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1.
J Food Sci ; 88(1): 28-56, 2023 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-36444520

RESUMEN

The effective food processing to reduce nuts and legumes allergenicity could not be easily and directly concluded from reading a few published reports. Therefore, we conducted a meta-analysis to investigate this issue. A literature search was conducted in eight electronic databases from January 2000 to June 11, 2021. The primary outcome of interest was the allergenicity of processed nuts or legumes determined by enzyme-linked immunosorbent assay from in vitro studies. Data with the standardized mean difference (SMD) of 95% confidence interval (CI) were pooled using a random-effect model by RevMan 5.4 software. Heterogeneity was assessed using Cochran's Q (PQ ) and I2 tests. The search strategy identified 18,793 articles. However, only 61 studies met the inclusion criteria and were included in this meta-analysis. There were 21 and 15 types of respective single and combined food processing treatments analyzed for their effects on reducing allergenicity. In single processing treatment, the extrusion and fermentation had the largest reduction in allergenicity, considering their SMD value, that is, -20.19 (95% CI: -22.22 to -18.17; the certainty of evidence: moderate) and -20.8 (95% CI: -24.10 to -17.50; the certainty of evidence: moderate), respectively. Whereas in the combination, the treatment of fermentation followed by proteolytic hydrolysis showed the most significant reduction (SMD: -53.34; 95% CI: -70.18 to -36.5) and the evidence quality of this treatment was considered moderate. In conclusion, these three food processing methods showed a desirable impact in reducing nuts or legumes allergenicity. PRACTICAL APPLICATION: Nuts and legumes play an essential role as protein sources in food consumption worldwide, but they usually contain allergens. Our study has investigated the food processing methods that effectively reduce their allergenicity by meta-analysis. The result gives valuable information for further laboratory investigation on allergens and can be used by food industries in providing foods from nuts and legumes with lower allergenicity.


Asunto(s)
Fabaceae , Nueces , Nueces/química , Alérgenos/análisis , Verduras , Manipulación de Alimentos/métodos
2.
Molecules ; 26(13)2021 Jun 23.
Artículo en Inglés | MEDLINE | ID: mdl-34201554

RESUMEN

The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from Aspergillus sp.), a temperature of 37 °C, a reaction time of 18 h, pH 8.2, and an E/S ratio of 2%. On the other hand, the best enzymatic conditions for producing peptide hydrolysates with high ACEi activity are through sequential hydrolytic activity by the combination of pepsin-pancreatic, an E/S ratio for each enzyme is 10%, the temperature and reaction time for each proteolysis are 37 °C and 0.74 h, respectively, pH for pepsin is 2.0, whereas for pancreatin it is 7.0. As an underutilized pulse, the studies on the enzymatic hydrolysis of velvet bean proteins in producing ACEi peptides are limited. Conclusively, the activity of soybean-based ACEi peptides is found to depend on their molecular sizes, the amino acid residues, and positions. Hydrophobic amino acids with nonpolar side chains, positively charged, branched, and cyclic or aromatic residues are generally preferred for ACEi peptides.


Asunto(s)
Inhibidores de la Enzima Convertidora de Angiotensina/aislamiento & purificación , Glycine max/metabolismo , Mucuna/metabolismo , Aminoácidos/química , Inhibidores de la Enzima Convertidora de Angiotensina/química , Aspergillus/enzimología , Endopeptidasas/química , Exopeptidasas/química , Globulinas/química , Hidrólisis , Interacciones Hidrofóbicas e Hidrofílicas , Pancreatina/química , Péptido Hidrolasas/química , Péptidos/química , Prolina/química , Proteínas de Soja/química , Temperatura
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