A new member of family 8 polysaccharide lyase chondroitin AC lyase (PsPL8A) from Pedobacter saltans displays endo- and exo-lytic catalysis

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• 作者：Aruna Rani ; Arun Goyal ; ^{arungoyl@iitg.ernet.in}
• 关键词：ECM ; extracellular matrix ; GAG ; glycosaminoglycan ; GlcNAc ; N-acetyl glucosamine ; GalNAc ; N-acetyl galactosamine ; GlcA ; d-glucuronic acid ; IdoA ; l-iduronic acid ; CS ; chondroitin sulphate ; DS ; dermatan sulphate ; C4S ; chondroitin 4-sulphate ; C6S ; chondroitin 6-sulphate ; TLC ; thin layer chromatography ; IMAC ; immobilized metal-ion affinity chromatography ; NMR ; nuclear magnetic resonance ; ESI&ndash ; MS ; Electron Spray Ionization-Mass Spectrometry
• 刊名：Journal of Molecular Catalysis B: Enzymatic
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：134
• 期：part_PA
• 页码：215-224
• 全文大小：1862 K
• 卷排序：134

文摘

PsPL8A is the first chondroitin AC lyase characterized from Pedobacter saltans. PsPL8A retains 85% activity or more at human physiological temperature and pH. PsPL8A enzyme activity is enhanced by 2 fold by Ca2+ and Na+ ions. PsPL8A displayed concomitant endo- and exo-lytic mode of catalysis. Di-, hexa-, octa- and dodeca-saccharides products of C4S were obtained by PsPL8A.