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Peas (Pisum sativum L.) are rich in protein, B vitamins, and dietary fiber, represented by hemicellulose and pectins. In terms of amino acids, pea proteins are as close to the reference protein as possible. The limiting amino acids of pea protein are sulfur-containing, i.e., methionine and cysteine. Peas are also rich in lysine, which is the limiting amino acid for wheat flour. Therefore, products of pea processing can expand the range of commercial high-protein foods, including functional bakery products. The research objective was to develop a technology for functional bread from a mix of wholemeal pea flour and wheat gluten. The study featured baking wheat flour, wheat gluten, wholemeal pea flour of San Cipriano and Vega varieties, dough samples, and ready-made bread. The carbohydrate-amylase complex of flour was studied using an Amilotest AT-97 device. The starch content was determined by the polarimetric method. The spectrophotometric method served to test the flower samples for protein while the Kjeldahl method was applied to the bread samples. The rheological properties of the dough were studied on a Reotest 2 viscometer. The sensory evaluation relied on a panel of experts, and the chemical composition was revealed by calculation and analytically. The wholemeal pea flour had a lower starch gel viscosity compared to the wheat flour sample. A greater amount of flour added during kneading increased the viscosity of the resulting dough. The acidity was rather high: 7.2 and 9.4 degrees for San Cipriano and Vega samples, respectively, and so was the autolytic activity (≤ 80 s). These useful qualities made it possible to reduce the technological process by 115 and 145 min. The resulting bread demonstrated good physical, chemical, and sensory indicators. The high-protein raw materials increased the protein content in bread by 41.9–46.4%, compared to the control sample, which equaled 33.1–34.2% of the recommended daily intake per 100 g of bread. The optimal ratio of wholemeal high-protein pea flour and wheat gluten was 20/80 for the San Cipriano samples and 30/70 for the Vega variety.
Peas (Pisum sativum L.) are rich in protein, B vitamins, and dietary fiber, represented by hemicellulose and pectins. In terms of amino acids, pea proteins are as close to the reference protein as possible. The limiting amino acids of pea protein are sulfur-containing, i.e., methionine and cysteine. Peas are also rich in lysine, which is the limiting amino acid for wheat flour. Therefore, products of pea processing can expand the range of commercial high-protein foods, including functional bakery products. The research objective was to develop a technology for functional bread from a mix of wholemeal pea flour and wheat gluten. The study featured baking wheat flour, wheat gluten, wholemeal pea flour of San Cipriano and Vega varieties, dough samples, and ready-made bread. The carbohydrate-amylase complex of flour was studied using an Amilotest AT-97 device. The starch content was determined by the polarimetric method. The spectrophotometric method served to test the flower samples for protein while the Kjeldahl method was applied to the bread samples. The rheological properties of the dough were studied on a Reotest 2 viscometer. The sensory evaluation relied on a panel of experts, and the chemical composition was revealed by calculation and analytically. The wholemeal pea flour had a lower starch gel viscosity compared to the wheat flour sample. A greater amount of flour added during kneading increased the viscosity of the resulting dough. The acidity was rather high: 7.2 and 9.4 degrees for San Cipriano and Vega samples, respectively, and so was the autolytic activity (≤ 80 s). These useful qualities made it possible to reduce the technological process by 115 and 145 min. The resulting bread demonstrated good physical, chemical, and sensory indicators. The high-protein raw materials increased the protein content in bread by 41.9–46.4%, compared to the control sample, which equaled 33.1–34.2% of the recommended daily intake per 100 g of bread. The optimal ratio of wholemeal high-protein pea flour and wheat gluten was 20/80 for the San Cipriano samples and 30/70 for the Vega variety.
Рассмотрен процесс гидролиза крахмала в семенах гороха при прорастании и в технологических процессах. Цель исследования – количественная оценка процесса гидролиза крахмала в естественных условиях (при прорастании семян), при переваривании его в желудочно-кишечном тракте (ЖКТ) и в результате технологического процесса переработки. Для достижения поставленной цели рассмотрен процесс гидролиза крахмала в семенах гороха при прорастании и в технологических процессах; изучены возможности повышения эффективности гидролиза α-амилазы при использовании её в технологических целях. Обсуждение результатов: на основании проведенных исследований доказано, что в области реальных температур технологических процессов молекула α-амилазы состоит из двух доменов с температурами денатурации (Tdn)3 = 31 °С и (Tdn)8 = 78 °С. При этом величина участка N8 зависит от источника, из которого выделена α-амилаза. В случае прорастания семени гороха ферменты белков (папаин) и крахмалов (α- и β-амилаза) находятся в одном объеме. Так как ферменты имеют белковую природу и α-амилаза синтезируется в процессе прорастания семени, то возможно дополнительное воздействие протеолитического фермента папаина или папаиноподобных структур на α-амилазу, особенно на ту ее часть, которая образует опушку фермента. В результате чего структура α-амилазы изменится – останутся только два домена N3 и N8 с укороченными опушками и куски опушек с центрами активации, которые способны диффундировать интенсивнее, чем в составе макромолекулы α-амилазы, и тем самым ускорить процесс расщепления α-1,4-гликозидных связей амилозы и амилопектина семени. Выводы: на основании исследования физического механизма воздействия папаиноподобных протеолитических ферментов на α-амилазу гороха определены оптимальные условия ограниченного гидролиза на стадии использования эндогенных протеиназ температура должна составлять 40 °С, на стадии использования внешних протеиназ и гидролиза зерен крахмала – до 50-55 °С. Показано, что разрушение третичных структур, например, путем предварительной тепловой обработки α-амилазы, позволит расширить область ограниченного протеолиза. The process of starch hydrolysis in pea seeds during germination and in technological processes is considered. The purpose of the study is to quantify the process of starch hydrolysis under natural conditions (during seed germination), during its digestion in the gastrointestinal tract and as a result of the technological process of processing. To achieve this goal, the process of starch hydrolysis in pea seeds during germination and in technological processes is considered; the possibilities of increasing the efficiency of α-amylase hydrolysis when used for technological purposes were studied. Discussion of the results: based on the studies carried out, it was proved that in the region of real temperatures of technological processes, the α-amylase molecule consists of two domains with denaturation temperatures (Tdn)3 = 31 °C and (Tdn)8 = 78 °C. In this case, the size of the N8 region depends on the source from which α-amylase was isolated. In the case of pea seed germination, the enzymes of proteins (papain) and starches (α- and β-amylase) are in the same volume. Since enzymes are of a protein nature and α-amylase is synthesized during seed germination, an additional effect of the proteolytic enzyme papain or papain-like structures on α-amylase is possible, especially on that part of it that forms the edge of the enzyme. As a result, the structure of α-amylase will change - only two domains N3 and N8 will remain with shortened edges and pieces of edges with activation centers that are able to diffuse more intensively than in the composition of the α-amylase macromolecule, and thereby accelerate the process of cleavage of α-1,4-glycosidic bonds of amylose and amylopectin of the seed. Conclusion: based on the study of the physical mechanism of the action of papain-like proteolytic enzymes on pea α-amylase, the optimal conditions for limited hydrolysis at the stage of using endogenous proteinases, the temperature should be 40 °C, at the stage of using external proteinases and hydrolysis of starch grains - up to 50-55 °C. It has been shown that the destruction of tertiary structures, for example, by preliminary heat treatment of α-amylase, will expand the area of limited proteolysis.
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