| Autor: |
Li, Chen, Tang, Tiancheng, Jiang, Jinju, Yao, Zhong, Zhu, Benwei |
| Předmět: |
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| Zdroj: |
Glycobiology; Oct2023, Vol. 33 Issue 10, p837-845, 9p |
| Abstrakt: |
Ulva is globally distributed specie and has a high economic value. Ulvan is one of the main active substances in Ulva , which has a variety of biological properties. Ulvan lyase degrades ulvan through a β-elimination mechanism which cleaves the β-glycosidic bond between Rha3S and GlcA or IdoA. The complex monosaccharide composition of ulvan makes it promising for use in food and pharmaceutical applications. This thesis explores a putative ulvan lyase from Alteromonas sp. KUL_42. We expressed and purified the protein, performed a series of characterizations and signal peptide had been removed. The results showed that the protein molecular weight of ULA-2 was 53.97 kDa, and it had the highest catalytic activity at 45 °C and pH 8.0 in Tris–HCl buffer. The K m and V max values were 2.24 mg · mL−1 and 2.048 μmol · min−1 · mL−1, respectively. The activity of ULA-2 was able to maintain more than 80% at 20 ~ 30 °C. ESI-MS analysis showed that the primary end-products were mainly disaccharides to tetrasaccharides. The study of ULA-2 enriches the ulvan lyase library, promotes the development and high-value utilization of Ulva resources, and facilitates further research applications of ulvan lyase in ulva oligosaccharides. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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