Preservation of (−)-Epigallocatechin-3-gallate Antioxidant Properties Loaded in Heat Treated β-Lactoglobulin Nanoparticles

2012 ◽  
Vol 60 (13) ◽  
pp. 3477-3484 ◽  
Author(s):  
Bo Li ◽  
Wenkai Du ◽  
Jianchang Jin ◽  
Qizhen Du
2022 ◽  
Vol 123 ◽  
pp. 107169
Author(s):  
Mirjana Radomirovic ◽  
Simeon Minic ◽  
Dragana Stanic-Vucinic ◽  
Milan Nikolic ◽  
Sam Van Haute ◽  
...  

1986 ◽  
Vol 53 (4) ◽  
pp. 601-613 ◽  
Author(s):  
Mary B. Grufferty ◽  
Patrick F. Fox

SummaryThe report that addition of KI03 (0·1 mm) to milk before ultra high temperature (UHT) treatment induces extensive proteolysis during subsequent storage at 37 °C was confirmed. None was produced by addition of H202 KMn04 or K2Cr207. The pH optimum for KI03-induced proteolysis was between 7·0 and 8·0 and the temperature optimum 37—45 °C. β-Casein was particularly susceptible and the proteolysis pattern was similar to that caused by indigenous alkaline milk proteinase (MPA, plasmin). Addition of plasmin to milk before UHT treatment (140 °C/10 s) caused slight proteolysis during subsequent storage but addition of 0·1 mm-KI03 and plasmin caused extensive proteolysis which was prevented by addition of soyabean trypsin inhibitor, indicating the probable involvement of plasmin in KI03-induced proteolysis in UHT-treated milk. Equally extensive proteolysis occurred in serum protein-free casein micelle systems (SPFCM), with or without KI03, during storage at 37 °C following UHT treatment, indicating a role for whey proteins in KI03-induced proteolysis. Addition of β-lactoglobulin (β-lg) to a SPFCM system inhibited proteolysis, but extensive proteolysis occurred in a SPFCM system containing both β-lg and KI03. MPA-free Na caseinate (prepared by heating at 140 °C for 7 min) underwent extensive proteolysis when treated with plasmin before UHT treatment; proteolysis was inhibited by addition of °-lg to this system and KI03 reversed the inhibitory effect of β-lg. Plasmin proteolysis of isolated αs1-casein was inhibited by denatured β-lg (90 °C/30 min) at a level of 4 mg/ml but not by native β-lg. When denatured in the presence of KI03, β-lg had a lower free SH content than the control and was less inhibitory for plasmin in proteolysis of isolated αsl-casein. The results show that denatured β-lg inhibits plasmin proteolysis of caseins in UHT milk and that inhibition is prevented by KI03. This inhibition may occur via thiol–disulphide interchange, which is prevented if the SH group of ²-lg is oxidized by KI03, thus permitting the stimulatory effect of KI03 on proteolysis in UHT-treated milk.


2020 ◽  
Vol 20 (1) ◽  
pp. 287-298 ◽  
Author(s):  
Aneta Brodziak ◽  
Jolanta Król ◽  
Joanna Barłowska ◽  
Zygmunt Litwińczuk ◽  
Anna Teter ◽  
...  

AbstractThe aim of the study was to compare the content of selected bioactive whey proteins and lipophilic vitamins, which largely determine the bioactive status of milk, in milk obtained from local breeds of cows raised in Poland (Polish Red, White-Backed and Simmental) and Polish Holstein-Friesian cows. Basic chemical composition and content of selected bioactive compounds (β-lactoglobulin, α-lactalbumin, lactoferrin, bovine serum albumin, and vitamins: E, A, D3 and β-carotene) in 550 milk samples were analysed. The milk produced by local breeds proved to be a more valuable source of whey proteins and lipophilic vitamins than that of the Polish Holstein-Friesians. It was distinguished by its content of all bioactive compounds, including those with antioxidant properties, i.e. vitamins E, A and D3 and β-lactoglobulin, and antimicrobial properties, mainly lactoferrin. Therefore, the milk of cows of local breeds should be considered a valuable material for processing, especially at the level of the farm or small local processing plant, to produce products that are richer in health-promoting compounds. The promotion of milk from local breeds can therefore be an opportunity for the farms that raise them.


1994 ◽  
Vol 3 (5) ◽  
pp. 473-479
Author(s):  
Tuomo Tupasela ◽  
Heikki Koskinen ◽  
Pirkko Antila

Whey is a by-product of cheesemaking. Whey dry matter contains mainly lactose, but also valuable whey proteins. The aim of this study was to develop improvements to whey protein membrane isolation processes. In our trials CaCl2 -added, pH-adjusted and heat-treated wheys were found to have MF (microfiltration) permeate fluxes about 30% higher than in untreated MF whey. The total solids and protein content of the MF permeates decreased compared to the original wheys. UF (ultrafiltration) trials were conducted using MF whey to compare it with centrifugally separated whey. The MF whey consistently maintained an UF flux about 1.5 to 2.5 times higher than that of the separated whey. Differently treated MF whey UF permeate fluxes also showed a difference. With CaCl2 addition, pH adjustment and heat treatment, the UF permeate fluxes were about 20 to 40% higher than when only MF was used. The total solids content decreased in each trial. The protein content of the UF concentrate also decreased compared to the MF permeate. The (β-lg (β-lactoglobulin) and α-la (α-lactalbumin) content was almost the same in UF concentrates as in MF permeates.


1977 ◽  
Vol 40 (12) ◽  
pp. 857-862 ◽  
Author(s):  
LANA S. WECKBACH ◽  
B. E. LANGLOIS

Grade A raw milk which had initial psychrotrophic counts of less than 103/ml was inoculated with an antibiotic-resistant Pseudomonas sp. to a final cell concentration of 102, 104, or 106/ml. The inoculated milk was held at 4 C for 14 h and then exposed to the following time-temperature treatments: 72 C for 15 sec, 79 C for 15 sec, 88 C for 10 sec, and 95 C for < 5 sec. An uninoculated raw milk control was handled and analyzed along with inoculated samples. Aliquots of milk were analyzed for marked Pseudomonas sp., total psychrotrophic counts, numbers of Pseudomonas, and for distribution of nitrogen before and after each heat treatment and after storage of non-heat-treated raw milk and heat-treated samples for 7 and 14 days at 7 C. Psychrotrophic counts were significantly affected by heat treatment, initial cell inoculum, days stored, and plating media. Non-casein N, non-casein protein, total albumin, β-lactoglobulin, proteose-peptone, and globulin N were significantly decreased by heat treatment. Non-casein N, non-casein protein, β-lactoglobulin, and proteose-peptone were significantly increased by days of storage.


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