Journal of Microbiology

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Novel Mutations in CYP51B from Penicillium digitatum Involved in Prochloraz Resistance: Jinlong Wang , Jinhui Yu , Jing Liu , Yongze Yuan , Na Li , Muqing He , Ting Qi , Geng Hui , Li Xiong , Deli Liu; J. Microbiol. 2014;52(9):762-770. Published online August 2, 2014; DOI: https://doi.org/10.1007/s12275-014-4112-2

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Green mold caused by Penicillium digitatum is one of the most serious postharvest diseases of citrus fruit, and it is ubiquitous in all citrus growing regions in the world. Sterol 14α-demethylase (CYP51) is one of the key enzymes of sterol biosynthesis in the biological kingdom and a prime target of antifungal drugs. Mutations in CYP51s have been found to be correlated with resistance to azole fungicides in many fungal species. To investigate the mechanism of resistance to prochloraz (PRC) in P. digitatum, the PRC sensitivity was determined in vitro in this study to assess the sensitivity of 78 P. digitatum isolates collected in Hubei province. The results showed that 25 isolates were prochloraz-resistant (PRC-R), including six high-resistant (HR) strains, twelve medium-resistant (MR) and seven low-resistant (LR) strains. A sequence analysis showed no consistent point mutations of PdCYP51A in the PRC-R strains, but four substitutions of CYP51B were found, Q309H in LR strains, Y136H and Q309H in HR strains, and G459S and F506I in MR strains, which corresponded to the four sensitivity levels. Based on the sequence alignment analysis and homology modeling followed by the molecular docking of the PdCYP51B protein, the potential correlation between the mutations and PRC resistance is proposed.

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Abstract: AtlA of Streptococcus mutans is a major autolysin and belongs to glycoside hydrolase family 25 with cellosyl of Streptomyces coelicolor. The autolysin gene (atlA) encoding AtlA was identified from S. criceti. AtlA of S. criceti comprises the signal sequence in the N-terminus, the putative cell-wallbinding domain in the middle, and the catalytic domain in the C-terminus. Homology modeling analysis of the catalytic domain of AtlA showed the resemblance of the spatial arrangement of five amino acids around the predicted catalytic cavity to that of cellosyl. Recombinant AtlA and its four point mutants, D655A, D747A, W831A, and D849A, were evaluated on zymogram of S. criceti cells. Lytic activity was destroyed in the mutants D655A and D747A and diminished in the mutants W831A and D849A. These results suggest that Asp655 and Asp747 residues are critical for lytic activity and Trp831 and Asp849 residues are also associated with enzymatic activity.

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Improved Production of Live Cells of Lactobacillus rhamnosus by Continuous Cultivation using Glucose-yeast Extract Medium: Liew Siew Ling , Rosfarizan Mohamad , Raha Abdul Rahim , Ho Yin Wan , Arbakariya Bin Ariff; J. Microbiol. 2006;44(4):439-446.; DOI: https://doi.org/2408 [pii]

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Abstract: In this study, the growth kinetics of Lactobacillus rhamnosus and lactic acid production in continuous culture were assessed at a range of dilution rates (0.05 h?1 to 0.40 h?1) using a 2 L stirred tank fermenter with a working volume of 600 ml. Unstructured models, predicated on the Monod and Luedeking-Piret equations, were employed to simulate the growth of the bacterium, glucose consumption, and lactic acid production at different dilution rates in continuous cultures. The maximum specific growth rate of L. rhamnosus, ┢max, was estimated at 0.40 h?1, and the Monod cell growth saturation constant, Ks, at approximately 0.25 g/L. Maximum cell viability (1.3 ≠ 1010 CFU/ml) was achieved in the dilution rate range of D = 0.28 h?1 to 0.35 h?1. Both maximum viable cell yield and productivity were achieved at D = 0.35 h?1. The continuous cultivation of L. rhamnosus at D = 0.35 h?1 resulted in substantial improvements in cell productivity, of 267% (viable cell count) that achieved via batch cultivation.

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