Reducing the antigenicity of milk whey protein using acid proteinases from Monascus pilosus

Lakshman, P.L.N.; Toyokawa, Yoichi; Tachibana, Sanro; Toyama, Hirohide; Taira, Toki; Yasuda, Masaaki

doi:10.1016/j.procbio.2010.11.014

Cited by 14 publications

(6 citation statements)

References 20 publications

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“…On the one hand, proteolysis using various enzymes or microbial proteinases, also in combination with heat denaturation, has been widely applied (Nakamura et al 1993;Kim et al 2007;El Mecherfi et al 2011); the reduction in BLG IgE immunoreactivity in the hydrolysates by in vitro test was also demonstrated (Izquierdo et al 2008;Shi et al 2014). Many hydrolytic processes were carried out using mixed protein substrates, which made the process kinetics and peptide source identification rather complicated (Lakshman et al 2011). In order to contain allergen risk for whey protein based foods, several analytical methods and laboratory immune assays have been proposed for the identification of allergenic proteins and their peptides (Monaci and Visconti 2010;Monaci and Visconti 2012) resulting in an ongoing update of allergen databases (Sircar et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Reduction of whey protein concentrate antigenicity by using a combined enzymatic digestion and ultrafiltration approach

et al. 2017

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The global interest in saving food resources is leading to recycle wasted-food materials to extract useful nutrients. In dairy industry, the recycling of whey proteins determines their utilization in the healthy-addressed foods, which, however, can cause immunological responses in allergic subjects. In this work, a whey protein concentrate (WPC) was alternatively hydrolyzed with pepsin, papain, trypsin and rennin in order to attenuate or abolish the β-lactoglobulin (BLG) antigenicity. The electrophoretic profiles of both pepsin and papain WPC hydrolysates proved the disappearance of the BLG band, even though a slight antigenicity was still found by ELISA. Pepsin hydrolysates, filtered through a 10-kDa cut-off membrane, did not produce immunological response. A deeper investigation carried out on pepsin digested and ultrafiltered samples by LC-MS/MS showed the disappearance of the immunoreactive BLG-fragment IVTQMKGLDIQKVAGTW. The remaining peptides, partially overlapped to major IgE binding epitopes, were not able to give immunoreactivity response. The combined WPC pepsin digestion with ultrafiltration confirmed to be a user-friendly strategy to reduce markedly the WPC antigenicity. The improvement of this two-steps process could be used to produce novel hypoallergenic infant food formulas.

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Section: Introductionmentioning

confidence: 99%

Reduction of whey protein concentrate antigenicity by using a combined enzymatic digestion and ultrafiltration approach

et al. 2017

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Section: Discussionmentioning

confidence: 99%

“…Since ripening temperature was much lower than appropriate growth for Monascus sp., and cheese surface was coated during ripening to interfere with aeration, this increase was due to proteinases, which had been induced in the solid WPC medium during cultivation, rather than growth of micro-organism during the ripening period. In terms of proteinase from Monascus sp., Lakshman, Toyokawa, et al, 2011) reported that extracellular acid proteinase from M. purpureus and M. pilosus reduced antigenicity of bovine milk whey protein. It is conceivable that M. ruber NBRC 32318 secreted proteinase responsible for whey protein as well during cultivation on WPC medium where whey protein was the major nitrogen source for fungal growth.…”

Section: Discussionmentioning

confidence: 99%

Application of red pigment producing edible fungi for development of a novel type of functional cheese

Kumura

Ohtsuyama

Matsusaki

et al. 2018

J Food Process Preserv

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To develop a novel type of functional cheese, nine strains of edible fungi, Monascus sp. were cultured on whey protein‐based solid medium and screened in terms of secondary metabolite production including red pigments, lovastatin, and citrinin. The amount of these metabolites in culture products depended not only on the strain, but also on the pH and temperature environment. The strain of M. ruber NBRC 32318 was selected because it produced red pigments and lovastatin with negligible amount of citrinin. After incubation at 25°C for 10 days with initial pH condition of 4.0, the culture products were mixed with cheese curds, followed by ripening for 3 months at 11.5°C. Higher level of water‐soluble nitrogen was recognized in the culture products containing cheese compared to control cheese. Practical applications For cheese making, diverse microorganisms have been used. However, there have been limited trials on the development of dairy products using red pigment producing Monascus species used for fermented rice in the Eastern Asia for more than 1,000 years. Using whey protein base solid substrate, we selected suitable Monascus strain and defined the culture condition that provided nephrotoxin citrinin‐free and functional metabolite of lovastatin‐containing culture products, which were mixed with fresh cheese curds for ripening. In the resulting red mold cheese, proteolysis was accelerated with no bitter flavor and rancid. Although further assessments concerning health benefits by animal studies and cheese quality by sensory evaluation are necessary to be commercialized as a novel type of functional cheese, this study provides fundamental information regarding screening of suitable strains with its appropriate culture condition on whey protein solid substrate, focusing on biotechnological, and chemical respects to ensure food safety.

