An evaluation of Fourier transforms infrared spectroscopy method for the classification and discrimination of bovine, porcine and fish gelatins

Çebi, Nur; Durak, M. Zeki; Toker, Ömer Said; Sağdıç, Osman; Arıcı, Muhammet

doi:10.1016/j.foodchem.2015.06.065

Cited by 176 publications

(110 citation statements)

References 17 publications

(27 reference statements)

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“…Such methods are infrared spectroscopy coupled with chemometrics of Principal Component Analysis (PCA) for differentiation of porcine and bovine gelatins (Hashim et al, 2010) and those with fish gelatine (Cebi et al, 2016), high performance liquid chromatography coupled with fluorescence detector and chemometrics of PCA (Nemati et al, 2004;Raraswati et al, 2013) and with some types of mass-spectrometer detectors (Zhang et al, 2009;Yilmaz et al, 2013), electrophoretic analysis (Hermanto et al, 2013), Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) combined with PCA (Azira et al, 2014), Enzyme-Linked Immuno-Sorbent Assay (ELISA) (Doi et al, 2009;Venien and Levieux, 2005), conventional method using calcium phosphate precipitation test (Hidaka and Liu, 2003) and Polymerase Chain Reaction (PCR) (Demirhan et al, 2012;Cai et al, 2012). The PCR is an ideal technique to be used for fat and sensitive detection of porcine DNA in gelatin due to the higher stability of DNA compared to protein (Aida et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Real-Time Polymerase Chain Reaction for Halal Authentication of Gelatin in Soft Candy

Sepminarti¹,

Sudjadi²,

Wardani³

et al. 2015

Asian J. of Biochemistry

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Currently, along with the development of science and technology, the diversification of food products occurs in the market. Food products can contain non-halal components like porcine gelatine. One of food suspected to use gelatine is soft candy. Gelatin can be made from pork or beef or other animal. The presence of porcine gelatine in any food products is not allowed for Moslem community, therefore an analytical method offering reliable results must be developed. This study is intended to use Real-Time Polymerase Chain Reaction (RT-PCR) for analysis of porcine gelatine in soft candy. Isolation of DNA was performed with mitochondrial DNA Isolation Kit K280-50 (Bio-Vision). The DNA was analyzed by RT-PCR using primer D-Loop 318. Analysis for the primer specificity was performed on fresh tissue (pig, cows, chickens, goats and rats) and gelatin sources (beef, pigs and catfish). Primer D-loop318 can amplify porcine DNA at the optimum temperature 61.4°C. Repeatability test demonstrated amplification of all positive response samples containing porcine DNA in serial dilution of 10000-1 pg). The Coefficient of Variation (CV) is 6.32%. The repeatability test was also performed on soft candy 100% having CV of 1.06%. The commercial soft candy samples evaluated do not contain porcine DNA.

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Section: Introductionmentioning

confidence: 99%

Real-Time Polymerase Chain Reaction for Halal Authentication of Gelatin in Soft Candy

Sepminarti¹,

Sudjadi²,

Wardani³

et al. 2015

Asian J. of Biochemistry

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“…Moreover it is not sufficient to differentiate gelatin species in mixtures (Cebi et al, 2016). Like FTIR, ELISA method requires proper quality and threshold concentration of gelatin species to have sufficient differentiation between bovine, porcine, and fish.…”

Section: Discussionmentioning

confidence: 99%

“…1313-11124 cm -1 spectral range provides to separate bovine and porcine gelatins from each other. The results indicate that classification of bovine, porcine and piscine gelatins are achieved with 100 % accuracy (Cebi et al, 2016). …”

mentioning

confidence: 89%

“…The obtained spectrums of bovine and porcine gelatins can be found very similar using 4000-650 cm -1 resolution. Cebi et al (2016) studied to differentiate porcine, bovine and fish gelatins by ATR-FTIR. They found that even though all kind of gelatin spectrums are similar, fish gelatin can be separated from bovine and porcine gelatin in 1100-1000 cm -1 spectral range.…”

Section: Fourier Transmission Infrared Spectroscopy (Ftir)mentioning

confidence: 99%

“…They found that even though all kind of gelatin spectrums are similar, fish gelatin can be separated from bovine and porcine gelatin in 1100-1000 cm -1 spectral range. While the concentrations of gelatin content in the solutions increase, the intensities of Amide I and II bands improve (Cebi et al, 2016). To classify bovine and porcine gelatins, Amide III band becomes important.…”

Section: Fourier Transmission Infrared Spectroscopy (Ftir)mentioning

confidence: 99%

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Origin Determination and Differentiation of Gelatin Species of Bovine, Porcine, and Piscine through Analytical Methods

Eryılmaz

Işık

Demircan

et al. 2017

Turkish JAF Sci.Tech.

