Optimization of proteins and minerals removal from shrimp shells to produce highly acetylated chitin

被引:54
作者
Younes, Islem [1 ]
Hajji, Sawssen [1 ]
Rinaudo, Marguerite [2 ]
Chaabouni, Moncef [3 ]
Jellouli, Kernel [1 ]
Nasri, Moncef [1 ]
机构
[1] ENIS, Lab Enzyme Engn & Microbiol, POB 1173-3038, Sfax, Tunisia
[2] Biomat Applicat, 6 Rue Lesdiguieres, F-38000 Grenoble, France
[3] ENIS, Lab Ind Chem, BP W 3038, Sfax, Tunisia
关键词
Chitin; Chemical demineralization; Enzymatic deproteinization; ALKALINE SERINE-PROTEASE; PURIFICATION; TRYPSIN; EXTRACTION; CHITOSAN;
D O I
10.1016/j.ijbiomac.2015.08.034
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chitin and derivatives used for biomedical or pharmaceutical applications require a high level of purity and quality that are difficult to achieve. In this study, we propose to optimize the extraction of chitin in order to obtain pure product keeping a structure as close as possible to the native form. Thus, demineralization step was firstly optimized using response surface methodology. In the optimized conditions predicted by the model, the obtained chitin has an acetylation degree (DA) and a demineralization degree (DM) equal to 99% and 100%, respectively. Then, different microbial and fish crude alkaline proteases were tested for their efficiency in deproteinization. Crude alkaline proteases giving the highest deproteinization degrees (DP), Bacillus mojavensis A21 and Scorpaena scrofa, were selected for chitin extraction. The obtained DP was 88 +/- 2% and 83 +/- 1%, respectively. At the end, effect of the use of mixed enzymatic treatment with the two selected crude enzymes and the order of demineralization/deproteinization steps were tested. The results demonstrated that two separated steps in enzymatic treatments realized on demineralized sample give the best DP (96%) preserving the DA (99%). (C) 2015 Published by Elsevier B.V.
引用
收藏
页码:246 / 253
页数:8
相关论文
共 42 条
[1]   BSF1 fibrinolytic enzyme from a marine bacterium Bacillus subtilis A26: Purification, biochemical and molecular characterization [J].
Agrebi, Rym ;
Haddar, Anissa ;
Hmidet, Noomen ;
Jellouli, Kemel ;
Manni, Laila ;
Nasri, Moncef .
PROCESS BIOCHEMISTRY, 2009, 44 (11) :1252-1259
[2]  
[Anonymous], J FOOD SCI TECHNOL
[3]  
[Anonymous], THESIS QUEBEC
[4]  
[Anonymous], NEMROD LOGICIEL
[5]  
[Anonymous], DESIGN OPTIMISATION
[6]  
[Anonymous], J AMINO ACIDS PROTEI
[7]  
[Anonymous], CHITIN
[8]  
[Anonymous], FOOD BIOPROD PROCESS
[9]  
[Anonymous], THESIS REIMS U
[10]  
[Anonymous], 1988, METHODE PLANS EXPERI