Abstracts Book - IMRC 2018

• SF5-P007
PRODUCTION OF N-ACETYL-GLUCOSAMINE ALPHA-CHITIN USING
A CHITINASE COCKTAIL
Flavio Augusto Cardozo 1 , William Facchinatto 2 , Sergio Paulo Campana Filho 2 , Luiz Alberto
Colnago 3 , Adalberto Junior 4
1 Universidade de São Paulo, Biomedical Sciences Institute, Brazil. 2 Universidade de São Paulo,
Sao Carlos Institute of Chemistry, Brazil. 3 Embrapa, Embrapa Instrumentation, Brazil.
4 Universidade de São Paulo, Faculty of Pharmaceutical Sciences, Brazil.
N-acetyl-D-glucosamine (GlcNAc) is a biocompound with great potential for
application in pharmaceuticals, cosmetics, nutritional supplements and
biomaterials. It has traditionally been produced by chemical hydrolysis of chitin,
the main constituent of the arthropod exoskeletons and is also present in the
cell walls of some fungi and algae. However, the most used chemical processes
have certain drawbacks, including acidic waste production, low yields and high
costs This study focused in the enzymatic production of GlcNAc, an
environmentally friendly alternative to the chemical processes currently used.
Optimal hydrolysis conditions were determined, and GlcNAc was effectively
produced colloidal alpha-chitin by using a chitinase cocktail produced by
Aeromonas caviae CHZ306. The chitinase cocktail composition and natural
alpha-chitin pretreatment were the key factors to improve the GlcNAc yield of
the enzymatic process. Results showed that the enzymes cocktail should be
composed by enzymes that completely hydrolyze chitin into GlcNAc, such as
endochitinases and exochitinases (chitobiosidases and N-acetylglucosaminidases),
and that the enzymes cocktails containing higher N-acetylglucosaminidases
activity result in higher GlcNAc yields. Moreover, the
pretreatment of alpha-chitin should significantly decrease its crystallinity,
degree of polymerization and solution viscosity while preserving its ability to
establish hydrogen bonds and hydrophobic interactions, which are required to
maintain the three-dimensional structure of the polymer and the activity of the
chitinases.
Acknowledgment:
This work was supported by FAPESP (2012/16824-0 and 2016/20970-2)
Keywords: Chitin, chitinase, N-acetyl-D-glucosamine
Presenting authors email: william.marcondes@gmail.com