Mass spectrometric detection of marker peptides in tryptic digests of gelatin: A new method to differentiate between bovine and porcine gelatin

Zhang, Guifeng; Liu, Tao; Wang, Qian; Chen, Li; Lei, Jiandu; Luo, Jian; Ma, Guanghui; Su, Zhiguo

doi:10.1016/j.foodhyd.2009.03.010

Cited by 100 publications

(78 citation statements)

References 17 publications

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“…It is unclear at this time whether these Hyp residues might be 3-Hyp or 4-Hyp or whether their appearance represents a lapse in fidelity of at least one of these enzymes or whether such sites represent previously unknown substrates at which hydroxylation serves specific functions. Supportive of our findings, Pro hydroxylation in an Gly-Pro-Ala motif has previously been reported for bovinederived collagen I (78). It should be noted that although X-position 4-Hyp residues are thought to destabilize triple helices when in the context of Gly-Hyp-Pro triplets (79), X-position 4-Hyp residues do not necessarily destabilize the triple helix when in the context of triplets that lack Pro or Hyp in the Y-position (80).…”

Section: Comparison Of the Col1 Ptms Of Bovine Placental ␣1(v) And Husupporting

confidence: 93%

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

Yang

Park

Davis

et al. 2012

Journal of Biological Chemistry

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Background: ␣1(V) is an extensively modified collagen chain important in disease. Results: Comprehensive mapping of ␣1(V) post-translational modifications reveals unexpectedly large numbers of X-position hydroxyprolines in Gly-X-Y amino acid triplets. Conclusion:The unexpected abundance of X-position hydroxyprolines suggests a mechanism for differential modification of collagen properties. Significance: Positions, numbers, and occupancy of modified sites can provide insights into ␣1(V) biological properties.

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Section: Comparison Of the Col1 Ptms Of Bovine Placental ␣1(v) And Husupporting

confidence: 93%

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

Yang

Park

Davis

et al. 2012

Journal of Biological Chemistry

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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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“…Gelatins of different origin are first digested with trypsin. Then, specific sequences of peptides are formed, which are further identified with a type of mass spectrometry (MS) or a chemometric technique (Zhang et al, 2009;Zhang et al, 2006). Many HPLC techniques have been investigated by researchers in recent years to reach a cost and time-efficient and highly sensitive and accurate method of differentiation.…”

Section: High Performance Liquid Chromatography With Mass Spectroscopmentioning

confidence: 99%

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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Mass spectrometric detection of marker peptides in tryptic digests of gelatin: A new method to differentiate between bovine and porcine gelatin

Cited by 100 publications

References 17 publications

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

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

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