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Hokkaido University Collection of Scholarly and Academic Papers >
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Isolation and characterization of two alginate lyase isozymes, AkAly28 and AkAly33, from the common sea hare Aplysia kurodai
| Title: | Isolation and characterization of two alginate lyase isozymes, AkAly28 and AkAly33, from the common sea hare Aplysia kurodai |
| Authors: | Rahman, Mohammad Matiur Browse this author | | Inoue, Akira Browse this author →KAKEN DB | | Tanaka, Hiroyuki Browse this author →KAKEN DB | | Ojima, Takao Browse this author →KAKEN DB |
| Keywords: | Aplysia kurodai | | Gastropod | | Alginate lyase | | PL-14 | | Alginate | | Brown seaweed |
| Issue Date: | Dec-2010 |
| Publisher: | Elsevier |
| Journal Title: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
| Volume: | 157 |
| Issue: | 4 |
| Start Page: | 317 |
| End Page: | 325 |
| Publisher DOI: | 10.1016/j.cbpb.2010.07.006 |
| PMID: | 20708706 |
| Abstract: | Two alginate lyase isozymes, AkAly28 and AkAly33, with approximate molecular masses of 28 and 33 kDa, respectively, were isolated from the digestive fluid of the common sea hare, Aplysia kurodai. Both of AkAly28 and AkAly33 were regarded as the endolytic polymannuronate (poly(M)) lyase (EC 4.2.2.3) since they preferably degraded poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreased the viscosity of sodium alginate solution in the initial phase of degradation. Optimal pH and temperature of the two enzymes were similarly observed at pH 6.7 and 40 °C, respectively. Temperature that caused a half inactivation of the two enzymes during 20-min incubation was also similar to each other, i.e., 38 °C. However, NaCl requirement and activity toward oligosaccharide substrates of the two enzymes were significantly different from each other. Namely, AkAly28 showed practically no activity in the absence of NaCl and the maximal activity at NaCl concentrations higher than 0.2 M, whereas AkAly33 showed ~ 20% of maximal activity despite the absence of NaCl and the maximal activity at around 0.1 M NaCl. AkAly28 hardly degraded oligosaccharides smaller than tetrasaccharide, while AkAly33 could degrade oligosaccharides larger than disaccharide producing disaccharide and 2-keto-3-deoxy-gluconaldehyde (an open chain form of unsaturated monosaccharide). Analysis of the N-terminal and internal amino-acid sequences of AkAly28 and AkAly33 indicated that both of the two enzymes belong to polysaccharide lyase family 14. |
| Relation: | http://www.elsevier.com/locate/cbpb |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/44107 |
| Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 尾島 孝男
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