Directed preparation of algal oligosaccharides with specific structures by algal polysaccharide degrading enzymes.

Seaweed polysaccharides have a wide range of sources and rich content, with various biological activities such as anti-inflammatory, anti-tumor, anticoagulant, and blood pressure lowering. They can be applied in fields such as food, agriculture, and medicine. However, the poor solubility of macromolecular seaweed polysaccharides limits their further application. Reports have shown that some biological activities of seaweed oligosaccharides are more extensive and superior to that of seaweed polysaccharides. Therefore, reducing the degree of polymerization of polysaccharides will be the key to the high value utilization of seaweed polysaccharide resources. There are three main methods for degrading algal polysaccharides into algal oligosaccharides, physical, chemical and enzymatic degradation. Among them, enzymatic degradation has been a hot research topic in recent years. Various types of algal polysaccharide hydrolases and related glycosidases are powerful tools for the preparation of algal oligosaccharides, including α-agarases, ß-agaroses, α-neoagarose hydrolases and ß-galactosidases that are related to agar, κ-carrageenases, ι-carrageenases and λ-carrageenases that are related to carrageenan, ß-porphyranases that are related to porphyran, funoran hydrolases that are related to funoran, alginate lyases that are related to alginate and ulvan lyases related to ulvan. This paper describes the bioactivities of agar oligosaccharide, carrageenan oligosaccharide, porphyran oligosaccharide, funoran oligosaccharide, alginate oligosaccharide and ulvan oligosaccharide and provides a detailed review of the progress of research on the enzymatic preparation of these six oligosaccharides. At the same time, the problems and challenges faced are presented to guide and improve the preparation and application of algal oligosaccharides in the future.

Directed preparation, structure-activity relationship and applications of alginate oligosaccharides with specific structures: A systematic review.

The alginate oligosaccharides (AOS) possess versatile activities (such as antioxidant, anti-inflammatory, antitumor, and immune-regulatory activities) and have been the research topic in marine bioresource utilization fields. The degree of polymerization (DP) and the ß-D-mannuronic acid (M)/α-L-guluronic acid (G)-units ratio strongly affect the functionality of AOS. Therefore, directed preparation of AOS with specific structures is essential for expanding the applications of alginate polysaccharides and has been the research topic in the marine bioresource field. Alginate lyases could efficiently degrade alginate and specifically produce AOS with specific structures. Therefore, enzymatic preparation of AOS with specific structures has drawn increasing attention. Herein, we systematically summarized the current research progress on the structure-function relation of AOS and focuses on the application of the enzymatic properties of alginate lyase to the specific preparation of various types of AOS. At the same time, current challenges and opportunities for AOS applications are presented to guide and improve the preparation and application of AOS in the future.

Recent advances in the production, properties and applications of alginate oligosaccharides - a mini review.

Alginate oligosaccharides (AOS) made from the degradation of alginate, to some extent, makes up for the poor solubility and bioavailability of alginate as a macromolecular substance and possess several beneficial biological activities that are absent in alginate. These properties include prebiotic, glycolipid regulatory, immunomodulatory, antimicrobial, antioxidant, anti-tumor, promoting plant growth and other activities. Consequently, AOS has significant potential for use in the agricultural, biomedical, and food industries, and has been the focus of research in the field of marine biological resources. This review comprehensively covers methods (physical, chemical, and enzymatic methods) for the production of AOS from alginate. More importantly, this paper reviews recent advances in the biological activity and potentially industrial and therapeutic applications of AOS, providing a reference for future research and applications of AOS.

Alginate degrading enzymes: an updated comprehensive review of the structure, catalytic mechanism, modification method and applications of alginate lyases.

Alginate, a kind of linear acidic polysaccharide, consists of α-L-guluronate (G) and ß-D-mannuronate (M). Both alginate and its degradation products (alginate oligosaccharides) possess abundant biological activities such as antioxidant activity, antitumor activity, and antimicrobial activity. Therefore, alginate and alginate oligosaccharides have great value in food, pharmaceutical, and agricultural fields. Alginate lyase can degrade alginate into alginate oligosaccharides via the ß-elimination reaction. It plays an important role in marine carbon recycling and the deep utilization of brown algae. Elucidating the structural features of alginate lyase can improve our knowledge of its catalytic mechanisms. With the development of structural analysis techniques, increasing numbers of alginate lyases have been characterized at the structural level. Hence, it is essential and helpful to summarize and discuss the up-to-date findings. In this review, we have summarized progress on the structural features and the catalytic mechanisms of alginate lyases. Furthermore, the molecular modification strategies and the applications of alginate lyases have also been discussed. This comprehensive information should be helpful to expand the applications of alginate lyases.

Effect of surface charge conditions of carriers on the immobilization of ß-d-glucosidase.

