An improved method for isolation of β-lactoglobulin

Lozano, José Manuel; Giraldo, Gloria I.; Romero, Carmen M.

doi:10.1016/j.idairyj.2007.05.003

Cited by 50 publications

(26 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Isolation and quantification of native whey proteins through RP-HPLC involves precipitation at low pH that can induce protein denaturation or produce low yields (Lozano, Giraldo, & Romero, 2008). Therefore, the influence of MEF on the extent of whey protein denaturation was also assessed by Native-PAGE.…”

Section: Whey Protein Denaturationmentioning

confidence: 99%

Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

View full text Add to dashboard Cite

Proteins are one of the food constituents most affected by heating, and some of the changes involve their unfolding, denaturation and gelation. Ohmic heating has often been claimed to improve the quality of foodstuffs due to its uniform heating and (putative) presence of a moderate electric field (MEF). However, this is still subject to discussion, so it is important to determine the effect of ohmic heating and of its MEF upon food constituents. Hence, the aim of this work was to evaluate the effects of MEF on denaturation, aggregation and viscoelastic properties of whey protein isolate (WPI), and compare them with those obtained via conventional heating under identical treatment conditions (up to 30 min at 85 o C). Results have shown that MEF interferes with whey protein unfolding and aggregation pathways at relatively high temperatures. MEF treatments have resulted in WPI solutions possessing more 8 and 10% of native Lactoglobulin and Lactalbumin, respectively, after 30 s of heating at 85 o C, when compared with a conventional heating method. Protein aggregates from MEF-treated WPI solutions presented a maximum increase in size of 78 nm, whereas conventional heating produced an increase of 86 nm. Unlike in conventional heating, aggregation of whey proteins during MEF was not sufficiently strong to form a true elastic gel network, since decreases in both storage and loss modulus were observed following MEF treatment. Our results suggest that MEF may provide a novel method for production of a whey protein matrix with distinctive gel-forming properties.2

show abstract

Section: Whey Protein Denaturationmentioning

confidence: 99%

Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Before the isolation process of β-Lg from whey, all whey samples centrifuged at 15333 x g, 4ºC for 15 min as a pretreatment procedure to remove fat and particulates (Lozano, Giraldo, & Romero, 2008). β-Lg content of whey in the beginning of isolation process and differences between protein content and effectiveness of isolation techniques were measured by using high-performance liquid chromatography (HPLC) (Shimadzu LC-20AT, Japan) which was performed on a Zorbax 300SB-C18 4.6 x 250mm (Agilent, USA) with a diode array detector.…”

Section: Physicochemical Analysismentioning

confidence: 99%

“…The method used by Lozano et al (2008) were modified and used for the isolation of β-Lg by anion exchange chromatography. The pH of free particulates was adjusted to 3.0 using concentrated phosphoric acid (85%, H 3 PO 4, Sigma, Germany) .…”

Section: Isolation Of β-Lg By Anion Exchange Chromatographymentioning

confidence: 99%

See 1 more Smart Citation

Comparison of Different Methods for Beta Lactoglobulin Isolation

Özer¹,

Öner²

2018

Food Health

View full text Add to dashboard Cite

Abstract:The aim of this study was to introduce a simple, high efficient and less expensive method for isolation of β-Lg from whey. Anion exchange chromatography, pepsin enzyme treatment and ultrafiltration tecniques were preferred for isolation process to compare differences. In addition to, centrifuge ultrafiltration techniques were using for the first time for isolation of β-Lg from whey. Physicochemical analysis of whey samples indicated that protein and β-Lg content in whey samples changed from 0.07 to 0.8% and 0.24 to 0.29 g/L, respectively. Treatment with the use of pepsin enzyme, anion exchanges chromatography and ultrafiltration techniques, resulted to β-Lg of 1.43, 6.56 and 43.59 folds respectively. Our results showed that ultrafiltration techniques are rapid and efficient that allows high protein yield and has advantages over other methods since it preserves the native structure of β-Lg. Additionally, when the enzymatic hydrolysis was used together with ultrafiltration technique, it was found efficient and pure than the enzymatic hydrolysis together with dialyse membrane. Also this study concluded that pepsin enzyme treatment and anion exchange chromatography are economic methods but they are not efficient enough and very time consuming. However isolation efficiency can be increased the use of isolation methods together.

show abstract

“…Hahn et al (1998) developed a fractionation scheme for IgG, lactoferrin and lactoperoxidase based on various cation exchangers. Lozano et al (2008) employed cation-exchange chromatography only as a final purification step after isolating BLG from bovine whey using precipitation. Doultani et al (2004) developed a cation-exchange column chromatography process that used selective elution to fractionate proteins from whey.…”

Section: Introductionmentioning

confidence: 99%

Purification of the two major proteins from whey concentrate using a cation‐exchange selective adsorption process

El‐Sayed

Chase

2009

Biotechnology Progress

View full text Add to dashboard Cite

The packed-bed adsorption and elution of aqueous solutions of whey concentrate powders were investigated at pH 3.7 using a 5-mL SP Sepharose FF column to separate and isolate two major proteins namely, alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) from these solutions. ALA displaced and eluted BLG from the column in a pure form. Pure ALA could then be eluted with good recovery. A novel consecutive two-stage separation process was developed to separate ALA and BLG from whey concentrate mixtures. Almost all of the BLG in the feed was recovered, with 78% being recovered at 95% purity and a further 20% at 86% purity. In addition, 67% of ALA was recovered, 48% at 54% purity and 19% at 60% purity.

show abstract

An improved method for isolation of β-lactoglobulin

Cited by 50 publications

References 25 publications

Influence of moderate electric fields on gelation of whey protein isolate

Influence of moderate electric fields on gelation of whey protein isolate

Comparison of Different Methods for Beta Lactoglobulin Isolation

Purification of the two major proteins from whey concentrate using a cation‐exchange selective adsorption process

Contact Info

Product

Resources

About