Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams

Luccia, Aldo Di; Picariello, Gianluca; Cacace, Giuseppina; Scaloni, Andrea; Faccia, Michele; Liuzzi, Vania C.; Alviti, G.; Musso, S. Spagna

doi:10.1016/j.meatsci.2004.10.004

Cited by 104 publications

(75 citation statements)

References 47 publications

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“…The quantitative analysis showed that nearly all proteins in the sarcoplasmic fractions of goat meat (978 ng/μl) and pork meat (814 ng/μl) ranged from 24 kDa to 62.5 kDa ( Table 1). The most abundant sarcoplasmic proteins present in the goat meat were probably ascribable, on the basis of their molecular weight and of some works of identification [23][24][25][26][27], to triosephosphate isomerase (26.3 kDa, 157 ng/μl), and fructose-bisphosphate aldolase A (40.9 kDa, 33 ng/μl); in addition, another protein of 38.2 kDa (147 ng/μl) was observed.…”

Section: Results and Discussion A Qualitative/quantitative Analysis mentioning

confidence: 95%

“…2c), Table 2) and ranged from 24 kDa to 62.5 kDa of Molecular Weight (MW). Previous works [23][24][25][26] identified these proteins as myokinase (24-24.96 kDa), triosephosphate isomerase (26.3-27.18 kDa), carbonic anhydrase (29.64-31.3 kDa), glyceraldheyde-3-phosphate dehydrogenase (34.09-35.08 kDa) and aldolase A (40.13-40.9 kDa). The heaviest protein present in both types of fresh meat exhibited MW of 57.7 kDa and 62.96 kDa, probably corresponding to pyruvate kinase muscle isozyme, and glucose-6-phosphate isomerase respectively.…”

Section: Results and Discussion A Qualitative/quantitative Analysis mentioning

confidence: 98%

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Micro-Electrophoretic Study of the Sarcoplasmic Fraction in the Dry-Cured Goat Raw Ham~!2008-07-02~!2008-10-14~!2008-11-26~!

Fratianni¹,

Sada²,

Orlando³

et al. 2008

TOFSJ

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Abstract:The water-soluble protein fractions in the "Violino di capra" goat dry cured ham were studied by using the "Lab-on-a-chip" version of a size-based capillary electrophoresis, and the results were compared with those obtained from the analysis of the corresponding fraction of pork meat and raw ham. The system automatically determined the relative concentration of each protein present in the sarcoplasmic fraction samples, where the nearly all proteins ranged from 24 kDa to 62.5 kDa, and made possible a supposition of the proteolysis process taking place after ripening of the goat raw ham. We propose the use of such technique as high-quality and routine analysis method in the biochemistry of food proteins.

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Section: Results and Discussion A Qualitative/quantitative Analysis mentioning

confidence: 95%

Section: Results and Discussion A Qualitative/quantitative Analysis mentioning

confidence: 98%

Micro-Electrophoretic Study of the Sarcoplasmic Fraction in the Dry-Cured Goat Raw Ham~!2008-07-02~!2008-10-14~!2008-11-26~!

Fratianni¹,

Sada²,

Orlando³

et al. 2008

TOFSJ

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show abstract

“…The first step of the protein hydrolysis is caused by cathepsins B, L, H, and D, calpains, peptidases, and cytosolic enzymes, which degrade the muscle proteins to polypeptides [49,78,79].…”

Section: Activity Of Proteasesmentioning

confidence: 99%

Manufacture of dry-cured ham: a review. Part 1. Biochemical changes during the technological process

Petrova

Aasen

Rustad

et al. 2015

Eur Food Res Technol

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various types of dry-cured ham are due to pig breed, feed of pigs, their weight and age, as well as differences in the production process. High-quality dry-cured hams, with a production length longer than 1 year, have distinct organoleptic characteristics: a rich, unique, and recognizable flavor and color in the range from rosy to maroon or brown red marbled with white fat. However, the sensorial, physical-chemical, aromatic, morphological, and textural characteristics of dry-cured ham vary significantly depending on the alterations in the technological process from producer to producer [1][2][3][4][5].The traditional technology for the production of dry-cured ham mainly consists of salting, postsalting (resting), and drying-ripening stages. In Northern Europe (Germany, Scandinavia), smoking is frequently applied. Salting and drying-ripening are the most important steps in the manufacture where the flavor of the final product is mainly formed.The duration of the postsalting and the drying-ripening stages varies depending on the type of dry-cured ham. The drying-ripening step lasts from 2-3 months to 2-3 years for the highest quality dry-cured hams. Increased time of ripening gives a higher degree of enzymatic degradation, contributing to taste and flavor of the final product and as a consequence of higher quality of dry-cured ham [6]. Shorter processing time allows faster production of drycured ham, but the quality characteristics will suffer. The technology for each particular kind of dry-cured ham is adjusted according to the desired priority: quality or high production capacity.During ripening, endogenous enzymes degrade proteins and lipids to amino and fatty acids correspondingly, which are mainly responsible for the flavor of dry-cured ham [7]. Free amino and fatty acids are further degraded and converted by enzymatic and chemical reactions, including oxidation, to volatile compounds. Free amino acids contribute Abstract Dry-cured ham is a traditional meat product highly appreciated by consumers. Production of dry-cured ham is a time-consuming process which varies between different ham types. There are many factors affecting the final characteristics of dry-cured ham. The quality of the raw material and the process conditions mainly influence the rate and the extent of biochemical reactions which are in turn responsible for the formation of specific flavor and texture. This review paper highlights the characteristics of the raw material, the enzymatic and chemical processes taking place during dry-cured ham manufacture and the compounds formed by these reactions. The rates of the enzymatic changes from fresh meat to the stage of final product are also described.

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“…Proteomics has been used to understand these processes, especially in products from pig meats such as dry-cured hams (Sentandreu et al, 2007;Theron et al, 2009). During ham ripening, endogenous proteases (cathepsins and calpains) and aminopeptidases produce complete hydrolysis of most fibrillar proteins, such as myosin heavy and light chains and actin, as well as some sarcoplasmic proteins (Di Luccia et al, 2005). Meat protein proteolysis creates small peptides, free amino acids, and degradation products that determine the texture, flavor, and odor of the final product (Toldrá et al, 2000;Sforza et al, 2001;Sentandreu et al, 2003).…”

Section: Postmortem Changes In Meat Proteinsmentioning

confidence: 99%

Proteomics in Food Science

Gallardo

Carrera

Ortea³

2013

Foodomics

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Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams

Cited by 104 publications

References 47 publications

Micro-Electrophoretic Study of the Sarcoplasmic Fraction in the Dry-Cured Goat Raw Ham~!2008-07-02~!2008-10-14~!2008-11-26~!

Micro-Electrophoretic Study of the Sarcoplasmic Fraction in the Dry-Cured Goat Raw Ham~!2008-07-02~!2008-10-14~!2008-11-26~!

Manufacture of dry-cured ham: a review. Part 1. Biochemical changes during the technological process

Proteomics in Food Science

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