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Activity of encapsulated Lactobacillus bulgaricus in alginate-whey protein microspheres BABT
Chen,Meng-Yan; Zheng,Wei; Dong,Qiu-Yue; Li,Zhen-Hua; Shi,Lu-E; Tang,Zhen-Xing.
In this work, alginate-whey protein was used as wall materials for encapsulating Lactobacillus delbrueckii subsp. bulgaricus (L. bulgaricus). The characteristics of encapsulated and free L. bulgaricus showed that the free L. bulgaricus lost viability after 1 min exposure to simulated gastric fluid (SGF) at pH 2.0 and 2.5. However, the viability of encapsulated L. bulgaricus did not decrease in SGF at pH 2.5 for 2 h incubation. The viable numbers of encapsulated L. bulgaricus decreased less than 1.0 log unit for 2 h incubation in SGF at pH 2.0. For bile stability, only 1.2 log units and 2.0 log units viability of the encapsulated L. bulgaricus was lost in 1 and 2% bile for 1 h exposure, respectively, compared with no survival of free L. bulgaricus under the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Encapsulation; Alginate; Whey protein; Probiotics; Stability.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000500736
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Enzyme activity and thermostability of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica by site-directed mutagenesis Electron. J. Biotechnol.
Zhang,Yu; Li,Zhen-Hua; Zheng,Wei; Tang,Zhen-Xing; Zhang,Zhi-Liang; Shi,Lu-E.
Background: To identify the critical amino acid residues that contribute to the high enzyme activity and good thermostability of Yersinia enterocolitica subsp. palearctica (Y. NSN), 15 mutants of Y. NSN were obtained by site-directed mutagenesis in this study. And their enzyme activity and thermostability were assayed. Effect of several factors on the enzyme activity and thermostability of Y. NSN, was also investigated. Results: The results showed that the I203F and D264E mutants retained approximately 75% and 70% enzyme activity, respectively, compared to the wild-type enzyme. In addition to the I203F and D264E mutants, the mutant E202A had an obvious influence on the thermostability of Y. NSN. According to the analysis of enzyme activity and...
Tipo: Journal article Palavras-chave: Factors affecting enzyme activity; Nuclease; Mutation; Mutagenesis; Nucleases without sequence specificity.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600005
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