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Gelatin origin determination has been a crucial issue with respect to religion and health concerns. It is necessary to analyze the origin of gelatin with reliable methods to ensure not only consumer choices but also safety and legal requirements such as labeling. There are many analytical methods developed for detection and/or quantification of gelatin from different sources including bovine, porcine and piscine. These analytical methods can be divided into physicochemical, chromatographic, immunochemical, spectroscopic and molecular methods. Moreover, computational methods have been used in some cases consecutively to ensure sensitivity of the analytical methods. Every method has different advantages and limitations due to their own principles, applied food matrix and process conditions of material. The present review intends to give insight into novel analytical methods and perspectives that have been developed to differentiate porcine, bovine and piscine gelatins and to establish their authenticity. Almost every method can be succeeded in origin determination; however, it is a matter of sensitivity in that some researches fail to ensure sufficient differentiation. IntroductionGelatin is a water soluble protein obtained by hydrolysis of collagen to several high molecular weight polypeptides. While the main component of the gelatin is protein (85-92%), it also contains mineral salts and moisture (Baziwane and He, 2003;Schrieber and Gareis, 2007). Gelatin has a great importance in pharmaceutical, cosmetic and especially food industry with its well-known functional properties such as gel formation in jellies, foam formation and stabilization in ice cream, emulsion stabilization in meat products, syneresis stabilization in yogurt (Nhari et al., 2012). Gelatin was produced approximately 326.000 metric tons in 2008 worldwide, and it is estimated to be consumed 395.840 metric tons by the year of 2017 according to Global Industry Analysts, Inc. which is one of the largest and reputed market research companies (Anonymous, 2016).The raw materials used in gelatin production are mainly from bovine and porcine sources: 80% from pig skin, 15% from cattle hide split, the remaining 5 % from bones, fish and other sources (GME, 2016). Gelatin origin determination has been a matter of paramount importance for Muslims, Hindus, Jews, vegetarians and vegans, in that, in Islam and Judaism, porcine derivatives are prohibited to consume, whereas in Hinduism, cow can neither be slaughtered nor consumed. Vegetarians and vegans prefer to eat animal-free foods (Boran et al., 2010;Nhari et al., 2012). Moreover, bovine gelatin has been restricted for human consumption due to Bovine Spongiform Encephalopathy (BSE) outbreak in 1986 in England and other countries (Venien and Levieux, 2005). Therefore, it is necessary to analyze the origin of gelatin with a reliable method. As far as it is concerned; physiochemical, chromatographic, immunochemical, spectroscopic and molecular methods have been developed to determine and differentiate gelatin o...

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Hofmeister Effect‐Assisted One Step Fabrication of Ductile and Strong Gelatin Hydrogels

Huang

Wang

2017

Adv Funct Materials

289

271

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Hydrogels with high strength and ductility are normally prepared from synthetic polymers, and most protein-based hydrogels are soft and brittle. Here, a strong, ductile gelatin hydrogel is prepared by simply soaking a virgin gelatin gel in an ammonium sulfate solution. The polymer chains in the covalent, crosslink-free network can freely move to homogeneously distribute stress, and more importantly, the highly kosmotropic ammonium sulfate ions greatly enhance the hydrophobic interactions and chain bundling within the gelatin gels. As a result, the treated hydrogels have an extraordinary ultimate strength (compressive and tensile strains of over 99% and 500%, respectively, and stresses of 12 and 3 MPa) superior to that of common protein gels. The physical crosslinks introduced by the Hofmeister effect can rapidly absorb energy and sustain large deformations via decrosslinking and dissociation, which result in energy dissipation and antifatigue properties. The effects of the gelatin and (NH 4 ) 2 SO 4 concentrations on the hydrogel mechanics are evaluated, and the possible strengthening mechanism is discussed. The effect of various ions in the Hofmeister series on the gelatin hydrogel is also investigated. Kosmotropic ions enhance the mechanical properties, whereas chaotropic ions soften and dissolve the gel.

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An evaluation of Fourier transforms infrared spectroscopy method for the classification and discrimination of bovine, porcine and fish gelatins

Cited by 176 publications

References 17 publications

Real-Time Polymerase Chain Reaction for Halal Authentication of Gelatin in Soft Candy

Real-Time Polymerase Chain Reaction for Halal Authentication of Gelatin in Soft Candy

Origin Determination and Differentiation of Gelatin Species of Bovine, Porcine, and Piscine through Analytical Methods

Hofmeister Effect‐Assisted One Step Fabrication of Ductile and Strong Gelatin Hydrogels

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