2022
DOI: 10.1016/j.foodchem.2021.130820
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A simple method for enrichment of β-lactoglobulin from bovine milk whey involving selective hydrolysis by two fungal protease preparations

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Cited by 7 publications
(3 citation statements)
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“…Pepsin hydrolysis of BLG (at pH 3, 37 °C), coupled with ultrafiltration (10 kDa MWCO), was found to reduce the BLG antigenicity in WPC [48]. More recently, two commercially available, food-grade fungal proteases (fungal protease 31,000 and fungal protease 60,000), were used to hydrolyze whey proteins in casein whey [49]. After incubation at pH 4 and 45 °C for 5 h, BLG remained intact, resulting in a selectively enriched high concentration BLG fraction, which could be recovered by ultrafiltration (10 kDa MWCO).…”
Section: Sizementioning
confidence: 99%
“…Pepsin hydrolysis of BLG (at pH 3, 37 °C), coupled with ultrafiltration (10 kDa MWCO), was found to reduce the BLG antigenicity in WPC [48]. More recently, two commercially available, food-grade fungal proteases (fungal protease 31,000 and fungal protease 60,000), were used to hydrolyze whey proteins in casein whey [49]. After incubation at pH 4 and 45 °C for 5 h, BLG remained intact, resulting in a selectively enriched high concentration BLG fraction, which could be recovered by ultrafiltration (10 kDa MWCO).…”
Section: Sizementioning
confidence: 99%
“…Acid proteases from Aspergillus flavus , Aspergillus oryzae , Aspergillus niger , Rhizomucor pusillus , Rhizomucor miehei , and Rhizopus species are all used to prepare oriental foods, such as tempeh and koji, and to produce cheese as a substitute for rennet. Important milk clotting enzymes are found in Rhizomucor pusillus , Rhizomucor miehei , Penicillium roqueforti , Penicillium camemberti , and Endothia parasitica ( Mandujano-González et al, 2016 ; Aleksandrina, 2021 ; Ha et al, 2022 ). Mesophilic fungi have been used to release proteolytic enzymes.…”
Section: Application Of Microbial Proteasesmentioning
confidence: 99%
“…β-Lactoglobulin (β-LG, or LG) that exists in the highest content of whey protein is commonly available as a by-product of cheese processing, but it has obtained much more attention for its biological activities [3] , [4] . Its monomer is composed of 162 amino acids with a molecular weight of 18,400 Da, of which the structure contains an α-helix and nine antiparallel β-sheets in a lamellar microstructure [5] .…”
Section: Introductionmentioning
confidence: 99%