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“…Enzymatic modifications of milk proteins usually result in decreased in vitro antigenic properties, for example, cross-linked whey protein (Villas-Boas et al, 2012), glycated and cross-linked whey protein (Zhang et al, 2016). Other studies also utilized protein hydrolysis or protein hydrolysis followed by protein cross-linking to treat whey protein and found that the antigenicity of whey protein can be decreased by using acid proteinases, alcalase, or alcalase plus TGase (Lakshman et al, 2011;Villas-Boas, Benedé, de Lima Zollner, Netto, & Molina, 2015;Zheng et al, 2008). This study obtained a result inconsistent to these reported works.…”

Section: Secondary Structural Features Of the Modified Productsmentioning

confidence: 99%

“…High-pressure treatment results in change of the epitopic regions of whey proteins and hydrolysates (Kleber, Maier, & Hinrichs, 2007;Peñas, Snel, Floris, Préstamo, & Gomez, 2006). Enzymatic hydrolysis by Alcalase and acid proteinases can reduce the antigenicity of α-lactalbumin and β-lactoglobulin (Lakshman et al, 2011;Zheng, Shen, Bu, & Luo, 2008). Lactic acid fermentation also is suggested to have effect on protein allergenicity (El-Ghaish et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity

Zhang

Wang

Liu

et al. 2016

CyTA - Journal of Food

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(2016) Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced invitro antigenicity, CyTA -Journal of Food, 14:4, 572-577, DOI: 10.1080/19476337.2016 To link to this article: https://doi.org/10. 1080/19476337.2016 In this study, two horseradish peroxidase (HRP)-based modifications were used to treat whey protein isolate (WPI) and skim milk powder (SKMP) at protein concentration of 50 g/L, pH 7.0, and 37°C, via dityrosine formation in protein molecules. When HRP, glucose oxidase, and glucose were used to treat WPI and SKMP, suitable usages of HRP, glucose oxidase, and glucose, and reaction time were selected from single factor trials based on relative dityrosine contents of the modified products. After that, the selected HRP plus the calculated H 2 O 2 were used to treat WPI and SKMP. Electrophoretic analysis demonstrated that the modified products contained some crosslinked proteins with greater molecular weights. Other analyses showed that the modified products had more ordered secondary structure, and higher in vitro α-lactalbumin and β-lactoglobulin antigenicity than the respective substrates. HRP-glucose oxidase-glucose system was more potent than HRP-H 2 O 2 system to enhance in vitro antigenicity of WPI and SKMP.Dos modificaciones de peroxidasa de rábano picante resultan en dos productos proteínicos con estructura secundaria ordenada y una antigenicidad in vitro mejorada RESUMEN En este estudio se utilizaron dos modificaciones de peroxidasa de rábano picante (HRP) para tratar aislado proteínico de lactosuero (WPI) y leche desnatada en polvo (SKMP) con una concentración proteínica de 50 g/L, pH 7,0 y 37°C, mediante formación de ditirosina en moléculas proteínicas. En referencia a HRP, se utilizaron glucosa oxidasa y glucosa para tratar WPI y SKMP, se seleccionaron la utilización adecuada de HRP, glucosa oxidasa y glucosa, además del tiempo de reacción de las pruebas de factor único basadas en los contenidos relativos de ditirosina de los productos modificados. Después, la HRP seleccionada y el H 2 O 2 calculado se utilizaron para tratar WPI y SKMP. El análisis electroforético demostró que los productos modificados contenían algunas proteínas reticuladas con un mayor peso molecular. Otros análisis mostraron que los productos modificados tenían más estructuras secundarias ordenadas, además de una mayor antigenicidad in vitro de lactoalbúmina α y lactoglobulina β que los substratos respectivos. El sistema HRPglucosa oxidasa-glucosa fue más potente que el sistema HRP-H 2 O 2 para mejorar la antigenicidad in vitro de WPI y SKMP. ARTICLE HISTORY

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Reducing the antigenicity of milk whey protein using acid proteinases from Monascus pilosus

Cited by 14 publications

References 20 publications

Reduction of whey protein concentrate antigenicity by using a combined enzymatic digestion and ultrafiltration approach

Reduction of whey protein concentrate antigenicity by using a combined enzymatic digestion and ultrafiltration approach

Application of red pigment producing edible fungi for development of a novel type of functional cheese

Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity

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