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 18,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To elucidate the function of cellobiose dehydrogenase (CDH) in cellulose degradation by Phanerochaete chrysosporium, production and localization of CDH were investigated and compared with those in shaking and aerated static cultures grown on cellulose. Substantial CDH activity was detected in the medium of the shake cultures after 8 days of incubation, while no CDH activity was detected in the medium of static cultures at any point during the incubation period. Light microscopy clearly showed that many cellulose particles were adsorbed on the surface of the hypha in static cultures, whereas no cellulose particles were absorbed to the hypha is shake cultures. The addition of laminarinase to static cultures was very effective in detaching cellulose particles from the hypha surfaces. Using a potentiometric assay performed with an oxidation-reduction potential electrode, some CDH activity could be detected on the hypha/cellulose complexes in static cultures. Thus, CDH is produced also in static cultures, albeit in lower amounts that in shake cultures, but the enzyme is not released into the medium. It seem likely that the beta-1,3-glucan layer plays an important role in CDH localization and cellulose degradation. Immunocytochemical confocal laser scanning microscopy for the static cultures demonstrated that most CDH was adsorbed on the surface of the cellulose, especially around the cracks, which were formed by the action of cellulases during the course of incubation. From these observations, we conclude a direct participation of CDH in the degradation of cellulose in cooperation with cellulases.
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PMID:Localization of cellobiose dehydrogenase in cellulose-grown cultures of Phanerochaete chrysosporium. 922 89

A 100-kDa protein was found to be a major cell wall protein in Saccharomyces cerevisiae cells cultured without shaking, but was not present in cells cultured with shaking. The amino acid sequence of this protein was identical to the sequence of Tir1p/Srp1p. TIR1/SRP1 has previously been identified as a gene induced by glucose, cold shock or anaerobiosis and was believed to be a cell membrane protein but not a cell wall protein. However, we found that beta-1,3-glucanase solubilized Tir1p/Srp1p from the cell wall and the purified Tir1p/Srp1p reacted with antiserum to beta-1,6-glucan and contained glucose. These results suggest that Tir1p/Srp1p is a major structural cell wall protein in the static-cultured yeast cells and is bound to the cell wall through beta-1,6-glucan. TIR1/SRP1 mRNA was transcribed only in the static culture and its transcription was regulated by the ROX1 repressor.
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PMID:Identification and analysis of a static culture-specific cell wall protein, Tir1p/Srp1p in Saccharomyces cerevisiae. 936 89

Beta-1,3-1,4-glucanase (EC3.2.1.73) as an important industrial enzyme has been widely used in the brewing and animal feed additive industry. To improve expression efficiency of recombinant beta-1,3-1,4-glucanase from Bacillus licheniformis EGW039(CGMCC 0635) in methylotrophic yeast Pichia pastoris GS115, the DNA sequence encoding beta-1,3-1,4-glucanase was designed and synthesized based on the codon bias of P. pastoris, the codons encoding 96 amino acids were optimized, in which a total of 102 nucleotides were changed, the G+C ratio was simultaneously increased from 43.6 to 45.5%. At shaking flask level, beta-1,3-1,4-glucanase activity is 67.9 and 52.3 U ml(-1) with barley beta-glucan and lichenan as substrate, respectively. At laboratory fermentor level, the secreted protein concentration is approximately 250 mg l(-1). The beta-1,3-1,4-glucanase activity is 333.7 and 256.7 U ml(-1) with barley beta-glucan and lichenan as substrate, respectively; however, no activity of this enzyme on cellulose is observed. Compared to the nonoptimized control, expression level of the optimized beta-1,3-1,4-glucanase based on preferred codons in P. pastoris shown a 10-fold higher level. The codon-optimized enzyme was approximately 53.8% of the total secreted protein. The optimal acidity and temperature of this recombinant enzyme were pH 6.0 and 45 degrees C, respectively.
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PMID:Codon optimization of Bacillus licheniformis beta-1,3-1,4-glucanase gene and its expression in Pichia pastoris. 1721 53

To compare of performance of beta-1,3-1,4-glucanase gene (bgl) in different expression systems, the beta-1,3-1,4-glucanase gene (GenBank Accession No. EU623974) was amplified from Bacillus amyloliquefaciens BS5582 by PCR and was cloned into three vectors pEGX-4T-1, pET20b(+) and pET28a(+) to construct pEGX-4T-1-bgl, pET20b(+)-bgl and pET28a(+)-bgl recombinant plasmids. The pEGX-4T-1-bgl was transformed into three different Escherichia coli host strains. The pET20b (+)-bgl and pET28a (+)-bgl were transformed into E. coli BL21 (DE3) respectively. Recombinant beta-glucanase was expressed by IPTG inducement in these recombinants. E. coli BL21 (DE3)-pET28a (+)-bgl had the highest enzyme activity. In Luria-Bertani medium, the total enzyme activity was (322.0 +/- 8.8) U/mL, which was 40.1% of original strain in optimal shaking flask condition. This recombinant's performance was studied in Terrific Broth medium under inducement of IPTG and lactose at the same time., and the highest total enzyme activity could reach (1883.3 +/- 45.8) U/mL (818.8% of the original), which indicate that the recombinant strain has a good value in industry application.
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PMID:[Optimization of cloning and expression of beta-glucanase gene from Bacillus amyloliquefaciens]. 1963 29