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Keywords = xanthanase

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14 pages, 2679 KiB  
Article
Whole-Cell PVA Cryogel-Immobilized Microbial Consortium LE-C1 for Xanthan Depolymerization
by Elena V. Zhurishkina, Elena V. Eneyskaya, Svetlana V. Shvetsova, Lyudmila V. Yurchenko, Kirill S. Bobrov and Anna A. Kulminskaya
Catalysts 2023, 13(9), 1249; https://doi.org/10.3390/catal13091249 - 29 Aug 2023
Cited by 3 | Viewed by 1696
Abstract
Xanthan is an extracellular heteropolysaccharide produced by the bacteria Xanthomonas campestris. Due to its unique properties, the polysaccharide and its derivatives are widely used in many industries, from food to biomedicine and oil production, that demands an efficient xanthan depolymerization method to [...] Read more.
Xanthan is an extracellular heteropolysaccharide produced by the bacteria Xanthomonas campestris. Due to its unique properties, the polysaccharide and its derivatives are widely used in many industries, from food to biomedicine and oil production, that demands an efficient xanthan depolymerization method to adapt this polysaccharide for various applications. Unlike the known chemical approaches, biological methods are considered to be more environmentally friendly and less energy intensive. In laboratory conditions, we have isolated a bacterial community capable of reducing the xanthan viscosity. Identification of the individual isolates in the microbial community and their testing resulted in the consortium LE-C1, consisting of two microorganisms Paenibacillus phytohabitans KG5 and Cellulosimicrobium cellulans KG3. The specific activities of the overall xanthanase and auxiliary enzymes that may be involved in the xanthan depolymerization were as follows: xanthanase, 19.6 ± 0.6 U/g; β-glucosidase, 3.4 ± 0.1 U/g; α-mannosidase, 68.0 ± 2.0 U/g; β-mannosidase, 0.40 ± 0.01 U/g; endo-glucanase, 4.0 ± 0.1 U/g; and xanthan lyase, 2.20 ± 0.07 U/mg. In order to increase the efficiency of xanthan biodegradation, the LE-C1 whole cells were immobilized in a poly(vinyl alcohol) cryogel. The resulting regenerative biocatalyst was able to complete xanthan depolymerization within 40 cycles without loss of activity or degradation of the matrix. Full article
(This article belongs to the Special Issue Enzymatic Catalysis in Bio-Based Chemicals Production)
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17 pages, 24865 KiB  
Article
An Insight into the Essential Role of Carbohydrate-Binding Modules in Enzymolysis of Xanthan
by Xin Ni, Tong Fu, Xueyan Wang, Jingjing Zhao, Zhimin Yu, Xianzhen Li and Fan Yang
Int. J. Mol. Sci. 2023, 24(6), 5480; https://doi.org/10.3390/ijms24065480 - 13 Mar 2023
Cited by 4 | Viewed by 2013
Abstract
To date, due to the low accessibility of enzymes to xanthan substrates, the enzymolysis of xanthan remains deficient, which hinders the industrial production of functional oligoxanthan. To enhance the enzymatic affinity against xanthan, the essential role of two carbohydrate binding modules—MiCBMx [...] Read more.
To date, due to the low accessibility of enzymes to xanthan substrates, the enzymolysis of xanthan remains deficient, which hinders the industrial production of functional oligoxanthan. To enhance the enzymatic affinity against xanthan, the essential role of two carbohydrate binding modules—MiCBMx and PspCBM84, respectively, derived from Microbacterium sp. XT11 and Paenibacillus sp. 62047—in catalytic properties of endotype xanthanase MiXen were investigated for the first time. Basic characterizations and kinetic parameters of different recombinants revealed that, compared with MiCBMx, PspCBM84 dramatically increased the thermostability of endotype xanthanase, and endowed the enzyme with higher substrate affinity and catalytic efficiency. Notably, the activity of endotype xanthanase was increased by 16 times after being fused with PspCBM84. In addition, the presence of both CBMs obviously enabled endotype xanthanase to produce more oligoxanthan, and xanthan digests prepared by MiXen-CBM84 showed better antioxidant activity due to the higher content of active oligosaccharides. The results of this work lay a foundation for the rational design of endotype xanthanase and the industrial production of oligoxanthan in the future. Full article
(This article belongs to the Special Issue Microbial Enzymes for Biotechnological Applications)
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13 pages, 1538 KiB  
Article
Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
by Huiqin Huang, Zhiguo Zheng, Xiaoxiao Zou, Zixu Wang, Rong Gao, Jun Zhu, Yonghua Hu and Shixiang Bao
Mar. Drugs 2022, 20(6), 388; https://doi.org/10.3390/md20060388 - 9 Jun 2022
Cited by 8 | Viewed by 3528
Abstract
Carbohydrate-active enzymes (CAZymes) are an important characteristic of bacteria in marine systems. We herein describe the CAZymes of Paenibacillus algicola HB172198T, a novel type species isolated from brown algae in Qishui Bay, Hainan, China. The genome of strain HB172198T is [...] Read more.
Carbohydrate-active enzymes (CAZymes) are an important characteristic of bacteria in marine systems. We herein describe the CAZymes of Paenibacillus algicola HB172198T, a novel type species isolated from brown algae in Qishui Bay, Hainan, China. The genome of strain HB172198T is a 4,475,055 bp circular chromosome with an average GC content of 51.2%. Analysis of the nucleotide sequences of the predicted genes shows that strain HB172198T encodes 191 CAZymes. Abundant putative enzymes involved in the degradation of polysaccharides were identified, such as alginate lyase, agarase, carrageenase, xanthanase, xylanase, amylases, cellulase, chitinase, fucosidase and glucanase. Four of the putative polysaccharide lyases from families 7, 15 and 38 were involved in alginate degradation. The alginate lyases of strain HB172198T exhibited the maximum activity 152 U/mL at 50 °C and pH 8.0, and were relatively stable at pH 7.0 and temperatures lower than 40 °C. The average degree of polymerization (DP) of the sodium alginate oligosaccharide (AOS) degraded by the partially purified alginate lyases remained around 14.2, and the thin layer chromatography (TCL) analysis indicated that it contained DP2-DP8 oligosaccharides. The complete genome sequence of P. algicola HB172198T will enrich our knowledge of the mechanism of polysaccharide lyase production and provide insights into its potential applications in the degradation of polysaccharides such as alginate. Full article
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