Abstract：
:Laccase and laccase-based cross-linked enzyme aggregates (CLEAs) were stabilized through the formation of a surrounding polymeric network made of chitosan and 3-aminopropyltriethoxysilane. The thermoresistance of the resulting enzyme polymer engineered structures of laccase (EPES-lac) and CLEAs (EPES-CLEA) were more than 30 times higher than that of free laccase and CLEAs at pH 3 and 40 °C. The EPES showed higher residual activity than the unmodified biocatalysts against chaotropic salts (up to 10 times), EDTA (up to 5 times), methanol (up to 15 times) and acetone (up to 20 times). The Michaelis-Menten kinetic parameters revealed that the affinity for 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) has doubled for the EPES-lac and EPES CLEA compared to their unmodified forms. The EPES-lac structures acted optimally at pH 4 and their activity was nearly temperature-independent, while the laccase activity of EPES-CLEA was optimal at pH 4 and 60 °C. Globally, the EPES have shown significantly improved properties which make them attractive candidate for the development of laccase-based applications.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Hassani T,Ba S,Cabana Hdoi
10.1016/j.biortech.2012.10.058subject
Has Abstractpub_date
2013-01-01 00:00:00pages
640-5eissn
0960-8524issn
1873-2976pii
S0960-8524(12)01560-Xjournal_volume
128pub_type
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journal_title：Bioresource technology
pub_type： 杂志文章
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更新日期：2016-11-01 00:00:00
abstract：:Fed-batch enzymatic hydrolysis process from alkali-pretreated sugarcane bagasse was investigated to increase solids loading, produce high-concentration fermentable sugar and finally to reduce the cost of the production process. The optimal initial solids loading, feeding time and quantities were examined. The hydrolys...
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