Fish processing waste as a source of alkaline proteases for laundry detergent

Espósito, Talita S.; Amaral, Ian P.G.; Buarque, Diego S.; Oliveira, Givanildo Bezerra; Carvalho, Luiz Bezerra de; Bezerra, Ranilson S.

doi:10.1016/j.foodchem.2008.05.049

Cited by 56 publications

(49 citation statements)

References 24 publications

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“…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.…”

Section: Effect Of Temperature On the Activity And Stability Of The Vmentioning

confidence: 87%

“…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].…”

Section: Effect Of Ph On Activity and Stability Of Alkaline Enzyme Exmentioning

confidence: 99%

“…The alkaline crude enzyme extract was preincubated with surfactants and oxidizing agents for 1 h at 30°C, and the remaining activity was measured at pH 10.0 and 50°C. The activity is expressed as a percentage of the activity level in the absence of additives Espósito et al [23] and Mendes et al [35] reported also the stability of tambaqui (Colossoma macropomum) and Nile tilapia (O. niloticus) proteases in the presence of several commercial detergents. The tambaqui proteases retained more than 50% of their activities when incubated with the detergents Ala ® , Bem-te-vi ® , and Omo ® for 1 h at 40°C, and maximum stability was achieved with Surf ® , since the enzyme retained 73.70% of its activity.…”

Section: Stability Of the Alkaline Crude Enzyme Extract With Commercimentioning

confidence: 99%

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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

Ali

Hmidet

Ghorbel-Bellaaj

et al. 2011

Appl Biochem Biotechnol

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Alkaline proteases from the viscera of the striped seabream (Lithognathus mormyrus) were extracted and characterized. Interestingly, the crude enzyme was active over a wide range of pH from 6.0 to 11.0, with an optimum pH at the range of 8.0-10.0. In addition, the crude protease was stable over a broad pH range (5.0-12.0). The optimum temperature for enzyme activity was 50 °C. The crude alkaline proteases showed stability towards various surfactants and bleach agents and compatibility with some commercial detergents. It was stable towards several organic solvents and retained more than 50% of its original activity after 30 days of incubation at 30 °C in the presence of 25% (v/v) dimethyl sulfoxide, N,N-dimethylformamide, diethyl ether, and hexane. The crude enzyme extract was also tested for shrimp waste deproteinization in the preparation of chitin. The protein removal with a ratio enzyme/substrate of 10 was about 79%.

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Section: Effect Of Temperature On the Activity And Stability Of The Vmentioning

confidence: 87%

Section: Effect Of Ph On Activity and Stability Of Alkaline Enzyme Exmentioning

confidence: 99%

Section: Stability Of the Alkaline Crude Enzyme Extract With Commercimentioning

confidence: 99%

See 1 more Smart Citation

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

Ali

Hmidet

Ghorbel-Bellaaj

et al. 2011

Appl Biochem Biotechnol

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“…The activity of the enzyme before incubation was taken as 100 %. Buffer solutions used for pH activity and stability are presented in "Material and Methods" section macropomum (Espósito et al 2009a) and higher than those of proteases from common carp (Cyprinus carpio L.) (Espósito et al 2009b) and striped seabream (lithognathus mormyrus) (El-Hadj Ali et al 2011) which exhibited an optimum temperature at 50°C.…”

Section: Effect Of Temperature On Protease Activity and Stabilitymentioning

confidence: 99%

Zebra blenny (Salaria basilisca) viscera as a source of solvent-stable proteases: characteristics, potential application in the deproteinization of shrimp wastes and evaluation in liquid laundry commercial detergents

et al. 2012

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The present study describes the characterization of crude protease extract from zebra blenny (Salaria basilisca) and its evaluation in liquid detergent and shrimp waste deproteinization. At least five caseinolytic proteases clear bands were observed in zymogram. The crude alkaline protease showed optimum activity at pH 8.0 and 60°C, and it was highly stable over a wide range of pH from 6.0 to 11.0. Proteolytic enzymes showed extreme stability towards non-ionic surfactants (5 % Tween 80 and 5 % Triton X-100) and oxidizing agents (1 % sodium perborate), and relative stability towards anionic surfactant (1 % Sodium dodecyl sulfate (SDS)). They also showed high stability and compatibility with various laundry liquid detergents from Tunisian market. Furthermore, the crude enzyme was stable towards several organic solvents and retained more than 50 % of its original activity after 30 days of incubation at 30°C in the presence of 50 % (v/v) dimethylsulfoxide (DMSO). Further, proteases from zebra blenny viscera were found to be effective in the deproteinization of shrimp wastes. The protein removal after 3 h at 40°C with an enzyme/substrate ratio (E/S) of 5 U/mg protein was about 77 %.

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“…The enzyme remains stable in both ionic and non-ionic surfactants and maintains around 80% of its catalyzing ability after 1 h of incubation with chemical detergent (Espósito et al, 2009). Due to the specificity of chymotrypsin on proteins and peptides, it can be used to break down proteinaceous contaminatnts (blood and foods) on cloth efficiently.…”

Section: Chemical Industrymentioning

confidence: 99%

Extraction, Purification and Characterization of Fish Chymotrypsin: A Review

K.¹

2011

American Journal of Biochemistry and Biotechnology

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Problem statement: Solid fish waste is generated from the unwanted parts of fish including heads, tails, fins, frames, offal (guts, kidney and liver) and skin. It accounts for up to 80% of material from production of surimi, 66% from production of fillet and 27% from production of headed and gutted fish. Currently, fish wastes are disposed off in land-based waste disposal systems or at sea generating toxic byproducts during the decomposition process. However, fish processing waste can be used to produce commercially valuable by-products, such as chymotrypsin. Approach: A comperehensive review of the literature on the extraction, purification and characeterization of fish chymotrypsin was performed. Results: Chymotrypsin is an endopeptidase secreted by the pancreatic tissues of vertebrates and invertebrates. It has 3 different structures (chymotrypsin A, B and C) varying slightly in solubility, electrophoretic mobility, isoelectric point and cleavage specificity. Only chymotrypsin A and B are found in fish. Compared with mammal chymotrypsin, fish chymotrypsins have similar amino acid composition and molecular weights. Fish chymotrypsins have higher specific activity, especially those from cold-water fish, and low pH and temperature tolerance. The factors affecting the concentration and activity of chymotrypsin in fish are water temperature, fish species, fish age, fish weight and starvation. Chymotrypsin has application in various industries including the food industry, leather production industry chemical industry and medical industry. Conclusion: Extraction techniques for chymotrypsin include: ultra-filtration, ammonium sulphate fractionation precipitation or water-in-oil microemulsions. Purification can be carried out using recrystallization and gel-filtration, ion-exchange and hydrophobic interaction chromatography. Further studies should focus on the optimization of purifiying chymotrypsin from fish processing wastes.

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Fish processing waste as a source of alkaline proteases for laundry detergent

Cited by 56 publications

References 24 publications

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

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

Zebra blenny (Salaria basilisca) viscera as a source of solvent-stable proteases: characteristics, potential application in the deproteinization of shrimp wastes and evaluation in liquid laundry commercial detergents

Extraction, Purification and Characterization of Fish Chymotrypsin: A Review

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