Surfactants- And Oxidants-Resistant Alkaline Proteases From Common Carp (Cyprinus Carpio L) Processing Waste

Abstract

Intestine from Cyprinus carpio L., an important fish in the Brazilian Aquaculture, is proposed in this work as a source of alkaline protease. The intestine crude extract was submitted to a partial purification by ethanol precipitation. The fraction 30–70% (v/v) of ethanol concentration showed higher recovery and specific activity when compared with the crude extract and was submitted to further studies. The optimal temperature and pH were found to be 50C and 11.0, respectively. The enzymatic activity was activated by nonionic surfactants and retained more than 60% of their initial proteolytic activity in the presence of the ionic surfactants. Almost 50% of enzymatic activity was retained in the presence of 5% (v/v) of hydrogen peroxide. The high proteolytic activity at 50C and alkaline pH, together with its stability in the presence of the surfactants and oxidants tested, indicate that this alkaline protease can well be used in detergent formulations. PRACTICAL APPLICATIONS Hydrolytic enzymes have been employed in a range of applications including processes in the food, textile and pharmaceutics industries. Among theses enzymes, proteases correspond for the highest sales on the enzyme market. In the present time, most proteolytic enzymes are extracted from bacteria (genus Bacillus). These biomolecules can also be extracted from the viscera of several fish species. This study relates the partial purification and physical chemical characteristics of alkaline protease found in the Cyprinus carpio intestine, one of the most important species for the world aquaculture. Surfactants and oxidant agents were also used to assay the stability of this enzyme. Therefore, this communication contributes to the optimization of the use of fish by‐products as well as the discovery of enzymes displaying desirable properties.

Golden Grey Mullet (Liza aurata) Alkaline Proteases: Biochemical Characterization, Application in the Shrimp Wastes Deproteinization, Laundry Commercial Detergents, and Preparation of Antioxidant Protein Hydrolysate

“…It can also be reported that the crude alkaline protease is more stable at 30 • C than 40 • C. These finding were similar to those for striped seabream (L. mormyrus; El-Hadj Ali et al, 2011), tambaqui proteases (C. macropomum; Espósito et al, 2009b), and Nile tilapia (O. niloticus; Mendes et al, 2009).…”

Solvent-Stable Digestive Alkaline Proteinases from Striped Seabream (Lithognathus mormyrus) Viscera: Characteristics, Application in the Deproteinization of Shrimp Waste, and Evaluation in Laundry Commercial Detergents

“…The relative activities at 40 and 60°C were about 76% and 37.5%, respectively, of that at 50°C. The optimal temperature of L. mormyrus proteases was similar to that of common carp (Cyprinus carpio L.) [34] and lower than that of Nile tilapia and tambaqui proteases [23,35] which have optimal temperatures in the range of 55 and 60°C, respectively. The thermal stability profile showed that alkaline enzyme extract is fully active for at least 60 min at 30 and 40°C, which is desirable for laundry purposes and from the ecological and economical point of view, mainly, because of saving of energy.…”

“…The visceral protease activity pattern was similar to those of other fish species such as intestine proteases of Nile tilapia (Oreochromis niloticus), proteases from the intestine and pyloric caeca of crevalle jack (Caranx hippos), spotted goatfish (Pseudopeneus maculates), parrotfish (Sparisoma sp. ), and traira (Hoplias malabaricus) [33], although, alkaline proteases from tambaqui (Colossoma macropomum) and common carp (Cyprinus carpio) intestine were reported to be active at higher pH values (10.0-12.0) [23,34].…”

Digestive alkaline proteinases from Serranus scriba viscera: Characteristics, application in the extraction of carotenoproteins from shrimp waste, and evaluation in laundry commercial detergents

“…The relative activities at 40 and 60 1C were about 59% and 40.1%, respectively, of that at 50 1C. The optimal temperature of S. scriba proteases was lower than that of farmed giant catfish, which exhibited optimal temperature at 60 1C (Vannabun et al, 2014) and similar to crude enzyme extracted from Lithognathus mormyrus (El Hadj-Ali et al, 2011) and Cyprinus carpio L. (Esposito et al, 2009). The thermal stability profile, reported in Fig.…”