In this study, a series of acidic or alkaline polypeptide chains were designed and grafted onto DEG-AM resin using Fmoc solid-phase synthesis to study the relationship between enzyme conformation and carrier surface charge. ß-d-glucosidase (ßGase) was then immobilized onto these modified carriers by adsorption. Each form of immobilized ßGase showed decreasing specific activity compared to that of the free. It could be attributed to both the changes in the enzyme conformation and the decrease in mass transfer efficiency. The optimum temperature of free ßGase, DEG@B3-ßGase is 55 °C, which of DEG@A3-ßGase is 65 °C and they all have the highest activity at pH 5. The Ea values ​​of free ßGase, DEG@A3-ßGase, and DEG@B3-ßGase are 0.546 kJ/mol, 0.224 kJ/mol, and 0.446 kJ/mol, and the Km values were 1.30 mmol/L, 1.44 mmol/L and 2.63 mmol/L, respectively. It shows that free ßGase and DEG@A3-ßGase are more similar. Meanwhile, the free ßGase (1.0 g/L, pH 5.0) stored at 4 °C has a shorter half-life (t1/2), which is only 9 days. However, the half-life of DEG@B3-ßGase and DEG@A3-ßGase is 20 days and over 60 days, indicating that the negative charged surface was conducive to maintenance of the structure and catalytic property of ßGase.

Elucidation of degrading pattern and substrate recognition of a novel bifunctional alginate lyase from Flammeovirga sp. NJ-04 and its use for preparation alginate oligosaccharides.

BACKGROUND: The alginate oligosaccharides have been widely used in agriculture, medicine, and food industries due to their versatile physiological functions such as antioxidant, anticoagulant, and antineoplastic activities. The bifunctional alginate lyases can degrade the alginate polysaccharide more efficiently into alginate oligosaccharides. Therefore, it is crucial to discover new bifunctional alginate lyase for alginate oligosaccharide production. RESULTS: Herein, a novel bifunctional alginate lyase FsAlgB was cloned and identified from deep-sea bacterium Flammeovirga sp. NJ-04, which exhibited broad substrate specificity and the highest activity (1760.8 U/mg) at pH 8.0 and 40 °C. Furthermore, the K m values of FsAlgB towards polyG (0.69 mM) and polyMG (0.92 mM) were lower than that towards sodium alginate (1.28 mM) and polyM (2.06 mM). Recombinant FsAlgB was further characterized as an endolytic alginate lyase, and it can recognize the tetrasaccharide as the minimal substrate and cleave the glycosidic bonds between the subsites of - 3 and + 1. CONCLUSION: This study provided extended insights into the substrate recognition and degrading pattern of alginate lyases with broad substrate specificity.

Insight into carrageenases: major review of sources, category, property, purification method, structure, and applications.

Carrageenan, a kind of linear sulfated polysaccharides consisting of D-galactose with alternating α-1,3 and ß-1,4 linkages, has been widely applied in the food and cosmetic industries as thickening and gelling agents due to excellent properties, such as gel-forming ability and chemical stability. It can be degraded by carrageenases to produce a series of even-numbered carrageenan oligosaccharides, which exhibit various fascinating functions, such as anti-inflammation, anti-coagulation, anti-tumor, and anti-thrombosis effects. Numerous carrageenases have been isolated and identified from various sources. The enzymes are grouped into three categories, namely κ-carrageenase, ι-carrageenase, and λ-carrageenase based on their substrate specificities and primary sequences, respectively. Elucidating the paradigm of the enzyme at every aspect would definitely enhance our understanding of the marine carbon cycling and natural evolution of glycoside hydrolases (GHs). The structural features of these enzymes have been fully illustrated, which will improve our knowledge of its catalytic mechanisms. In this review, we have summarized the recent progresses of major sources, category, and the enzyme's biochemical characteristics. Additionally, structural characteristics and catalytic mechanisms have been introduced in detail. We conclude with a brief discussion of the potential of the carrageenases in possible future applications in preparing functional oligosaccharides with versatile activities. This comprehensive information should be helpful regarding the application of carrageenases.

Gold Nanoparticles: Promising Agent to Improve the Diagnosis and Therapy of Cancer.

BACKGROUND: Gold nanoparticles have been exploited for nanobiotechnology applications for the last two decades. New insights of the nanomaterials as promising agent for cancer diagnosis and therapy have just started to emerge. Due to the size- and shape-dependent optical, electrical and thermal properties, gold nanoparticles are being developed as diagnostic reagents, drug carriers, contrast agents, photothermal agents and radiosensitisers. This review aims to summarize the latest advances of gold nanoparticles in cancer treatment. METHODS: We undertook a systematical search for research literatures using a well-framed review question and presented the applications in different fields, including early cancer diagnosis, imaging, radiotherapy, chemotherapy, gene therapy and photothermal therapy, which were fully described, filtered, combined and analyzed in order to provide documented proofs on the applications of gold nanoparticles in current cancer treatments. RESULTS: One hundred and sixty papers were included in the review, the majority of which represent latest researches in the field of gold nanoparticle-based diagnosis and therapy for cancer. Conventional treatment strategies for cancer cannot identify normal and cancer cells. While due to the high surface area to volume ratio and rich surface functionalization chemistry, gold nanoparticle can greatly enhance the targeting with adverse side effects of traditional treatment on normal tissues being avoided. CONCLUSION: Gold nanoparticles have greatly improved the traditional treatment due to their unique properties. However, their size-dependent toxicity, distribution and clearance need further studies to make them a clinical reality.