Optimization of the porcine liver enzymatic hydrolysis conditions

Abstract

Worldwide porcine slaughterhouses produce significant amounts of by‐products, such as porcine liver, daily. Even though the liver presents a very restricted market demand when raw, this product is composed of an exceptional nutritional content, with emphasis on protein, being, therefore, characterized as a potential raw material to produce protein hydrolysates. This article aimed to study the production of protein hydrolysate using the commercial enzymes Alcalase 2.4L™ and Novo Pro‐D™. For the development of this research, a central composite rotatable design with 4 axial points was applied for each enzyme. The factors evaluated were protein/water and enzyme/substrate ratios. The best hydrolysis results indicate average percentages of hydrolysis degree of 27.5% for both enzymes. The presence of low‐molecular‐weight peptides was also evidenced by the electrophoresis technique. It is, therefore, concluded that there is positive viability for the use of hydrolyzed porcine liver in differentiated food applications with an aggregate market value. Practical Applications At present, the worldwide growing dissemination of food scarcity has become a stimulus for the food industry to rethink the efficient use of raw materials to avoid waste and maximize the use of existing nutritional resources. A potential way of exploiting the nutritional value of the protein by‐products with no commercial applications is their transformation into protein hydrolysates by means of enzymatic processes. Protein hydrolysates have been in focus in the scientific community with industrial applications as beneficial products to the ingesting body, for acting as either nutraceuticals or functional bioactive foods. Commercialization of this type of product has become a growing market niche. Thus, this research, which presents an investigation regarding the conditions of the porcine liver hydrolysis, fits within current issues, with innovative potential of obtainment of bioactive peptides from by‐products.

In vitro antioxidant and angiotensin I‐converting enzyme inhibitory properties of enzymatically hydrolyzed quinoa (Chenopodium quinoa) and kiwicha (Amaranthus caudatus) proteins

“…Betancur‐Ancona et al (2014) mentioned that enzymatic hydrolysis of proteins is a promising option for modifying the biological and functional properties of food proteins. Enzymatic hydrolysis presents notable product selectivity through simplified production routes, low generation of undesirable bitter‐tasting peptides, lower environmental and physiological toxicity, and consequently, high quality and productivity (Maluf et al, 2020). Obtaining protein hydrolysates from quinoa and kiwicha using commercial enzymes have been poorly addressed so far.…”

Application of preliminary high-pressure processing for improving bioactive characteristics and reducing antigenicity of whey protein hydrolysates

“…The processing time and the enzyme–substrate ratio can be determinant for the process success, not only because they generate changes in the chemical composition of the peptides, in the bioactive properties, in the sensory quality of the product, but also because they directly reflect on the cost of the process, which tends to be more expensive with higher amounts of enzyme and longer processes (Maluf et al., 2020). Thus, the treatments NPD1 and FC7 for 120 min of reaction were selected to conduct the following experiments.…”

Expeller-Pressed Pomegranate Seed (Punica granatum L.) as a Protein Source for the Production of Antioxidant Peptides

“…The pro le could result from substrate oversaturation resulting in inhibition of the enzyme or auto-digestion (Singh et al 2018). Enzymatic hydrolysis of ying squid muscle protein (Fang et al 2012), corn gluten meal (Zhuang et al 2013), and porcine liver (Maluf et al 2020) exhibited similar patterns. This study showed that the optimal enzyme/substrate ratio for enzymatic hydrolysis was 1.3% (v/w).…”