Use of Mass Spectrometry to Profile Peptides in Whey Protein Isolate Medium Fermented by Lactobacillus helveticus LH-2 and Lactobacillus acidophilus La-5

Caseinomacropeptide (CMP) is released from bovine kappa-casein after rennet treatment and is one of the major peptides in whey protein isolate. CMP has in vitro anti-inflammatory and antibacterial activities. CMP has two major amino acid sequences with different modifications, including glycosylation, phosphorylation and oxidation. However, no previous work has provided a comprehensive profile of intact CMP. Full characterization of CMP composition and structure is essential to understand the bioactivity of CMP. In this study, we developed a top-down glycopeptidomics-based analytical method to profile CMP and CMP-derived peptides using Orbitrap mass spectrometry combined with nano-liquid chromatography with electron-transfer/higher-energy collision dissociation. The liquid chromatography–tandem mass spectrometry (LC–MS/MS) spectra of CMPs were annotated to confirm peptide sequence, glycan composition and other post-translational modifications using automatic data processing. Fifty-one intact CMPs and 159 CMP-derived peptides were identified in four samples (one CMP standard, two commercial CMP products and one whey protein isolate). Overall, this novel approach provides comprehensive characterization of CMP and CMP-derived peptides and glycopeptides, and it can be applied in future studies of product quality, digestive survival and bioactivity.

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Functional and Technological Potential of Whey Protein Isolate in Production of Milk Beverages Fermented by New Strains of Lactobacillus helveticus

Applied Sciences ◽

10.3390/app10207089 ◽

2020 ◽

Vol 10 (20) ◽

pp. 7089

Author(s):

Katarzyna Skrzypczak ◽

Waldemar Gustaw ◽

Emilia Fornal ◽

Anna Kononiuk ◽

Monika Michalak-Majewska ◽

...

Keyword(s):

Whey Protein ◽

Water Solution ◽

Fermented Milk ◽

Whey Protein Isolate ◽

Protein Isolate ◽

Lactobacillus Helveticus ◽

Biologically Active ◽

Protein Nitrogen ◽

Technological Potential ◽

Wide Range

With their desired functional and technological properties, whey protein preparations are used in the food industry. In turn, lactic acid fermentation may contribute to release of a wide range of biologically active peptides (BAPs) (known also as bioactive peptides or biopeptides) from whey and milk proteins, which are perceived as potential therapeutic tools and important constituents of personalized food suitable for prevention of many civilization and diet-related diseases. Therefore, the objective of this study was to determine the suitability of new Lb. helveticus strains for production of fermented milk beverages (drinking type) supplemented with whey protein isolate (WPI). Liquid chromatography-high-resolution mass spectrometry (LC-HRMS) was employed to assess if WPI (water solution) might be a suitable precursor for BAPs produced by selected strains of Lb. helveticus. In order to identify the bioactivities of the peptides generated in WPI hydrolysates, the procedures indicated in databases were used. The fermented products differed from each other in some texture parameters, the content of protein, total nitrogen, and non-protein nitrogen, and the proteolysis index, which was dependent on the strain. Strain B734 was found to exhibit technological potential for development of new health-oriented fermented milk beverages with characteristics of functional food. Additionally, it proved to be able to release a wide range of BAPs from WPI with antioxidative, antibacterial, and immuno- and cyto-modulatory effects, as well as ACE (angiotensin-converting enzyme) inhibitory and antihypertensive activities.

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The Viability of Lactobacillus acidophilus Microencapsulated in Ca-Alginate Whey Protein Isolate Glycerol Bead Using Emulsification Method

International Journal of Current Microbiology and Applied Sciences ◽

10.20546/ijcmas.2017.607.164 ◽

2017 ◽

Vol 6 (7) ◽

pp. 1373-1380

Author(s):

Gisthananda Madyasta ◽

Pur wadi ◽

Imam Thohari ◽

Abdul Manab

Keyword(s):

Whey Protein ◽

Lactobacillus Acidophilus ◽

Whey Protein Isolate ◽

Protein Isolate ◽

Ca Alginate

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Whey protein isolate-lignin complexes as encapsulating agents for enhanced survival during spray drying, storage, and in vitro gastrointestinal passage of Lactobacillus reuteri KUB-AC5

LWT ◽

10.1016/j.lwt.2021.111725 ◽

2021 ◽

pp. 111725

Author(s):

Phùng Diệp Huy Vũ ◽

Akkaratch Rodklongtan ◽

Pakamon Chitprasert

Keyword(s):

Whey Protein ◽

Spray Drying ◽

Lactobacillus Reuteri ◽

Whey Protein Isolate ◽

Protein Isolate

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Fabrication of Oil-in-Water Emulsions with Whey Protein Isolate–Puerarin Composites: Environmental Stability and Interfacial Behavior

Foods ◽

10.3390/foods10040705 ◽

2021 ◽

Vol 10 (4) ◽

pp. 705

Author(s):

Yejun Zhong ◽

Jincheng Zhao ◽

Taotao Dai ◽

Jiangping Ye ◽

Jianyong Wu ◽

...

