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Dive into the research topics where F. Polidori is active.

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Featured researches published by F. Polidori.


Small Ruminant Research | 1991

Effects of feeding calcium salts of long chain fatty acids on milk yield, milk composition and plasma parameters of lactating goats

A. Baldi; F. Cheli; C. Corino; V. Dell'Orto; F. Polidori

Abstract Thirty-two goats were fed concentrates, one containing 6% calcium salts of fatty acids. Rations contained equal quantities of Ca and N. Fatty acid calcium salts significantly increased milk fat (from 3.4 ± 0.1 to 3.7 ± 0.2%), but the percentage of short and medium chain fatty acids (C4 to C14) in milk fat decreased (from 37.5 ± 1.0 to 32.2 ± 0.6%). The group fed fatty acid calcium salts had increases in plasma cholesterol (3.5 ± 0.2 vs. 4.3 ± 0.2 mmol/1), phospholipids (2.5 ± 0.1 vs. 2.9 ± 0.1 mmol/1) and gamma-glutamyltranspeptidase (28.9 ± 1.5 vs. 33.5 ± 2.3 U/1).


Meat Science | 2000

Tenderization of wether lambs meat through pre-rigor infusion of calcium ions

Paolo Polidori; M Trabalza Marinucci; Francesco Fantuz; Carlo Renieri; F. Polidori

A study involving 36 wether lamb carcasses was conducted in order to evaluate the effects of 0.3 M CaCl(2) injection on final tenderness in muscle Longissimus thoracis et lumborum. Injection of wether lamb carcasses with CaCl(2) accelerated the post mortem tenderization process. Both control and distilled water injected animals had similar Ca(2+)-dependent proteases (μ-calpain and m-calpain) and their inhibitor (calpastatin) activities, whereas these were all significantly decreased in CaCl(2) injected animals. The effect of CaCl(2) injection on tenderness was recorded by measuring shear force values 2 and 6 days post mortem. Tenderness was significantly improved by CaCl(2) injection at both at 2 and 6 days post mortem. It was concluded that activation of μ-calpain and m-calpain was responsible for the observed post mortem proteolysis and tenderization.


Journal of Dairy Research | 1998

Distribution of plasminogen activator forms in different fractions of buffalo milk.

Francesco Fantuz; A. Baldi; V. Dell'Orto; F. Polidori; Carlo Angelo Sgoifo Rossi; I. Politis; Christian W. Heegaard

In Italy buffalo milk is an important animal product utilized solely for the manufacture of Mozzarella cheese. Of an estimated population of 200000 buffalo there are ∼25000 controlled animals. The average milk production, expressed over 270 d lactation, is 2000 kg/head with average fat and protein contents of 82·6 and 46·4 g/l respectively (Associazione Italiana Allevatori, 1996). In recent years there has been a steady increase in the number of dairy buffalo replacing dairy cows as a consequence of the European Union quota system. The cheesemaking qualities of milk depend on many factors, the most important of which are the concentrations of intact casein and fat. Milk in which casein has been broken down by proteolytic enzymes is of less value to cheese manufacturers (Lucey & Kelly, 1994). Plasmin (EC 3.4.21.7), the most important endogenous milk proteinase, occurs in milk together with its inactive proenzyme, plasminogen (Schaar & Funke, 1986). Plasmin hydrolyses α s -casein and β-casein, although κ-casein has been reported to be resistant (Fox, 1981). However, Andrews & Alichanidis (1983) found κ-casein to be hydrolysed quite rapidly by plasmin. Plasmin activity is higher in mastitic than normal milk (Bastian & Brown, 1996). Stage of lactation affects plasmin activity: late lactation is associated with higher concentrations of plasmin (Gilmore et al . 1995; Baldi et al . 1996). Thus, plasmin could be a major problem in herds with seasonal breeding such as buffalo, which progress through lactation in synchrony and are therefore at a similar stage of lactation at a given time. The cascade of reactions leading to plasminogen activation is regulated by a complex network of molecular interactions between plasminogen activators (PA; EC 3.4.21.31) and at least three types of specific PA inhibitors (PAI-1; PAI-2; PAI-3; Saksela, 1985; Politis, 1996). There are two types of highly specific PA: tissue-PA (t-PA) and urokinase-PA (u-PA) (Saksela & Rifkin, 1988). PA activity is higher in mastitic than normal milk (Heegaard et al . 1994 a ). However, previous studies on PA in milk were carried out on bovine and caprine milk. No information is available on the presence and type of PA in buffalo milk. Thus the objective of the present study was to determine the level and type of PA in different fractions of buffalo milk: casein, serum, and somatic cells.


Journal of Dairy Science | 2001

Plasminogen Activation System in Goat Milk and its Relation with Composition and Coagulation Properties

Francesco Fantuz; F. Polidori; F. Cheli; A. Baldi


Small Ruminant Research | 1999

Response of dairy ewes in late lactation to recombinant bovine somatotropin

V. Chiofalo; A. Baldi; G. Savoini; F. Polidori; V. Dell'Orto; I. Politis


Congresso ASPA | 2001

Studies on the protein fractions of donkey milk

Francesco Fantuz; Silvia Vincenzetti; Paolo Polidori; Alberto Vita; F. Polidori; Elisabetta Salimei


Italian Journal of Animal Science | 2005

Donkey's milk caseins characterization

Silvia Vincenzetti; Paolo Polidori; Francesco Fantuz; Pierluigi Mariani; Natalina Cammertoni; Alberto Vita; F. Polidori


Animal Research | 2001

Post mortem proteolysis and tenderization of beef muscle through infusion of calcium chloride

Paolo Polidori; Massimo Trabalza-Marinucci; Francesco Fantuz; F. Polidori


Archive | 2001

Effetti del differente periodo di frollatura delle carcasse di agnelloni sulla tenerezza della carne.

Paolo Polidori; Francesco Fantuz; Gianvincenzo Lebboroni; F. Polidori


Milchwissenschaft-milk Science International | 2001

Plasminogen activation system in milk from Friesian and Jersey cows: relationships with milk production and composition

Francesco Fantuz; O. Pedron; F. Polidori; D. Tedesco; A. Baldi

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A Baldi

University of Perugia

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