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Characterization of a thermostable κ‐carrageenase from a hot spring bacterium and plant protection activity of the oligosaccharide enzymolysis product
Journal of the science of food and agriculture, 2019-03, Vol.99 (4), p.1812-1819
Li, Jiang
Pan, Aihong
Xie, Maisheng
Zhang, Pingping
Gu, Xiaoqian
2019
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Li, Jiang
Pan, Aihong
Xie, Maisheng
Zhang, Pingping
Gu, Xiaoqian
Titel
Characterization of a thermostable κ‐carrageenase from a hot spring bacterium and plant protection activity of the oligosaccharide enzymolysis product
Ist Teil von
Journal of the science of food and agriculture, 2019-03, Vol.99 (4), p.1812-1819
Ort / Verlag
Chichester, UK: John Wiley & Sons, Ltd
Erscheinungsjahr
2019
Quelle
Wiley-Blackwell Journals
Beschreibungen/Notizen
Background Seaweed oligosaccharides are environmentally‐friendly natural products and their use for disease control in sustainable agriculture is extremely promising. Enzymatic digestion to prepare seaweed oligosaccharides has drawn considerable interest. However, the study of enzymatically degraded products of carrageenan is still in its infancy compared with that of other hydrocolloids such as agar and alginate. To prepare degraded carrageenan on a commercial scale, it is necessary to select superior producer bacterial strains to improve the yield and thermostability of carrageenases. Results The carrageenan‐degrading bacterium Bacillus sp. HT19 was isolated from sediment of a hot spring in Indonesia, and a κ‐carrageenase with high activity was purified from the culture supernatant. The purified enzyme, named Car19, had maximum activity (538 U mg−1) at 60 °C and pH 7.0. Notably, the enzyme retained >90% of its initial activity after incubation at 60 °C for 24 h. The Ca2+ obviously improved the thermostability of Car19 at 70 °C. The Km and Vmax values of purified Car19 were 0.061 mg mL−1 and 115.13 U mg−1, respectively, with κ‐carrageenan as substrate. Thin‐layer chromatography and electrospray ionization mass‐spectrometry analysis of hydrolysates indicated that the enzyme exolytically depolymerized κ‐carrageenan to neo‐carrabiose. The hydrolysate enhanced the resistance of cucumber to cucumber mosaic virus and increased the activity of antioxidant enzymes in infected plants. Conclusion To our knowledge, Car19 is the most thermostable κ‐carrageenase reported so far. Its high optimal reaction temperature and thermostability, and unitary hydrolysate constituent, makes Car19 a promising candidate for the preparation of carrageenan oligosaccharides with plant protection activity. © 2018 Society of Chemical Industry
Sprache
Englisch
Identifikatoren
ISSN: 0022-5142
eISSN: 1097-0010
DOI: 10.1002/jsfa.9374
Titel-ID: cdi_proquest_journals_2177547286
Format
–
Schlagworte
Algae
,
Alginates
,
Alginic acid
,
antioxidant enzymes
,
Antioxidants
,
Bacillus - chemistry
,
Bacillus - enzymology
,
Bacillus - genetics
,
Bacillus - isolation & purification
,
Bacteria
,
Bacterial Proteins - chemistry
,
Bacterial Proteins - isolation & purification
,
Bacterial Proteins - metabolism
,
Calcium
,
Calcium ions
,
Carrageenan
,
Carrageenan - chemistry
,
Carrageenan - metabolism
,
Carrageenan - pharmacology
,
carrageenan oligosaccharide
,
Chemical activity
,
cucumber mosaic virus
,
Cucumis sativus - virology
,
Cucumovirus - drug effects
,
Cucumovirus - physiology
,
Degradation
,
Depolymerization
,
Disease control
,
Disease resistance
,
Enzyme Stability
,
Enzymes
,
Enzymolysis
,
Glycoside Hydrolases - chemistry
,
Glycoside Hydrolases - isolation & purification
,
Glycoside Hydrolases - metabolism
,
Hot springs
,
Hot Springs - microbiology
,
Hot Temperature
,
Hydrolysates
,
Ionization
,
Kinetics
,
Natural products
,
Oligosaccharides
,
Oligosaccharides - chemistry
,
Oligosaccharides - metabolism
,
Oligosaccharides - pharmacology
,
Organic chemistry
,
Plant Diseases - prevention & control
,
Plant Diseases - virology
,
Plant protection
,
Seaweeds
,
Spectrometry
,
Substrates
,
Sustainable agriculture
,
Thermal stability
,
thermostability
,
Viruses
,
κ‐carrageenase
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