Magnetotactic bacteria have the unique ability to synthesize magnetosomes (nano-sized magnetite or greigite crystals arranged in chain-like structures) in a variety of shapes and sizes. The chain alignment of magnetosomes enables magnetotactic bacteria to sense and orient themselves along geomagnetic fields. There is steadily increasing demand for magnetosomes in the areas of biotechnology, biomedicine, and environmental protection. Practical difficulties in cultivating magnetotactic bacteria and achieving consistent, high-yield magnetosome production under artificial environmental conditions have presented an obstacle to successful development of magnetosome applications in commercial areas. Here, we review information on magnetosome biosynthesis and strategies for enhancement of bacterial cell growth and magnetosome formation, and implications for improvement of magnetosome yield on a laboratory scale and mass-production (commercial or industrial) scale.

Xylanases with high specific activity has been focused with great interest as a useful enzyme in biomass utilization. The production of recombinant GH11 xylanase (MYCTH_56237) from Myceliophthora thermophila has been improved through N-terminal signal peptide engineering in P. pastoris. The production of newly recombinant xylanase (termed Mtxyn11C) was improved from 442.53 to 490.7 U/mL, through a replacement of α-factor signal peptide with the native xylanase signal peptide segment (MVSVKAVLLLGAAGTTLA) in P. pastoris. Scaling up of Mtxyn11C production in a 7.5 L fermentor was improved to the maximal production rate of 2503 U/mL. In this study, the degradation efficiency of Mtxyn11C was further examined. Analysis of the hydrolytic mode of action towards the birchwood xylan (BWX) revealed that Mtxyn11C was clearly more effective than commercial xylanase and degrades xylan into xylooligosaccharides (xylobiose, xylotriose, xylotetraose). More importantly, Mtxyn11C in combination with a single multifunctional xylanolytic enzyme, improved the hydrolysis of BWX into single xylose by 40%. Altogether, this study provided strategies for improved production of xylanase together with rapid conversion of xylose from BWX, which provides sustainable, cost-effective and environmental friendly approaches to produce xylose/XOSs for biomass energy or biofuels production.

The lignocellulosic enzymes of Trichoderma asperellum have been intensely investigated toward efficient conversion of biomass into high-value chemicals/industrial products. However, lack of genome data is a remarkable hurdle for hydrolase systems studies. The secretory enzymes of newly isolated T. asperellum ND-1 during lignocellulose degradation are currently poorly known. Herein, a high-quality genomic sequence of ND-1, obtained by both Illumina HiSeq 2000 sequencing platforms and PacBio single-molecule real-time, has an assembly size of 35.75 Mb comprising 10,541 predicted genes. Secretome analysis showed that 895 proteins were detected, with 211 proteins associated with carbohydrate-active enzymes (CAZymes) responsible for biomass hydrolysis. Additionally, T. asperellum ND-1, T. atroviride IMI 206040, and T. virens Gv-298 shared 801 orthologues that were not identified in T. reesei QM6a, indicating that ND-1 may play critical roles in biological-control. In-depth analysis suggested that, compared with QM6a, the genome of ND-1 encoded a unique enzymatic system, especially hemicellulases and chitinases. Moreover, after comparative analysis of lignocellulase activities of ND-1 and other fungi, we found that ND-1 displayed higher hemicellulases (particularly xylanases) and comparable cellulases activities. Our analysis, combined with the whole-genome sequence information, offers a platform for designing advanced T. asperellum ND-1 strains for industrial utilizations, such as bioenergy production.

Lignocellulosic biomass is a renewable raw material. Industrial interest with new technology has grown to take advantage of this raw material. Different microbial enzymes are treated with biomass to produce the desired products under ideal industrial conditions. Xylanases are the key enzymes that degrade the xylosidic linkages in the xylan backbone of the biomass, and commercial enzymes are categorized into different glycoside hydrolase families. Thermophilic microorganisms are an excellent source of thermostable enzymes that can tolerate the extreme conditions of industrial processing. Thermostability of xylanases from thermophilic microorganisms has given the importance for a specific activity at elevated temperatures and distinction due to biochemical properties, structure, and mode of action. Optimized xylanases can be produced through genetic engineering: a novel xylanase is isolated from an extreme environment and then genetically modified to improve suitability for industrial contexts. Recombinant protein techniques have made it possible to engineer and express thermostable xylanases in bacteria, yeasts, and filamentous fungi. We will discuss the biotechnological potential of xylanases from thermophilic microorganism and the ways they are being optimized and expressed for industrial applications.

Background: Natural biological magnetite nanoparticles are widely distributed from microorganisms to humans. It is found to be very important in organisms, especially in navigation. Moreover, purified magnetite nanoparticles also have potential applications in bioengineering and biomedicine. Magnetotactic bacteria (MTB) is considered one of the most abundant species around the world which can form intracellular membrane enveloped magnetic nanoparticles, referred to as magnetosomes. To our knowledge, the biomineralization of magnetosome in MTB involves a serious of genes located on a large unstable genomic region named magnetosome island, which specially exists in MTB. The magnetite core of magnetosome formed via a Fe (III) ion intermediates, for instance, α -Fe ₂ O ₃ and ferrihydrite. Though the biosynthesis of magnetosome represents a general biomineralization mechanism of biogenic magnetite, knowledge of magnetosome biosynthesis and biomineralization remains very limited. Method: Cells used in this study were cultured in a 7.5-L bioreactor, samples for intermediate capture were taken each certain time interval after the generation of magnetosome biosynthesis condition. High-resolution transmission electron microscopy were used to analyze the detailed structure of magnetosomes. The parameters of the crystal structures were obtained by Fast Fourier Transform analyses. Results: In this study, we identified a novel intermediate phase, ε -Fe ₂ O ₃ , during the magnetite maturation process in MTB via kinetic analysis. Unlike α -Fe ₂ O ₃ , which has been reported as a precursor during magnetosome biosynthesis in MTB before, ε -Fe ₂ O ₃ , due to its thermal instability, is a rare phase with scarce natural abundance. This finding confirmed that ε -Fe ₂ O ₃ is an important novel intermediate during the biomineralization of magnetosome in MTB, and shed new light on the magnetosome biosynthesis pathway.