Study on the thermal behavior of casein under nitrogen and air atmosphere by means of the TG-FTIR technique

Mocanu, Anca Mihaela; Moldoveanu, Costel; Odochian, Lucia; Păiuş, Cristina; Apostolescu, Nicolae; Neculau, R.

doi:10.1016/j.tca.2012.07.031

Cited by 64 publications

(27 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fourier transform–infrared (FT‐IR) analysis as a classic physical technique has been widely used to show chemical characteristics of organic molecules, for instance, to evidence those typical chemical groups and bonds in the molecules. The combination of TG and FT‐IR analysis can be used to investigate the thermal degradation mechanism of polymers or to detect the gaseous species eliminated by thermal degradation of casein . Confocal laser scanning microscopy (CLSM) analysis is a more intuitive analysis for some microstructural characteristics, and can be used to investigate the targets clearly and directly.…”

Section: Introductionmentioning

confidence: 99%

Caseinate–gelatin and caseinate‐hydrolyzed gelatin composites formed via transglutaminase: chemical and functional properties

Luo

Zhao

2014

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

Caseinate–gelatin and caseinate‐hydrolyzed gelatin composites formed via transglutaminase: chemical and functional properties

Luo

Zhao

2014

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

“…Casein includes four individual gene product components denoted αs1-, αs2-, β- and κ-casein, which differ in primary structure and type and degree of post-translational modification [5]. These four casein types are essentially different in their molecular weights as follows: αs1-casein (MW = 23 KD, ~38.49%), αs2-casein (MW 25KD, ~10.06%), β-casein (MW 24KD, ~38.74%), κ-casein (MW19KD, ~12.57%) [6]. The main physiological role of casein in the milk system was widely accepted to be a source of amino acids required by growth of the neonate.…”

Section: Introductionmentioning

confidence: 99%

Characterization of casein hydrolysates derived from enzymatic hydrolysis

Wang

Feng

et al. 2013

Chemistry Central Journal

View full text Add to dashboard Cite

BackgroundCasein is the main proteinaceous component of milk and has made us interest due to its wide applications in the food, drug, and cosmetic industries as well as to its importance as an investigation material for elucidating essential questions regarding the protein chemistry. Enzymatic hydrolysis is an important method commonly used in the modification of protein structure in order to enhance the functional properties of proteins. The relationship between enzymatic hydrolysis and structure change of casein need to make more study.ResultsDuring hydrolysis, degree of hydrolysis in the casein hydrolysates increased rapidly in the initial 20 minutes, reached a plateau after 45 minutes, and then kept relative constant for the rest of the hydrolysis. The relative percentage of the released peptides with molecular weight of over 50 kD significantly decreased with hydrolyzation, while those with MW of 30–50 kD and below 20 kD increased significantly. The contents of a-helix and β-turn in the hydrolysates increased compared to the original casein. Moreover, the molecular flexibilities of the casein hydrolysates, estimated by the ratio of α-helix to β-structure, were lower than that of original casein protein.ConclusionsThe significant changes in molecular weight distribution and structure characteristics of casein hydrolysates were found compared to the control sample. This change should be the basis of enhancement of functional properties.

show abstract

“…It can be seen from Figure (a) that the casein exhibits two stages of degradation process under N 2 atmosphere. The first stage before 250 °C corresponds to the degradation of small side groups and the release of physically retained water . The second stage of decomposition occurs after 250 °C corresponds to the breakage of main chains of casein, with 23.4% char residues left at 700 °C.…”

Section: Resultsmentioning

confidence: 99%

The preparation of fully bio‐based flame retardant poly(lactic acid) composites containing casein

Zhang

Jin

Chen

et al. 2018

J of Applied Polymer Sci

View full text Add to dashboard Cite

In this work, a bio‐based flame retardant, casein, was incorporated into poly(lactic acid) (PLA) matrix by melt compounding in order to improve the fire resistance and sustain the biodegradable character of PLA simultaneously. The fire performance of PLA composites was evaluated by limiting oxygen index, UL‐94 vertical burning, and cone calorimeter tests, respectively. The results indicated that the introduction of 20% casein increased the limiting oxygen index value of PLA composites from 20.0% to 32.2%, upgraded the UL‐94 rating from no rating to V‐0, and decreased the peak heat release rate from 779 to 639 kW/m2. The decomposition products of PLA composites were analyzed by Fourier transform infrared, and the morphology of the char after combustion was observed by scanning electron microscopy. It was suggested that casein took effects in both gas phase by releasing non‐flammable gases (such as NH3 and H2O) and condensed phase by the formation of protective char layers. However, the presence of casein in PLA induced an unavoidable deterioration in the mechanical performance. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2018, 135, 46599.

show abstract

Study on the thermal behavior of casein under nitrogen and air atmosphere by means of the TG-FTIR technique

Cited by 64 publications

References 29 publications

Caseinate–gelatin and caseinate‐hydrolyzed gelatin composites formed via transglutaminase: chemical and functional properties

Caseinate–gelatin and caseinate‐hydrolyzed gelatin composites formed via transglutaminase: chemical and functional properties

Characterization of casein hydrolysates derived from enzymatic hydrolysis

The preparation of fully bio‐based flame retardant poly(lactic acid) composites containing casein

Contact Info

Product

Resources

About