NDLI: Characterization of β-N-Acetylhexosaminidase from rhizostomous jellyfish, Rhopilema asamushi, Mesogloea

Content Provider	Springer Nature Link
Author	Nagai, Takeshi Watarai, Yuko Suzuki, butaka
Copyright Year	2001
Abstract	β-N-Acetylhexosaminidase (EC 3.2.1.52) was purified from rhizostomous jellyfish mesogloea and characterized. Using two purification steps, this enzyme was purified up to 27.4-fold with a recovery rate of 46% compared with crude extract. The molecular weight of the enzyme was estimated to be about 136 kDa, composed of subunit molecular weights of 68 kDa. The enzyme activity was inhibited by SH-reagents, indicating that it contains a SH-group in its active site. The enzyme has a high affinity for pNPGlcNAc with Km value of 0.021 mM. The rate of hydrolysis of N-acetylchito-oligosaccharides tended to decrease with increasing degree of polymerization of the substrate. The parameters of k cat were 92.0 s−1 for pNPGlcNAc, 38.2 s−1 for GlcNAc2, 14.0 s−1 for GlcNAc3, 4.1 s−1 for GlcNAc4, 1.6 s−1 for GlcNAc5, 0.9 s−1 for GlcNAc6, respectively. These results suggest that this β-N-acetylhexosaminidase is an exo-fashion hydrolytic enzyme involved in chitin degradation.
Starting Page	53
Ending Page	59
Page Count	7
File Format	PDF
ISSN	09201742
Journal	Fish Physiology and Biochemistry
Volume Number	25
Issue Number	1
e-ISSN	15735168
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2001-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Animal Biochemistry Hydrobiology Zoology Animal Anatomy / Morphology / Histology Animal Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Biochemistry Aquatic Science

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