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Hydrolysis of white shrimp shell (Litopenaues vannamei) protein by chicken intestine enzymes.

Authors :
Sjaifullah, Achmad
Winata, I. Nyoman Adi
Septiana, Cici Desi
Source :
AIP Conference Proceedings; 2023, Vol. 2818 Issue 1, p1-3, 3p
Publication Year :
2023

Abstract

The shell of white shrimp (Litopenaeus vannamei) contains several valuable organic materials such as chitin, protein, fat, minerals, and some pigments. Chitin is a raw material for producing chitosan which is very widely used. Chitin isolation from white shrimp shells is carried out through several stages, namely deproteination, demineralization and depigmentation stages. Shrimp shell deproteination in preparing chitin can be done chemically or enzymatically which is believed to be an environmentally friendly process. This article describes the process of deproteinizing white shrimp shells to produce chitin enzymatically using protease enzymes found in chicken intestines. Protein in shrimp shells will be hydrolyzed by enzymes from the chicken intestine so that it can be separated from chitin. The effect of incubation time and the ratio of chicken intestines and shrimp shells during the deproteinization of white shrimp shells has been studied. A mixture of white shrimp shell and chicken intestine with a weight ratio of 1/0; 2/1; and 1/2 were incubated for 48 hours at pH 1.5. The ability of chicken intestine proteases to hydrolyze white vaname shrimp shell protein was determined by measuring the total nitrogen in shrimp shell residues during the hydrolysis. The results showed that the hydrolysis process occurred optimally at the mixture of shrimp shells and chicken intestines ratio of 1/2 for 48 hours with a total nitrogen content value of 5.27%, equivalent to the nitrogen content in chitin which is widely reported. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0094243X
Volume :
2818
Issue :
1
Database :
Complementary Index
Journal :
AIP Conference Proceedings
Publication Type :
Conference
Accession number :
170046356
Full Text :
https://doi.org/10.1063/5.0131611