Literature DB >> 33255627

RSM Optimization for the Recovery of Technofunctional Protein Extracts from Porcine Hearts.

Dolors Parés1, Mònica Toldrà1, Estel Camps1, Juan Geli1, Elena Saguer1, Carmen Carretero1.   

Abstract

Meat byproducts, such as the internal organs from slaughtered animals, are usually underutilized materials with low commercial value. The functional (emulsifying, gelling, and foaming) properties of soluble protein extracts derived from pork hearts were investigated, as well as their molecular weight distribution. A central composite design (CCD) for two process variables (pH and ionic strength of the extraction buffer) was used to foreknow the effects of the process conditions on the physicochemical characteristics and technofunctionality of the protein extracts by means of the response surface methodology (RSM). SDS-PAGE patterns of the heart protein solutions revealed multiple bands with molecular weights ranging from 15 to 220 kDa, mainly corresponding to sarcoplasmic, myofibrillar, as well as blood proteins. The best extraction conditions to obtain protein fractions with good foaming properties would correspond to acid pH (pH ≤ 5) and high salt content (2-4%). On the contrary, solutions recovered at pH > 5 with low NaCl contents were the ones showing better emulsifying properties. Regarding gelation ability, heat-induced gels were obtained from extracts at pH 6.5-8, which showed improved firmness with increasing NaCl content (2-4%). Satisfactory second-order polynomial models were obtained for all the studied response variables, which can be useful in guiding the development of functional ingredients tailored for specific uses to maximize applications.

Entities:  

Keywords:  meat byproducts; porcine heart; protein extraction; response surface methodology; technofunctional properties

Year:  2020        PMID: 33255627      PMCID: PMC7761421          DOI: 10.3390/foods9121733

Source DB:  PubMed          Journal:  Foods        ISSN: 2304-8158


  19 in total

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9.  Evaluation of functional properties of offal proteins.

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  1 in total

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