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Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Crustaceans are common arthropods used in biotechnological and molecular research. Crabs, shrimp, lobsters, krill, and barnacles are all found in this category. β -N-acetylhexosaminidase and chitinase are two forms of chitinolytic enzymes found in the liver, pancreas, and crustacean integument. Chitinolytic mechanisms in the integument have been shown to play an important role in molting and ingestion of chitin-containing foods in the hepatopancreas. While marine zooplankton are intended to shed on a regular basis, there is a considerable amount of abandoned chitin, which can be a major carbon source and energy source for chitin-degrading microbes’ development and reproduction. Chitin synthesis in the entire marine biocycle is estimated at approximately 2.3 million metric tons per year. Researchers have discovered a broad variety of microorganisms capable of producing chitinase, such as Arthrobacter, Clostridium Penicillium, Serratia, Rhizopus, Sporocytophaga, Pseudomonas, Bacillus, Enterobacter, Klebsiella, Flavobacterium, Streptomyces, Aspergillus, Chromobacterium, Myxobacter, Vibrio fluvialis, Vibrio alginolyticus, Aeromonas hydrophila, Vibrio mimicus, Listonella anguillarum and Vibrio parahaemolyticus. Direct application of chitinolytic enzymes (e.g., antifungals) and hydrolysis of chitin into chitooligosaccharides are the two main applications of chitinolytic enzymes. In this case, the chitooligosaccharides’ chemical structure has a significant impact on their function.
Industrial Applications of Fungal Chitinases: An Update
Published in Devarajan Thangadurai, Jeyabalan Sangeetha, Industrial Biotechnology, 2017
Mishra Padmanabh, S. K. Singh, Smita S. Nilegaonkar
During recent times, chitinases have gained interest in different biotechnological applications due to their ability to degrade chitin in the fungal cell wall and insect exoskeleton, leading to their use as antimicrobial or insecticidal agents (Karasuda et al., 2003; Mostafa et al., 2009). Another interesting application of chitinase is for bioconversion of chitin, a cheap biomaterial, into pharmacological active products, namely GlcNAc and chito-oligosaccharides (Bhattacharya et al., 2007). Production of chitin derivatives with suitable enzymes is more appropriate for sustaining the environment than using chemical reactions (Songsiriritthigul et al., 2009). Other interesting applications include the preparation of protoplasts from filamentous fungi, bio-control of insects and mosquitoes as well as the production of SCP (Dahiya et al., 2006; Hayes et al., 2006). Thus, there have been many reports on cloning, expression and characterization of chitinases from various organisms, including bacteria, fungi, plants and animals (Deshpande, 1986; Fukamizo, 2000). The major applications of chitinases are discussed and summarized in Figure 7.2.
Factors Responsible for Spatial Distribution of in Soil
Published in Suhaib A. Bandh, Javid A. Parray, Nowsheen Shameem, Climate Change and Microbial Diversity, 2023
Chitin is the most abundant polysaccharide after cellulose in nature and basically found in the exoskeleton region of different insects, fungi, yeast, algae, and in the internal structures of vertebrates. Chitinase are the enzymes that degrade chitin thus contributing in carbon and nitrogen cycle. These enzymes have great importance in controlling pathogens of agricultural lands (Hamid et al., 2013). Saprophytic soil bacteria Actinobacteria are the most important taxa among soil microbial community for synthesizing Chitinase enzyme (Bai et al., 2016). In terms of Chitinase activity, streptomyces is the most abundant genera of actinobacteria (Brzezinska et al., 2013). Apart from these, Bacillus thuringenesis is also an important source of chitinase enzymes which is used as bioinsectiside in agriculture (Veliz et al., 2017). Chitin catabolism takes place in two steps; initially, chitin polymers are cleaved by chitinase into chitin oligosaccharides and then further cleaved by chitobiases into N-acetylglucosamine and monosaccharides (Chen et al., 2010). Chitinase have been categorized into two main groups; endochitinase and exochitinase. The endochitinase randomly cleaves chitin at the internal sites, thus forming dicetylchitobiose dimer and soluber multimers of GlcNAc, such as chitotriose and chitotetrose (Sasaki et al., 2006). Exochitinase has been further divided into two more subcategories; chitobiosidase, involved in catalyzing release of diacetylchitibiose progressively from the nonreducing end of chitin microfibril. The second one is 1,4-ß-glucosaminidase, cleaving the oligomeric product of endochitinase and chitobiosidase into monomers of GlcNAc (Hamid et al., 2013).
