Characterization of Hyaluronan-Degrading Enzymes from Yeasts

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• 作者：Dzianis Smirnou ; Martin Kr?má? ; Jaromír Kulhánek…
• 关键词：Hyaluronate 4 ; glycanohydrolase ; Lyase ; Characteristics ; Thermostability ; Pseudozyma aphidis ; Cryptococcus laurentii
• 刊名：Applied Biochemistry and Biotechnology
• 出版年：2015
• 出版时间：October 2015
• 年：2015
• 卷：177
• 期：3
• 页码：700-712
• 全文大小：930 KB
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• 作者单位：Dzianis Smirnou (1)
  Martin Kr?má? (1)
  Jaromír Kulhánek (2)
  Martina Hermannová (2)
  Lenka Bobková (1)
  Luká? Franke (1)
  Stanislav Pepeliaev (1)
  Vladimír Velebny (3)
  
  1. Contipro Biotech s.r.o., Dolní Dobrou? 401, 561 02, Dolní Dobrou?, Czech Republic
  2. Contipro Pharma a.s., Dolní Dobrou? 401, 561 02, Dolní Dobrou?, Czech Republic
  3. Contipro Group s.r.o., Dolní Dobrou? 401, 561 02, Dolní Dobrou?, Czech Republic
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Biochemistry
  
• 出版者：Humana Press Inc.
• ISSN：1559-0291

文摘

Hyaluronidases (HAases) from yeasts were characterized for the first time. The study elucidated that hyaluronate 4-glycanohydrolase and hyaluronan (HA) lyase can be produced by yeasts. Six yeasts producing HAases were found through express screening of activities. The extracellular HAases from two of the yeast isolates, Pseudozyma aphidis and Cryptococcus laurentii, were characterized among them. P. aphidis HAase hydrolyzed β-1,4 glycosidic bonds of HA, yielding even-numbered oligosaccharides with N-acetyl-d-glucosamine at the reducing end. C. laurentii produced hyaluronan lyase, which cleaved β-1,4 glycosidic bonds of HA in β-elimination reaction, and the products of HA degradation were different-sized even-numbered oligosaccharides. The shortest detected HA oligomer was dimer. The enzymes-pH and temperature optima were pH 3.0 and 37-5 °C (P. aphidis) and pH 6.0 and 37 °C (C. laurentii), respectively. Both HAases showed good thermostability. Keywords Hyaluronate 4-glycanohydrolase Lyase Characteristics Thermostability Pseudozyma aphidis Cryptococcus laurentii