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Zhang,Yu; Zheng,Wei; Gu,Jian-Fei; Ni,Jian; Wang,Ling; Tang,Zhen-Xing; Shi,Lu-E. |
ABSTRACTIn this work, the mixture of alginate and soy protein isolate used as a wall material was developed to encapsulateEnterococcus faecalis HZNU P2 (E. faecalis HZNU P2). The survival ability in the simulated gastric fluid (SGF) and bile salt solution, storage stability at different temperatures and release properties in the simulated intestinal fluid (SIF) of encapsulated cells were assessed. The results showed that encapsulation could offer sufficient protection toE. faecalis HZNU P2. The viability of encapsulatedE. faecalis HZNU P2 did not decrease in SGF at pH 2.5 or 2.0 after 2 h incubation, while free cells were reduced from 11 to 9.85 log CFU/mL in SGF (pH 2.5) at the same exposure time. Only minor viability of encapsulatedE. faecalis HZNU P2... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enterococcus faecalis; Encapsulation; Soy protein isolate; Alginate; Stability; Viability. |
Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000500805 |
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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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Lou,Dan; Ye,Jifeng; Yang,Lianhua; Wu,Zheng; Zheng,Wei; Zhang,Hui. |
Icariin, a prenylated flavonol glycoside isolated from Epimedium, has been considered as a potential alternative therapy for osteoporosis. The present study aimed to clarify the detailed molecular mechanisms of action of icariin on osteoblast function, using bone marrow-derived mesenchymal stem cells (BM-MSCs). BM-MSCs were first stimulated by icariin. Then, gene and protein expression of cAMP/PKA/CREB signaling molecules were analyzed by RT-PCR and western blotting (WB), and alkaline phosphatase (ALP) was analyzed in cell lysates by ELISA. MTT assays indicated that icariin did not have significant effects on cell viability up to 1 µM. Icariin showed a dose-dependent effect on the alkaline phosphatase activity of BM-MSCs. WB analysis showed that icariin... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Icariin/molecular mechanisms; BM-MSCs; CAMP; PKA; CREB. |
Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-82502019000100592 |
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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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