2010
DOI: 10.1016/j.biortech.2010.01.036
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Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste

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Cited by 101 publications
(71 citation statements)
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“…These results were completely different from that reported in previous studies [28,37,[40][41][42], in which an incomplete conversion of chitin into its monomer was observed during the degradation process. Thus, based on the patterns of hydrolysate formation, it can be concluded that the chitinase obtained from Chitinibacter sp.…”
Section: Analysis Of the Hydrolyzed Productscontrasting
confidence: 84%
“…These results were completely different from that reported in previous studies [28,37,[40][41][42], in which an incomplete conversion of chitin into its monomer was observed during the degradation process. Thus, based on the patterns of hydrolysate formation, it can be concluded that the chitinase obtained from Chitinibacter sp.…”
Section: Analysis Of the Hydrolyzed Productscontrasting
confidence: 84%
“…GC72 (Gao, Zhang, Chen, Hao, Tong, & Ouyang, 2015), Laceyella putida (Shibasaki, Uchimura, Miura, Kobayashi, Usami, & Horikoshi, 2014) and Massilia timonae (Adrangi, Faramarzi, Shahverdi, & Sepehrizadeh, 2010). Moreover, many chitinase genes from Bacillus halodurans (da Silva, García-Fraga, López-Seijas, & Sieiro, 2014), B. licheniformis (Sandalli, Kacagan, Canakci, & Belduz, 2008;Songsiriritthigul, Lapboonrueng, Pechsrichuang, Pesatcha, & Yamabhai, 2010), Chitiniphilus shinanonensis (Huang, Shizume, Nogawa, Taguchi, & Shimosaka, 2012), Paenibacillus barengoltzii (Fu, Yan, Yang, Yang, Guo, & Jiang, 2014), Pseudoalteromonas tunicate (García-Fraga et al, 2015), Sanguibacter antarcticus (Lee et al, 2010), Serratia proteamaculans (Purushotham & Podile, 2012), and Vibrio sp. (Bendt et al, 2011) have been cloned and heterologously expressed.…”
Section: Introductionmentioning
confidence: 98%
“…12,15,38,39) Accordingly, the high temperature optimum and the thermal stability of the chitinase from Scorpaena scrofa provide further confirmation of its potential industrial application in the recycling of chitin wastes. 43) Substrate specificity of SsChi50 The ability to hydrolyze several carbohydrates substrates is an important criterion for the effectiveness of chitinases. Accordingly, kinetic experiments were performed via reducing sugar assays using natural substrates.…”
Section: )mentioning
confidence: 99%
“…The high activity and stability exhibited by SsChi50 in an acidic environment (pH 2.0-5.0) makes it suitable for the digestion of chitinous substances ingested as food as well as for biotechnological applications involving the bioconversion of chitin waste. 43,44) Chitinase activity was evaluated in a pH range of 2.0-11.0 using buffers of pH values with colloidal chitin as substrate. The pH stability of the enzyme was determined by incubating the chitinase in buffers ranging from 2.0-9.0 for 48 h at 60 C, and residual activity was measured colorimetrically using standard procedures.…”
Section: )mentioning
confidence: 99%