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The present work aimed at evaluating if heavy pig low-protein diets balanced for amino acid (AA) profile affect the quality characteristics of dry cured hams. To the aim, 40 hams obtained by Italian Duroc×Italian Large White pigs fed three different dietary crude protein and indispensable AA levels were compared with those obtained by a conventional Parma ham Protected Designation of Origin diet (C). No physico-chemical (aw, pH), chemical (gross composition, NaCl, lipid peroxidation, non-protein nitrogen, total volatile bases) or sensory characteristics of hams were systematically affected by the administered diet, animal sex or their interaction with the exception of total and subcutaneous fat (the latter measured by an image analysis procedure). Considering gilts, low-protein diets resulted in samples with higher fat content and subcutaneous fat thickness with respect to hams obtained with C diet. In conclusion, low protein diets in the finishing phase of pig breeding could reduce the environmental impact due to nitrogen excretion without significantly affecting ham quality.
This article was published in the following journal.
Name: Meat science
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That component of SPEECH which gives the primary distinction to a given speaker's VOICE when pitch and loudness are excluded. It involves both phonatory and resonatory characteristics. Some of the descriptions of voice quality are harshness, breathiness and nasality.
A heterodimeric protein that is a cell surface antigen associated with lymphocyte activation. The initial characterization of this protein revealed one identifiable heavy chain (FUSION REGULATORY PROTEIN 1, HEAVY CHAIN) and an indeterminate smaller light chain. It is now known that a variety of light chain subunits (FUSION REGULATORY PROTEIN 1, LIGHT CHAINS) can dimerize with the heavy chain. Depending upon its light chain composition a diverse array of functions can be found for this protein. Functions include: type L amino acid transport, type y+L amino acid transport and regulation of cellular fusion.
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
A heterodimeric protein that is a cell surface antigen associated with lymphocyte activation. The initial characterization of this protein revealed one identifiable heavy chain (ANTIGENS, CD98 HEAVY CHAIN) and an indeterminate smaller light chain. It is now known that a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS) can dimerize with the heavy chain. Depending upon its light chain composition a diverse array of functions can be found for this protein. Functions include: type L amino acid transport, type y+L amino acid transport and regulation of cellular fusion.
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