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

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

Proteases were extracted from the viscera of Colossoma macropomum and precipitated with ethanol (30–70%, v/v). The enzymatic extract was partially purified with a yield of 75% (2926 U/g of tissue); at least five caseinolytic proteases bands were observed in zymogram. The optimum pH of the preparatio...

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Bibliographic Details
Published in:Food chemistry Vol. 112; no. 1; pp. 125 - 130
Main Authors: Espósito, Talita S., Amaral, Ian P.G., Buarque, Diego S., Oliveira, Givanildo B., Carvalho, Luiz B., Bezerra, Ranilson S.
Format: Journal Article
Language:English
Published: Oxford Elsevier Ltd 2009
[Amsterdam]: Elsevier Science
Elsevier
Subjects:
Alkaline protease
alkaline proteases
Biological and medical sciences
Colossoma macropomum
detergents
enzymatic treatment
Ethanol
fish processing
Fish processing waste
fish waste
Food industries
food processing wastes
freshwater fish
Fundamental and applied biological sciences. Psychology
Laundry detergent
laundry products
Protein recovery
proteinases
proteolysis
Tambaqui
Tambaqui ( Colossoma macropomum)
trypsin
waste utilization
Protein recovery
Fish processing waste
Ethanol
Laundry detergent
Tambaqui ( Colossoma macropomum)
Alkaline protease
Peptidases
Detergent
Tambaqui (Colossoma macropomum)
Enzyme
Waste treatment
Hydrolases
Protein
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Summary:Proteases were extracted from the viscera of Colossoma macropomum and precipitated with ethanol (30–70%, v/v). The enzymatic extract was partially purified with a yield of 75% (2926 U/g of tissue); at least five caseinolytic proteases bands were observed in zymogram. The optimum pH of the preparation was in the alkaline pH range (10–12). The optimum temperature of activity was 60 °C and only about 15% of the initial activity was lost after an incubation period of 30 min at the above mentioned temperature. Both trypsin and chymotrypsin-like enzymes were detected in the proteases, but with a stronger prevalence for the former. These proteolytic enzymes remained stable in the presence of non-ionic (Tween 20 and Tween 80) and ionic surfactants (saponin and sodium choleate). They also revealed high resistance (60% residual activity) when incubated with 10% H 2O 2 for 75 min. Furthermore, the preparation retained approximately 80% of its proteolytic activity after incubation for 1 h at 40 °C with the commercial detergent.
Bibliography:http://dx.doi.org/10.1016/j.foodchem.2008.05.049
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2008.05.049