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1.
Molecules ; 26(8)2021 Apr 20.
Article in English | MEDLINE | ID: mdl-33924144

ABSTRACT

Australian sweet lupin, the largest legume crop grown in Western Australia, is receiving global attention from the producers of new foods. To understand the effect of protein on cheese yield, lupin milk proteins were separated from the first, second, and third filtrations by cheesecloths. However, proteins from the first and second were analyzed using two-dimensional polyacrylamide gel electrophoresis; then, the isolated proteins associated with cheese production were identified. The research also focused on identifying the optimal method of cheese production based on the coagulation process, temperature, yield, and sensory evaluation. Lupin curds from the two cultivars, Mandelup and PBA Jurien, were produced using vinegar, lemon juice, starter culture, vegetable rennet enzyme as coagulant, as well as curd generated using starter culture and vegetable rennet enzyme. Cow's milk was used as a control. The results indicated that first-time filtration produced better extraction and higher yield of lupin proteins and cheese than the second filtration. A sensory analysis indicated that lupin cheese produced from PBA Jurien lupin milk using vinegar, 7.80% expressed as acetic acid, and ground in 45 °C water, was the most acceptable. The cheeses were examined for their protein, carbohydrates, fat, ash, and moisture contents. The concentration of protein was approximately 27.3% and 20.6%, respectively, in the cheese from PBA Jurien and Mandelup. These results suggest that lupin milk can adequately supply the proteins needed in human diets and, thus, could be used in the production of many existing products that require animal milk as an input.


Subject(s)
Cheese , Fabaceae/chemistry , Milk/chemistry , Plant Proteins/chemistry , Animals , Australia , Caseins/chemistry , Cattle , Chymosin/chemistry , Humans , Milk Proteins/chemistry
2.
Molecules ; 25(14)2020 Jul 16.
Article in English | MEDLINE | ID: mdl-32708569

ABSTRACT

Soybean-based food products are a major source of protein. In the present study, proteins in soybean milk from seeds of the cultivar Bunya (Glycine max) were extracted using the cheesecloth and the centrifuge methods. The milk was produced through mechanical crushing of both whole and split seeds in water. Following separation by either the cheesecloth or centrifuge, proteins were isolated from the soybean milk by using thiourea/urea solubilisation and then separated them using two-dimensional polyacrylamide gel electrophoresis. The isolated proteins were identified by mass spectrometry. A total of 97 spots were identified including 49 that displayed different abundances. Of the two separation techniques, centrifuge separation gave higher protein extraction and more intense protein spots than cheesecloth separation. Eleven of the ß-subunits of ß-conglycinin, three of the α-subunits of ß-conglycinin, and four of the mutant glycinin showed different levels of abundances between separation techniques, which might be related to subsequent cheese quality. Notably, split-seed soybean milk has less allergenic proteins with four α-subunits of ß-conglycinin compared to whole-seed milk with eight of those proteins. The sensory evaluation showed that the cheese produced from split-soybean milk received higher consumer preferences compared to that of whole seed, which could be explained by their proteomic differences. The demonstrated reference map for whole and split-seed soybean milk could be further utilized in the research related to soybean cheesemaking.


Subject(s)
Cheese/analysis , Glycine max/chemistry , Milk/chemistry , Proteomics , Animals , Food Hypersensitivity , Globulins/genetics , Milk/metabolism , Seeds/chemistry , Seeds/genetics , Soybean Proteins/genetics , Glycine max/genetics
3.
Molecules ; 25(8)2020 Apr 13.
Article in English | MEDLINE | ID: mdl-32295067

ABSTRACT

Lupin seeds are rich in proteins and other essential ingredients that can help to improve human health. The protein contents in both whole and split seeds of two lupin cultivars (Mandleup and PBA Jurien) were used to produce the lupin milk using the cheesecloth and centrifuge method. Proteins were extracted from the lupin milk using thiourea/urea solubilization. The proteins were separated by a two-dimensional polyacrylamide gel electrophoresis and then identified with mass spectrometry. A total of 230 protein spots were identified, 60 of which showed differential abundances. The cheesecloth separation showed protein extractability much better than that of the centrifuge method for both the cultivars. The results from this study could offer guidance for future comparative analysis and identification of lupin milk protein and provide effective separation technique to determine specific proteins in the cheese-making process.


Subject(s)
Lupinus/chemistry , Plant Extracts/chemistry , Plant Proteins/analysis , Proteome/metabolism , Seeds/chemistry , Solid Phase Extraction/methods , Electrophoresis, Gel, Two-Dimensional/methods , Lupinus/metabolism , Mass Spectrometry , Plant Extracts/isolation & purification , Plant Proteins/chemistry , Plant Proteins/metabolism , Proteome/chemistry , Proteomics , Seeds/metabolism
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