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Purification and characterization of novel κ-carrageenase from marine Tamlana ***4

Chinese Journal of Oceanology and Limnology 2010年第6期28卷 1139-1145页

作者：孙飞雪马悦欣王颖刘倩 Key Laboratory of Mariculture Ministry of AgricultureDalian Ocean University

We isolated a bacterial strain （HC4） that is able to degrade k-carrageenan from a live specimen of the red alga Hyalosiphonia caespitosa. With 16S rRNA gene sequencing, we identified the strain as Tamlana sp., and then purified an extracellular K-carrageenase from a culture of Tamlana sp. HC4 by ammonium sulfate precipitation, Sephadex G-200 gel filtration chromatography, and DE-cellulose 52 anion-exchange chromatography. The purified enzyme yields a single band on SDS-PAGE with a molecular mass of 66.4 kDa. The optimal pH and temperature for κ-carrageenase activity are at 8.0 and 30~C, respectively. The enzyme is stable over the range ofpH 7.2-8.6 below 45℃. The enzyme activity is strongly inhibited by Zn2＋ and Cu2＋ at 1 mmol/L. The enzyme-catalyzed reaction follows Michaelis-Menten kinetics with the Michaelis constant （Kin） at 7.63 mg/ml. Analysis of the degradation products of the κ-carrageenase by ESI-MS and 13C-NMR spectroscopy indicates that the enzyme degrades κ-carrageenan down to the level ofκ-neocarrabiose sulfate.

关键词： κ-carrageenase Tamlana purification characterization

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Expanding the application range of theκ‑carrageenase OUC‑FaKC16A when preparing oligosaccharides fromκ‑carrageenan and furcellaran

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Marine Life Science & Technology 2023年第3期5卷 387-399页

作者： Chengcheng Jiang Francesco Secundo Xiangzhao Mao College of Food Science and Engineering Ocean University of ChinaQingdao 266003China Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology Qingdao 266237China Key Laboratory for Biological Processing of Aquatic Products China National Light IndustryQingdao 266237China Istituto di Scienze e Tecnologie Chimiche“Giulio Natta” Consiglio Nazionale delle RicercheVia Mario Bianco 920131 MilanItaly

Carrageenan oligosaccharides are important products that have demonstrated numerous bioactivities useful in the food,medicine,and cosmetics ***,the specifc structure–function relationships of carrageenan oligosaccharides are not clearly described due to the defciency of high specifc ***,a truncated mutant OUC-FaKC16Q based on the reportedκ-neocarratetrose(Nκ4)-producingκ-carrageenase OUC-FaKC16A from Flavobacterium algicola was constructed and further *** truncating the C-terminal Por_Secre_tail(PorS)domain(responsible for substrate binding),the catalytic efciency and temperature stability decreased to a certain ***,this truncation also enabled OUC-FaKC16Q to hydrolyze Nκ4 intoκ-neocarrabiose(Nκ2).The ofset of Arg265 residue in OUC-FaKC16Q may explain this ***,the high catalytic abilities,the main products,and the degradation modes of OUC-FaKC16A and OUC-FaKC16Q toward furcellaran were also *** suggested OUC-FaKC16A and OUC-FaKC16Q could hydrolyze furcellaran to produce mainly the desulfated oligosaccharides DA-G-(DA-G4S)2 and DA-G-DA-G4S,*** a result,the spectrum of products ofκ-carrageenase OUC-FaKC16A has been fully expanded in this study,indicating its promising potential for application in the biomanufacturing of carrageenan oligosaccharides with specifc structures.

关键词： Carrageenan oligosaccharides κ-carrageenase Expression Degradation mode Desulfated oligosaccharides

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