Hydrolysate Protein Production from Catfish with Understanding of the Potential Antioxidant Activity | Chapter 5 | Novel Aspects on Chemistry and Biochemistry Vol. 9

This chapter identifies the way of producing Hydrolysate protein from the sailfin catfish, scientifically known as Pterygoplichthys pardalis which is a freshwater fish belonging to the Loricariidae family. Catfish is considered one of the invasive species in Indonesia but the effectiveness of this fish is unrevealed till now. for this reason, we use this fish as the raw material for protein hydrolysate. Protein hydrolysate is the process of breaking down the protein into amino acids through the reaction of hydrolysis facilitated by acids, bases or enzymes.

The selected sample (Pterygoplichthys pardalis) was collected from a river located in Blitar Regency, East Java, Indonesia. The catfish specimens were thoroughly rinsed with water to eliminate any impurities and subsequently transported to the laboratory in a temperature-controlled container maintained at 4°C.

The experiment of hydrolysis involved different levels of pH (control, 5,7, 9). Two different durations (12 and 24 hours) were selected for implementing the hydrolysis process and each was replicated three times. This experiment selected a few parameters that include yield, antioxidant activity, degree of hydrolysis, protein levels, and ash content. These parameters were extensively impacted (p <0.05) by the time of hydrolysis, pH and their interactions.

It can be concluded that the most significant effect (p < 0.05) has been shown by the moisture content, pH and the duration of hydrolysis although their interactions did not (p > 0.05). It has been observed that the pH treatment (p < 0.05) has significantly affected the Fat content. Therefore, it can be concluded that a pH of 9 and a duration of 24 hours were the optimal conditions that can produce fish protein hydrolysate (FPH) from sailfin catfish.

Author(s) Details:

Asep Awaludin Prihanto,
Fishery Product Technology, Faculty of Fisheries and Marine Science, Brawijaya University, Malang, East Java, 65145, Indonesia and Bio-Seafood Research Unit, Brawijaya University, Malang, East Java, 65145, Indonesia.

Rahmi Nurdiani,
Fishery Product Technology, Faculty of Fisheries and Marine Science, Brawijaya University, Malang, East Java, 65145, Indonesia and Bio-Seafood Research Unit, Brawijaya University, Malang, East Java, 65145, Indonesia.

Lina Widya Sari,
Bio-Seafood Research Unit, Brawijaya University, Malang, East Java, 65145, Indonesia.

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Proposal for the Modification of Plant Proteins in Order to Release Bioactive Peptides against Metabolic Syndrome | Chapter 6 | New Visions in Science and Technology Vol. 10

 Hypertension, dyslipidemia, and insulin resistance are among the illnesses that make up the metabolic syndrome. Its treatment is centred on lifestyle changes, although this approach frequently fails to improve metabolic syndrome signs over time. The sequences of certain representative vegetable proteins were investigated in order to uncover bioactive peptides with activity against metabolic syndrome illnesses. Legumin (chickpea), glutelin type A-2 (chickpea), glutelin type B-2 (rice), prolamin PPROL 17 (maize), and glutelin (rice) are five proteins that have shown to have a strong potential for preventing metabolic syndrome. After simulating gastrointestinal digestion, we created and assessed in silico alterations to their amino acid sequence to release bioactive peptides (SGD). The method described here enables the creation of proteins that could be used to treat metabolic syndrome, which can then be produced and studied afterwards. These proteins can be made through heterologous expression in bacteria or yeast, and in the long run, transgenic plants could be used to make them. These proteins may be employed as functional meals in the future.

Author(S) Details

Diego Armando Maldonado-Torres
Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, CIBA-IPN, Carretera estatal Tecuexcomac-Tepetitla Km. 1.5, Tepetitla 90700, Tlaxcala, México.

D. Alejandro Fernández-Velasco
Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, UNAM, Ciudad de México 04510, México.

Gema Morales-Olán
Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, CIBA-IPN, Carretera estatal Tecuexcomac-Tepetitla Km. 1.5, Tepetitla 90700, Tlaxcala, México.

Flor de Fátima Rosas-Cárdenas
Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, CIBA-IPN, Carretera estatal Tecuexcomac-Tepetitla Km. 1.5, Tepetitla 90700, Tlaxcala, México.

Silvia Luna-Suárez
Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, CIBA-IPN, Carretera estatal Tecuexcomac-Tepetitla Km. 1.5, Tepetitla 90700, Tlaxcala, México.

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