Chitin is one of the most abundant biomolecules on earth, occurring in crustacean shells and cell walls of fungi. While the polysaccharide is threatening to pollute coastal ecosystems in the form of accumulating shell-waste, it has the potential to be converted into highly profitable derivatives with applications in medicine, biotechnology, and wastewater treatment, among others. Traditionally this is still mostly done by the employment of aggressive chemicals, yielding low quality while producing toxic by-products. In the last decades, the enzymatic conversion of chitin has been on the rise, albeit still not on the same level of cost-effectiveness compared to the traditional methods due to its multi-step character. Another severe drawback of the biotechnological approach is the highly ordered structure of chitin, which renders it nigh impossible for most glycosidic hydrolases to act upon. So far, only the Auxiliary Activity 10 family (AA10), including lytic polysaccharide monooxygenases (LPMOs), is known to hydrolyse native recalcitrant chitin, which spares the expensive first step of chemical or mechanical pre-treatment to enlarge the substrate surface. The main advantages of enzymatic conversion of chitin over conventional chemical methods are the biocompability and, more strikingly, the higher product specificity, product quality, and yield of the process. Products with a higher M due to no unspecific depolymerisation besides an exactly defined degree and pattern of acetylation can be yielded. This provides a new toolset of thousands of new chitin and chitosan derivatives, as the physio-chemical properties can be modified according to the desired application. This review aims to provide an overview of the biotechnological tools currently at hand, as well as challenges and crucial steps to achieve the long-term goal of enzymatic conversion of native chitin into specialty chemical products.
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http://dx.doi.org/10.3390/md18020093 | DOI Listing |
Foods
January 2025
State Key Laboratory of Food Science and Resources, Engineering Research Center for Biomass Conversion, Ministry of Education, Nanchang University, Nanchang 330047, China.
In order to overcome the bioavailability limitation of polysaccharide (LPS) caused by its high molecular weight and complex structure, two low-molecular-weight degraded polysaccharides, namely G-LPS(8) and G-LPS(16), were prepared through enzymatic degradation. The molecular weight of LPS was significantly reduced by enzymolysis, leading to increased exposure of internal functional groups and altering the molar ratio of its constituent monosaccharides. The results of antioxidant experiments showed that enzymatic hydrolysis had the potential to enhance the antioxidant performance of LPS.
View Article and Find Full Text PDFExp Hematol Oncol
January 2025
Jiangsu Provincial Key Laboratory of Critical Care Medicine, Advanced Institute for Life and Health, Center of Clinical Laboratory Medicine, Department of Pharmacy, School of Medicine, Zhongda Hospital, Southeast University, Nanjing, 210009, China.
Transfusion safety and blood typing continue to present significant challenges in clinical practice, including risks of incorrect blood transfusions and blood shortages. One promising solution is the enzymatic conversion of all red blood cell (RBC) types into universal O-type RBCs. However, the major obstacle to this strategy is the relatively low catalytic efficiency of the enzymes involved.
View Article and Find Full Text PDFNat Commun
January 2025
The Picower Institute for Learning and Memory, MIT, Cambridge, MA, USA.
Many essential proteins require pyridoxal 5'-phosphate, the active form of vitamin B6, as a cofactor for their activity. These include enzymes important for amino acid metabolism, one-carbon metabolism, polyamine synthesis, erythropoiesis, and neurotransmitter metabolism. A third of all mammalian pyridoxal 5'-phosphate-dependent enzymes are localized in the mitochondria; however, the molecular machinery involved in the regulation of mitochondrial pyridoxal 5'-phosphate levels in mammals remains unknown.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
January 2025
School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, Jiangsu, China.
As the chip of synthetic biology, enzymes play a vital role in the bio-manufacturing industry. The development of diverse functional enzymes can provide a rich toolbox for the development of synthetic biology. This article reports the construction of an artificial enzyme with the introduction of a non-natural cofactor.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
January 2025
School of Life Sciences, Anhui University, Hefei 230000, Anhui, China.
The high content of sucrose and raffinose reduces the prebiotic value of soybean oligosaccharides. Fructan sucrases can catalyze the conversion of sucrose and raffinose to high-value products such as fructooligosaccharides and melibiose. To obtain a fructan sucrase that can efficiently convert soybean oligosaccharides, we first mined the fructan sucrase gene from microorganisms in the coastal areas of Xisha Islands and Bohai Bay and then characterized the enzymatic and catalytic properties of the enzyme.
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