Purification and characterization of Stenotrophomonas maltophilia chitinase with antifungal and insecticidal properties
Published in Preparative Biochemistry & Biotechnology, 2023
Cigdem Aktas, Damla Ruzgar, Sumeyra Gurkok, Arzu Gormez
Exo-chitinases, produced by bacteria and archaea and resistant to extreme conditions (pH, temperature, high salt concentrations, etc.), are often preferred in biotechnological processes and are used in studies. Mainly, it has been reported that chitinases belong to the different genera such as Alteromonas, Aeromonas, Arthrobacter, Beneckea, Bacillus, Chromobacterium, Clostridium, Escherichia, Klebsiella, Paenibacillus, Pseudomonas, Serratia, Stenotrophomonas, Streptomyces, and Vibrio[6,14,15] and some of them have been used in biotechnological areas. In recent years, some studies have used the chitinase enzyme against fungi and especially insect pests that cause important diseases in the agricultural field.[16–20]
Purification and characterization of chitinase produced by thermophilic fungi Thermomyces lanuginosus
Published in Preparative Biochemistry & Biotechnology, 2022
Nisha Suryawanshi, J. Satya Eswari
The purified enzyme was characterized for the effect of different pH, temperature, time, and metal ions on the activity and stability of chitinase. With different substrate concentration the chitinase activity was found to be increased with increase in substrate concentration. For the activity test at different time duration the enzyme activity was found highest in 30 min after that the activity started decreasing. For different temperature and pH, the effect on chitinase activity was also analyzed and it was observed that chitinase activity was highest at 50 °C and it was more stable at the same temperature. In case of pH the activity and stability of chitinase both were found highest at pH 3 and 4. The effect on chitinase activity was also observed in presence of different metal ions and chemical compounds. It was observed that the Mn2+, and Fe3+ have not shown any effect whereas Mg2+, Ca2+, and K + showed very less effect on chitinase activity. The Cu2+ and Hg2+ were found to reduce the chitinase activity. In case of chemical compounds β-ME was found to enhance the activity of chitinase and the Tween 20, Tween 80 and SDS showed very less effect while EDTA found to reduce the chitinase activity. Hence, it concludes that Cu2+, Hg2+ and EDTA have inhibitory effect on chitinase activity, whereas β-ME act as activator for chitinase activity.
Chaperone-assisted soluble expression and characterization of chitinase chiZJ408 in Escherichia coli BL21 and the chitin degradation by recombinant enzyme
Published in Preparative Biochemistry & Biotechnology, 2022
Ping Yu, Xinxin Wang, Jian Ma, Qili Zhang, Qingwei Chen
Chitinase can degrade chitin to chito-oligosaccharides which are beneficial to human beings.[7] Chito-oligosaccharides have the functions of improving the body’s immunity,[8] inhibiting tumor cells,[9] anti-coagulation and anti-thrombotic, lowering blood lipids, reducing cholesterol and anti-infective effect,[10] and are widely used in food, pharmaceutical, and medical fields. Chitinase comes from a wide range of sources and has been found in bacteria, fungi, protozoa, viruses, arthropods, and plants.[11] The use of biological enzymes instead of chemical methods to degrade chitin resources can reduce costs and pollution and improve product purity. It allows the production of specific chitin oligosaccharides in a controlled way and environmentally friendly process.[12,13] However, most of the currently isolated chitinases often suffer from low activity. Wild-type chitinases are expensive to purify, making them difficult to use in industrial production. The production of chitinase by genetic engineering has the advantages of high yield, single product, and easy separation. Therefore, the expression of chitinase-encoding genes through genetic engineering is expected to obtain a lot of chitinases.