Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro

Zhao, Yuan; Sun, Zewei; Zhang, Bo; Wang, T.

doi:10.1080/09540101003758954

Cited by 34 publications

(23 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enzymatic hydrolysis of glycinin and β-conglycinin with tryptic and peptic enzymes showed that, at a low pH, glycinin was denatured and more susceptible to hydrolysis, while β-conglycinin was denatured at higher temperature and became more hydrolyzed in contrast to glycinin, which was not affected. However, the IgG-binding capacity was never completely removed [40,41]. In our research, the immunoreactive proteins were not recognized in only one hydrolysate (SHB HVP), while, in the other two, they were found.…”

Section: Discussioncontrasting

confidence: 56%

Soy Preparations Are Potentially Dangerous Factors in the Course of a Food Allergy

Jędrusek‐Golińska

Piasecka‐Kwiatkowska

Zielińska

et al. 2019

Foods

View full text Add to dashboard Cite

The special properties of soy preparations make them common additives for food production and can be dangerous for sensitive individuals. Our aim was to check consumers’ awareness of potential risks of soy preparations added to numerous food products, depending on respondents’ education, and to evaluate immunoreactive properties of chosen soy preparations. A personal questionnaire was used. Respondents (n = 251) were aged 23–28 years old, lived in Poland, and were graduates or students in their last year of food technology, medicine, and university of technology. The slot blot and Western blotting methods were used to mark immunoreactivity of soy preparations. It was shown that most respondents often or usually read labels of food products they buy. The surveyed indicated protein is the allergenic component in soy. Almost half of them were of the opinion that hydrolysis removes the allergenic properties of soy. Most of the medical students surveyed thought that people allergic to soy may consume products that contain soy preparations. The analytical results indicated that soy preparation contained protein fractions that were immunoreactive with sera of allergenic patients. It was proven that preparations, even hydrolysates, contain immunoreactive proteins that may be the source of hidden allergens, even though they are not recognized as dangerous by well-educated respondents.

show abstract

Section: Discussioncontrasting

confidence: 56%

Soy Preparations Are Potentially Dangerous Factors in the Course of a Food Allergy

Jędrusek‐Golińska

Piasecka‐Kwiatkowska

Zielińska

et al. 2019

Foods

View full text Add to dashboard Cite

show abstract

“…Several researchers have investigated the structure and functional properties changes of SPI, glycinin (11S), and β-conglycinin (7S) during heat treatment [9][10][11][12][13]. Hu et al [14] found that the structure of glycinin was maintained when heated at the temperature range of 20-60 • C. However, heating above 80 • C significantly decreased the content of β-sheets and increased the content of random coils [15,16]. Natarajan et al [17] revealed that the first denaturation temperature of β-soy conglycinin was 65 • C. When the temperature of the protein rose to 75 • C, the content of β-sheet structure no longer increased.…”

Section: Introductionmentioning

confidence: 99%

A Study of Structural Change during In Vitro Digestion of Heated Soy Protein Isolates

Tian

Teng

Zhang

et al. 2019

Foods

View full text Add to dashboard Cite

Use of soy protein isolate (SPI) as the encapsulating material in emulsions is uncommon due to its low solubility and emulsification potential. The aim of this study was to improve these properties of SPI via heat treatment-induced modifications. We modified SPI under various heating conditions and demonstrated the relationship between structure and in vitro digestibility in simulated gastric fluid by means of Sodium Dodecyl Sulphide-Polyacrylamide Gel Electrophoresis (SDS-PAGE) and Raman spectroscopy. It was found that the degree of hydrolysis (DH) of SPI increased and then decreased upon increasing exposure to heat. Different subunits of conglycinin were digested and degraded by pepsin. Heat treatment improved digestion characteristics that would reduce e the unnecessary loss of protein, offering potential for the efficient delivery of nutrients in nanoemulsions. These results could have significant relevance for research groups that are interested in the biological interactions and activity of functional SPI.