Keyword(s):

Interfacial Tension ◽

Whey Protein ◽

Surface Protein ◽

Whey Protein Isolate ◽

Protein Isolate ◽

Environmental Stability ◽

Dependent Manner ◽

Emulsifying Properties ◽

Interfacial Behavior ◽

Concentration Dependent Manner

Protein–polyphenol interactions influence emulsifying properties in both directions. Puerarin (PUE) is an isoflavone that can promote the formation of heat-set gels with whey protein isolate (WPI) through hydrogen bonding. We examined whether PUE improves the emulsifying properties of WPI and the stabilities of the emulsions. We found that forming composites with PUE improves the emulsifying properties of WPI in a concentration-dependent manner. The optimal concentration is 0.5%, which is the highest PUE concentration that can be solubilized in water. The PUE not only decreased the droplet size of the emulsions, but also increased the surface charge by forming composites with the WPI. A 21 day storage test also showed that the maximum PUE concentration improved the emulsion stability the most. A PUE concentration of 0.5% improved the stability of the WPI emulsions against environmental stress, especially thermal treatment. Surface protein loads indicated more protein was adsorbed to the oil droplets, resulting in less interfacial WPI concentration due to an increase in specific surface areas. The use of PUE also decreased the interfacial tension of WPI at the oil–water interface. To conclude, PUE improves the emulsifying activity, storage, and environmental stability of WPI emulsions. This result might be related to the decreased interfacial tension of WPI–PUE composites.

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Effect of thermally induced denaturation on molecular interaction-response relationships of whey protein isolate based films and coatings

Progress in Organic Coatings ◽

10.1016/j.porgcoat.2016.11.032 ◽

2017 ◽

Vol 104 ◽

pp. 161-172 ◽

Cited By ~ 13

Author(s):

Markus Schmid ◽

Sandra Pröls ◽

Daniel M. Kainz ◽

Felicia Hammann ◽

Uwe Grupa

Keyword(s):

Whey Protein ◽

Molecular Interaction ◽

Whey Protein Isolate ◽

Protein Isolate ◽

Thermally Induced

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Whey Protein Isolate Microgel Properties Tuned by Crosslinking with Organic Acids to Achieve Stabilization of Pickering Emulsions

Foods ◽

10.3390/foods10061296 ◽

2021 ◽

Vol 10 (6) ◽

pp. 1296

Author(s):

Jéssica Thaís do Prado Silva ◽

João Vitor Munari Benetti ◽

Taís Téo de Barros Alexandrino ◽

Odilio Benedito Garrido Assis ◽

Jolet de Ruiter ◽

...

Keyword(s):

Contact Angle ◽

Organic Acids ◽

Whey Protein ◽

Physical Stability ◽

Whey Protein Isolate ◽

Protein Isolate ◽

Pickering Emulsions ◽

Food Grade ◽

Oil Water ◽

Coffee Oil

Whey protein isolate (WPI) can be used effectively to produce food-grade particles for stabilizing Pickering emulsions. In the present study, crosslinking of WPI microgels using organic acids (tannic and citric acids) is proposed to improve their functionality in emulsions containing roasted coffee oil. It was demonstrated that crosslinking of WPI by organic acids reduces the microgels’ size from ≈1850 nm to 185 nm and increases their contact angle compared to conventional WPI microgels, achieving values as high as 60°. This led to the higher physical stability of Pickering emulsions: the higher contact angle and smaller particle size of acid-crosslinked microgels contribute to the formation of a thinner layer of particles on the oil/water (O/W) interface that is located mostly in the water phase, thus forming an effective barrier against droplet coalescence. Particularly, emulsions stabilized by tannic acid-crosslinked WPI microgels presented neither creaming nor sedimentation up to 7 days of storage. The present work demonstrates that the functionality of these crosslinked WPI microgels can be tweaked considerably, which is an asset compared to other food-grade particles that mostly need to be used as such to comply with the clean-label policy. In addition, the applications of these particles for an emulsion are much more diverse as of the starting material.

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