I read this book the same weekend that the Packers took on the Rams, and the experience of the latter event, obviously, colored my judgment. Although I abhor anything that smacks of being a handbook (like, \"How to Earn a Merit Badge in Neurosurgery\") because too many volumes in biomedical science already evince a boyscout-like approach, I must confess that parts of this volume are fast, scholarly, and significant, with certain reservations. I like parts of this well-illustrated book because Dr. Sj6strand, without so stating, develops certain subjects on technique in relation to the acquisition of judgment and sophistication. And this is important! So, given that the author (like all of us) is somewhat deficient in some areas, and biased in others, the book is still valuable if the uninitiated reader swallows it in a general fashion, realizing full well that what will be required from the reader is a modulation to fit his vision, propreception, adaptation and response, and the kind of problem he is undertaking. A major deficiency of this book is revealed by comparison of its use of physics and of chemistry to provide understanding and background for the application of high resolution electron microscopy to problems in biology. Since the volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of The instrument and its ancillary tools are simply and well presented. The potential use of chemical or cytochemical information as it relates to biological fine structure , however, is quite deficient. I wonder when even sophisticated morphol-ogists will consider fixation a reaction and not a technique; only then will the fundamentals become self-evident and predictable and this sine qua flon will become less mystical. Staining reactions (the most inadequate chapter) ought to be something more than a technique to selectively enhance contrast of morphological elements; it ought to give the structural addresses of some of the chemical residents of cell components. Is it pertinent that auto-radiography gets singled out for more complete coverage than other significant aspects of cytochemistry by a high resolution microscopist, when it has a built-in minimal error of 1,000 A in standard practice? I don't mean to blind-side (in strict football terminology) Dr. Sj6strand's efforts for what is \"routinely used in our laboratory\"; what is done is usually well done. It's just that …

Methods in Enzymology.

Molecular assembly is crucial in functional molecular materials and devices. Among the molecular interactions that can form assemblies, stacking among π-conjugated molecular backbones plays an essential role in charge transport through organic materials and devices. The single-molecule junction technique allows for the application of an electric field of approximately 108 V/m to the nanoscale junctions and to investigate the electric field-induced assembly at the single-stacking level. Here, we demonstrate an electric field-induced stacking effect between two molecules using the scanning tunneling microscope break junction (STM-BJ) technique and we found an increase in the stacking probability with increasing intensity of the electric field. The combined density functional theory (DFT) calculations suggest that the molecules become more planar under the electric field, leading to the energetically preferred stacking configuration. Our study provides a new strategy for tuning molecular assembly by employing a strong electric field.

Electric Field-Induced Assembly in Single-Stacking Terphenyl Junctions.

Biomineralization is a common process in organisms to produce hard biomaterials by combining inorganic ions with biomacromolecules. Multifunctional nanoplatforms are developed based on the mechanism of biomineralization in many biomedical applications. In the past few years, biomineralization-based nanoparticle drug delivery systems for the cancer treatment have gained a lot of research attention due to the advantages including simple preparation, good biocompatibility, degradability, easy modification, versatility, and targeting. In this review, the research trends of biomineralization-based nanoparticle drug delivery systems and their applications in cancer therapy are summarized. This work aims to promote future researches on cancer therapy based on biomineralization. Rational design of nanoparticle drug delivery systems can overcome the bottleneck in the clinical transformation of nanomaterials. At the same time, biomineralization has also provided new research ideas for cancer treatment, i.e., targeted therapy, which has significantly better performance.

Biomineralization: An Opportunity and Challenge of Nanoparticle Drug Delivery Systems for Cancer Therapy

The use of porous silicon (PS) for biosensing applications is now emerging as it offers desired properties such as better surface-volume ratio, tunable pore size, ease of fabrication, and compatibility with the current silicon-based technology. These superior properties make PS as a promising candidate for the immobilization of biomolecules with higher retention, stability, storage, and operational ease. High specificity and catalytic activity of the enzyme for the substrate are advantageous for the detection of a particular analyte with higher accuracy in less time. Immobilization of enzyme on the PS surface alters the surface electrical and optical properties, and can conveniently be used for the sample analysis. In the present review, the strategies of enzyme immobilization on PS and various influencing factors are discussed in detail. The scope of PS for enzyme immobilization and prerequisite surface modifications has been assessed in brief. The review discusses the various methods of enzyme immobilization on PS with their benefits and bottlenecks with special emphasis on the approaches to overcome the difficulties during the immobilization process. Further, various properties of PS influencing the process of immobilization have been outlined in brief. An overall analysis of enzyme immobilization on PS surface has been given for the successful development of PS based enzymatic biosensors.

