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| Dhake,A.B.; Patil,M.B.. |
| The fungus Penicillium purpurogenum was found to produce intracellular ß-glucosidase. Maximum activity of ß-glucosidase was observed on sucrose. Various cultural parameters of cultivation of P. purpurogenum for production of ß-glucosidase were optimized. Maximum enzyme content was observed after 96 hours of cultivation at 30º;C. Addition of amino acids histidine and cysteine induced ß-glucosidase synthesis to certain extent. The optimum temperature and pH for ß-glucosidase activity was 50º;C and 5.5 respectively. ß-glucosidase of P.purpurogenum shows stability at pH 2 thus it could be an ideal enzyme for debittering in fruit juice and wine industries. |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: SS-glucosidase; Penicillium. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822005000200013 |
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| Kaur,Jatinder; Chadha,Bhupinder S; Kumar,Badhan A; Kaur,Ghatora, S; Saini,Harvinder S. |
| This study reports the purification and characterization of ß-glucosidase from a newly isolated thermophilic fungus, Melanocarpus sp. Microbial Type Culture Collection (MTCC) 3922. The molecular weight of ß-glucosidase was determined to be ~ 92 and 102 kDa with SDS PAGE and gel filtration, respectively, and pI of ~ 4.1. It was optimally active at 60ºC and pH 6.0, though was stable at 50ºC and pH 5.0 - 6.0. The presence of DTT, mercaptoethanol and metal ions such as Na+, K+, Ca2+, Mg2+and Zn2+ positively influenced the activity of ß-glucosidase but the activity was inhibited in the presence of CuSO4. ß-Glucosidase recognized pNP- ß-glucopyranoside (pNPG) as the preferred substrate, and showed very low affinity for pNP- ß-D-cellobioside. Km and Vmax for the... |
| Tipo: Journal article |
Palavras-chave: SS-glucosidase; Melanocarpus sp; Purification; Substrate specificity; Transglycosylation. |
| Ano: 2007 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582007000200010 |
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