show abstract

“…The combination of flavourzyme and pancreatin hydrolysis was the most effective on β ‐hexosaminidase inhibition followed by alcalase and pancreatin, respectively (Figure ). MBPHFP 270 , MBPHA 90 and MBPHP 90 significantly (Zhao et al, ) reduced allergic activity when compared to other groups. The effects of MBPHFP, MBPHA and MBPHP on cell viability were determined using the MTT assay (Figure ).…”

Section: Resultsmentioning

confidence: 94%

“…On the other hand, some legume allergens exhibit very high stability to peptic digestion. For example, soybean β ‐conglycinin was not destroyed after 60 min of pepsin hydrolysis (Astwood et al, ; Zhao et al, ). Ara h 1 is a major allergen found in peanut; in vitro gastric digestion led to rapid breakdown into smaller fragments, but still retained its allergenicity to induce histamine release in basophils (Eiwegger et al, ).…”

Section: Resultsmentioning

confidence: 99%

“…In addition, individual proteases have been used singly to reduce allergenicity such as hydrolysis of glycinin and β ‐conglycinin with pepsin (Zhao, Qin, Sun, Zhang, & Wang, ), peanut with trypsin (Yu et al, ), peanut with chymotrypsin (Yu et al, ), as well as soymeal and soybean with alcalase (Tsumura, Kugimiya, Bando, Hiemori, & Ogawa, ; Wang et al, ). Therefore, we hypothesized that the use of enzyme combinations will be more effective than single enzymes in producing hypoallergenic protein hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Anti-allergic activity of mung bean (Vigna radiata (L.) Wilczek) protein hydrolysates produced by enzymatic hydrolysis using non- gastrointestinal and gastrointestinal enzymes

et al. 2018

View full text Add to dashboard Cite

Mung bean seed is a well-known plant protein consumed in Asian countries but the protein is usually retrieved as a waste product during starch production. This study investigated the anti-allergic property of mung bean protein hydrolysates (MBPH) produced by enzymatic hydrolysis using non-gastrointestinal (non-GI), GI and a combination of non-GI+GI enzymes. The hydrolysates were investigated for any anti-allergic property by detecting the amount of β-hexosaminidase released in RBL-2H3 cells, and complemented with the MTT assay to show cell viability. It was found that MBPH hydrolyzed by a combination of flavourzyme (non-GI enzyme) and pancreatin (GI enzyme) exhibited the highest anti-allergic activity (135.61%), followed by those produced with alcalase, a non-GI enzyme (121.74%) and 80.32% for pancreatin (GI enzyme). Minimal toxicity (<30%) of all hydrolysates on RBL-2H3 cells line was observed. The results suggest that MBPH can potentially serve as a hypoallergenic food ingredient or supplement. Practical applicationsMung bean (Vigna radiata L. (Wilczek)) is also known as "green gram" and it is an excellent source of protein. The major mung bean storage proteins are the globulin, albumin and legumin, which are also referred to as legume allergens. Our study showed that mung bean peptides obtained after enzymatic hydrolysis influenced β-hexosaminidase inhibition without any toxic effect on RBL-2H3 cells. This indicates that mung bean allergenicity can be reduced after enzymatic hydrolysis and the protein hydrolysates could be labelled as a hypoallergic food, ingredient, supplement and/or protein substitute in the formulation of food products. K E Y W O R D Santi-allergic, gastrointestinal enzymes, mung bean protein hydrolysates, non-gastrointestinal enzymes, peptides sequence, RBL-2H3, β-hexosaminidase

show abstract

Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro

Cited by 34 publications

References 30 publications

Soy Preparations Are Potentially Dangerous Factors in the Course of a Food Allergy

Soy Preparations Are Potentially Dangerous Factors in the Course of a Food Allergy

A Study of Structural Change during In Vitro Digestion of Heated Soy Protein Isolates

Anti-allergic activity of mung bean (Vigna radiata (L.) Wilczek) protein hydrolysates produced by enzymatic hydrolysis using non- gastrointestinal and gastrointestinal enzymes

Contact Info

Product

Resources

About