Strategies, challenges and opportunities of enzyme immobilization on porous silicon for biosensing applications

Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.

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Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

Programmable stimuli-responsive polypeptides for biomimetic synthesis of silica nanocomposites and enzyme self-immobilization

Green preparation of covalently co-immobilized multienzymes on silica nanoparticles for clean production of reducing sugar from lignocellulosic biomass

Exploring a simple and versatile technique for direct immobilization of target enzymes from cell lysate without prior purification is urgently needed. Thus, a novel all-in-one strategy for purification and immobilization of β-1,3-xylanase was proposed, the target enzymes were covalently immobilized on silica nanoparticles via elastin-like polypeptides (ELPs)-based biomimetic silicification and SpyTag/SpyCatcher spontaneous reaction. Thus, the functional carriers that did not require the time-consuming surface modification step were quickly and efficiently prepared. These carriers could specifically immobilize the SpyTag-fused target enzymes from the cell lysate without pre-purification. The ELPs-SpyCatcher hardly leaked from the carriers (0.5%), and the immobilization yield of enzyme was up to 96%. Immobilized enzyme retained 85.6% of the initial activity and showed 88.6% of the activity recovery. Compared with free ones, the immobilized β-1,3-xylanase showed improved thermal stability, elevated storage stability and good pH tolerance. It also retained more than 70.6% of initial activity after 12 reaction cycles, demonstrating its excellent reusability. The results clearly highlighted the effectiveness of the novel enzyme immobilization method proposed here due to the improvement of overall performance of immobilized enzyme in respect to free form for the hydrolysis of macromolecular substrates. Thus, it may have great potential in the conversion of algae biomass as well as other related fields.

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A novel all-in-one strategy for purification and immobilization of β-1,3-xylanase directly from cell lysate as active and recyclable nanobiocatalyst

Lytic polysaccharide monooxygenases (LPMOs) with synergistic effect on polysaccharide hydrolase represent a revolution in biotechnology, which may accelerate the conversion of biomass to the second-generation biofuels. Discovering more hydrolases that have synergism with LPMOs will considerably expand the knowledge and application of biomass degradation. The LPMOs named CgAA9 were verified to exhibit 1.52-fold synergism when incubated with β-1,3-xylanase at a molar ratio of 3:1. The ion chromatography results proved that CgAA9 did not alter the endogenous hydrolysis mode of β-1,3-xylanase. Meanwhile, to decrease the operational cost of enzymes, a novel strategy for immobilizing LPMOs and β-1,3-xylanases based on the biomimetic silica nanoparticles was developed. It enabled preparation of immobilized enzymes directly from the cell lysate. The immobilization efficiency and activity recovery reached 84.6 and 81.4%. They showed excellent reusability for 12 cycles by retaining 68% of initial activity. The optimum temperature for both free and immobilized biocatalyst were 40 and 37 °C, indicating they were ideal candidates for typical simultaneous saccharification and fermentation (SSF) in ethanol production from algea biomass. This was the first report on the synergy between LPMOs and β-1,3-xylanase, and the strategy for enzyme self-immobilization was simple, timesaving, and efficient, which might have great potentials in algae biomass hydrolysis. • The lytic polysaccharide monooxygenases (LPMOs) from Chaetomium globosum were firstly verified to boost the hydrolysis of β-1,3-xylanases for β-1,3-xylan.
 • A novel strategy for simple preparation of SpyCather-modifed silica nanopartilcles and intelligent immobilization of target enzymes from the cell lysate was proposed.
 • The immobilized LPMOs and β-1,3-xylanases could be reasonable alternatives for typical simultaneous saccharification and fermentation (SSF) in manipulation of algae biomass.

Enzymatic degradation of algal 1,3-xylan: from synergism of lytic polysaccharide monooxygenases with β-1,3-xylanases to their intelligent immobilization on biomimetic silica nanoparticles

Yue Qiu

Papers

Programmable stimuli-responsive polypeptides for biomimetic synthesis of silica nanocomposites and enzyme self-immobilization

Green preparation of covalently co-immobilized multienzymes on silica nanoparticles for clean production of reducing sugar from lignocellulosic biomass

A novel all-in-one strategy for purification and immobilization of β-1,3-xylanase directly from cell lysate as active and recyclable nanobiocatalyst

Enzymatic degradation of algal 1,3-xylan: from synergism of lytic polysaccharide monooxygenases with β-1,3-xylanases to their intelligent immobilization on biomimetic silica nanoparticles

Unique silica biomimetic mineralization of acidic elastin-like polypeptides without hydroxyl and charged residues