasts. Certainly the use of flours that have little and weak * gluten favor the digestive process but a fundamental role is played by the sourdough (better if associated with very limited quantities of brewer’s yeast). The sourdough with its lactobacilli carries out a strong action of hydrolysis (chopping) of the gluten proteins both directly and by activating the proteases of the flour. Many studies and researches have been devoted to this subject, one in particular:

Protein Digestibility of Cereal Products Iris Joye
Department of Food Science, University of Guelph, Guelph, ON N1G 2W1, Canada; ijoye@uoguelph.ca; Tel.: +1-519-824-4120 (ext. 52470). Published: 8 June 2019
Abstract: Protein digestibility is currently a hot research topic and is of big interest to the food industry. Different scoring methods have been developed to describe protein quality. Cereal protein scores are typically low due to a suboptimal amino acid profile and low protein digestibility. Protein digestibility is a result of both external and internal factors. Examples of external factors are physical inaccessibility due to entrapment in e.g., intact cell structures and the presence of antinutritional factors. The main internal factors are the amino acid sequence of the proteins and protein folding and crosslinking. Processing of food is generally designed to increase the overall digestibility through affecting these external and internal factors. However, with proteins, processing may eventually also lead to a decrease in digestibility. In this review, protein digestion and digestibility are discussed with emphasis on the proteins of (pseudo)cereals.”