Elements for optimizing a one-step enzymatic bio-refinery process of shrimp cuticles: Focus on enzymatic proteolysis screening
Type | Article | ||||||||
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Date | 2017-09 | ||||||||
Language | English | ||||||||
Author(s) | Baron Regis![]() ![]() |
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Affiliation(s) | 1 : Ifremer, BRM, Rue de l’Ile d’Yeu, BP21105, 44311 Nantes cedex 03, France 2 : Ifremer, PBA, Rue de l’Ile d’Yeu, BP21105, 44311 Nantes cedex 03, France 3 : Université de Nantes, GEPEA UMR CNRS 6144, CRTT, Boulevard de l’Université, 44600 Saint-Nazaire cedex, France 4 : Ynsect, Rue de l’Ile d’Yeu, BP21105, 44311 Nantes cedex 03, France |
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Source | Biotechnology Reports (2215-017X) (Elsevier BV), 2017-09 , Vol. 15 , P. 70-74 | ||||||||
DOI | 10.1016/j.btre.2017.01.003 | ||||||||
Keyword(s) | bio-refinery, shrimp cuticles, acidic enzymatic proteolysis | ||||||||
Abstract | This article complements an earlier work published in 2015 Baron et al. (2015) that showed the interest of a shrimp shells bio-refining process. We compare here the effect of eleven commercial proteases at pH 3.5 or 4.0 on a residual amount of shrimp shells proteins after 6 hours at 50 °C. The two pH are obtained when respectively 40 and 25 mmol of formic acid are added to 5 g of mild dried shell. Deproteinisation yield above 95% are obtained. Residual amino acids profile in the solid phase was identical for the eleven proteases except for pepsin which was similar to the raw material profile. A significant relative increase in the proportion of Glycine is observed for the ten other cases. Likewise, shapes of size exclusion chromatograms of the dissolved phase are similar except with pepsin. |
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