AI Article Synopsis

  • The study builds on a previous 2015 paper, examining how eleven commercial proteases affect protein extraction from shrimp shells at pH levels of 3.5 and 4.0.
  • Using formic acid, the researchers achieve over 95% deproteinization of the shrimp shells after 6 hours at 50°C.
  • While most proteases lead to a similar residual amino acid profile that notably increases Glycine content, pepsin stands out by resembling the original profile of the raw material.

Article 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 h 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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5491397PMC
http://dx.doi.org/10.1016/j.btre.2017.01.003DOI Listing

Publication Analysis

Top Keywords

shrimp shells
8
elements optimizing
4
optimizing one-step
4
one-step enzymatic
4
enzymatic bio-refinery
4
bio-refinery process
4
process shrimp
4
shrimp cuticles
4
cuticles focus
4
focus enzymatic
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!