Mass spectrometric analysis of enzymatic digestion of denatured collagen for identification of collagen type

Zhang, Guifeng; Sun, Aimei; Li, Weijun; Liu, Tao; Su, Zhiguo

doi:10.1016/j.chroma.2006.03.039

Cited by 33 publications

(28 citation statements)

References 15 publications

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“…That is why they are used in combination with mass spectroscopy or chemometry (Zhang et al, 2006). Methods other than computational ones which involve laboratory practices have to be confirmed and have repeatability under laboratory collaborative studies to assure both accuracy and quality of the results (Azilawati et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

“…Cheng et al (2012), referring to previous applications of the technique, have used collagen marker peptides to differentiate bovine, porcine, donkey (hide) gelatins and tortoise shell glue, and deer-horn glue (Nemati et al, 2004;Zhang et al, 2006). They have coupled the method with PCA analysis to have uniqueness.…”

Section: Uplc/q-tof-ms Methods Coupledmentioning

confidence: 99%

“…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%

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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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Section: Discussionmentioning

confidence: 99%

Section: Uplc/q-tof-ms Methods Coupledmentioning

confidence: 99%

Section: High Performance Liquid Chromatography With Mass Spectroscopmentioning

confidence: 99%

See 1 more Smart Citation

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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“…While it is true that the triple helix structure of collagen usually prevents or dramatically slows proteolysis, the collagen structure is disrupted by heat which allows protease digestion (Bruckner and Prockop 1981). Specific recent examples of proteolysis of collagen by trypsin are given in Yuanlong et al (2012) and Zhang et al (2006). An example of proteolysis of collagen by subtilisin is given in Vasileva-Tonkova For each time point, two 1-mL filtered portions from the hydrolysis assay were added to weighed vials.…”

Section: Protein Measurement Of Extractsmentioning

confidence: 99%

Proteolysis of meat and bone meal to increase utilisation

Piazza

García

2014

Anim. Prod. Sci.

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Abstract. Meat and bone meal (MBM), an important by-product of the meat industry, is the ground, rendered remainder of farm animals after removal of the hide and meat. Most protein in MBM is insoluble, which limits its usefulness. Defatted, milled porcine MBM was subjected to saturating amounts of trypsin, a selective protease, and subtilisin, a protease with broad selectivity. Samples were withdrawn over a 48-h time course of hydrolysis and filtered to remove insoluble material. The rate at which the MBM protein was converted to a soluble form was equivalent for both proteases. Over the time course, trypsin generated fewer free amino groups than did subtilisin, and at a specified time, the molecular weight (MW) of the soluble trypsin hydrolysate was higher than that of the subtilisin hydrolysate. Assay of amino group formation showed that the proteases were still active even after soluble protein generation had ceased. The hydrolysates are useful for a variety of food and non-food uses. The hydrolysates were tested for flocculation activity in an ongoing effort to find sources for renewable flocculant. Kaolin flocculant activity was observed with the soluble fraction obtained before hydrolysis of MBM and also observed with the relatively high MW hydrolysates from short treatment with trypsin and subtilisin. Low MW fractions obtained from by subtilisin treatment at 30-48 h also showed kaolin-settling ability, probably through a coagulation or charge neutralisation process.

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“…These methods are very specific, but also very expensive and require many sample handling steps [25]. Other options which enable scientists to determine the molar ratios of particular collagen types employ the separation of the peptide mixture produced by enzymatic digestion by various separation methods, such as CE, SDS-PAGE or HPLC [26] and their detection by UV, mass spectrometry (MS) or tandem mass spectrometry (MS/MS) [1,27].…”

Section: Introductionmentioning

confidence: 99%

Determination and Quantification of Collagen Types in Tissues Using HPLC-MS/MS

Pataridis¹,

Eckhardt²,

Mikulíková³

et al. 2009

CAC

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Abstract:A method for the determination and quantification of collagen types (I -V) using sample pretreatment has been developed. This work is a continuation of our previous work dealing with the determination of collagen types I and III in tissues [1].The tissues (rat placenta and porcine cartilage) were firstly homogenized with a pestle in a grinding mortar with liquid nitrogen. Collagens were isolated from these tissues by cleavage with pepsin. The collagen types of interest were then precipitated successively by adding sodium chloride. For quantitation purposes, the sample preparation protocol has been simplified to the one-step precipitation of collagens from a solution containing 4.5 mol/L of sodium chloride. The fractions were fragmented by cyanogen bromide and digested with trypsin. After that, HPLC-MS/MS (high performance liquid chromatography coupled to an ion trap mass spectrometer) analyses of the resulting peptide mixtures (peptide maps) were performed. Based on these analyses, specific (marker) peptides for each of the collagen types were selected. The marker peptides were then synthesized and used to identify and quantify the above-mentioned collagen types in tissues using HPLC-MS/MS, and for determining the limits of detection and quantification.The applicability of this method for collagen analysis was demonstrated.

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Mass spectrometric analysis of enzymatic digestion of denatured collagen for identification of collagen type

Cited by 33 publications

References 15 publications

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

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

Proteolysis of meat and bone meal to increase utilisation

Determination and Quantification of Collagen Types in Tissues Using HPLC-MS/MS

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