Recombinant production and characterisation of two chitinases from Rasamsonia emersonii, and assessment of their potential industrial applicability
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Chitinase
Thermostability
Molecular mass
The chitinases of rape seeds were separated by chitin affinity columns regenerated from three different molecular chitosans of 20 cPs, 276 cPs and 1,200 cPs. The chitinase of rape seeds occurred in the order of Ch1, Ch2, and Ch3 on SDS-PAGE. The protein contents recovered were 3.95, 1.59, and 1.90% from chitin affinity columns of 20, 276, and 1200 cPs, while the respective chitinase activities were 47.2, 80.9, and 60.2%. The hydrolysis products of seed chitinase observed on TLC plates primarily consisted of dimers and trimers after 12 hrs of incubation with swollen chitin, while they were primarily dimers and monomers on TLC plates after 12 hrs of incubation with chitin-oligomers. In conclusion, the highest recovery rate of the chitinase activity from rape was obtained using a chitin affinity column filled with 276 cPs chitosan, and the chitinase was a very specific enzyme for the selective production of GlcNAc monomers and dimers.
Chitinase
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Thermostability
Mesophile
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The one guaranteed property of enzymes isolated from extremely thermophilic micro-organisms is their thermostability. Most significantly, almost any such enzyme will be more thermostable than the functionally similar enzyme from a lower temperature source. Thermostability is not an isolated property: resistance to heat denaturation imparts stability to a number of other denaturing influences (detergents, organic solvents, etc). These characteristics of hyperthermophilic enzymes are the most likely basis for the development of new biotechnological applications. A limited number of hyperthermophilic enzymes have found application in specialist biotechnological applications; others have visible potential in growing areas of biotechnology. Existing and potential applications are discussed using DNA manipulation enzymes, dehydrogenases, and esterases as examples.
Thermostability
Heat stability
Denaturation (fissile materials)
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Thermostability
Mesophile
Trichoderma harzianum
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Thermostability
Mesophile
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Thermostability
Enzyme Kinetics
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Thermostability
Asparaginase
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S. marcescens QM 81466 균주는 chitin 분해 효소(1mg/Lmedium)를 선택적으로 높게 생성시킬 수 있는 균주로서, chitin을 N-acetyl-B-D-glucosam mine(NAG)으로 효소적 가수분해를 할 때 chitinase와 chitobiase의 두 가지 가수분해 효소계를 구 성시킨다. 본 연구에서는 이 균주의 chitinase/chitobiase 생성을 위한 chitin 입자크기에 대한 최적화와, 회분 발효계에서 이 균주의 세포 밀도 배양에 따른 두 효소 생성의 변화를 조사하여 NAG 생산성의 증대를 시도하였다. 아울러. chitin과 CM chitin이 chitinase/chito biase 생성비 와 NAG 생성 에 미치는 영향을 검토하였는데, CM-chitin을 colloidal 및 결정성 chitin 대신에 사용했을 때, chitinase 활성을 약 7~10U/mL 증가시켰다. 이 경우에 있어서, chitinase/chitobiase의 비는 9:1로 서 NAG의 생성량이 3.0g/L로서 높게 나타났다.
Chitinase
N-Acetylglucosamine
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Chitinases, which can hydrolyze chitin, occur in a wide range of microorganisms including viruses, bacteria, and fungi.The derivatives of chitin are potentially useful in several areas such as food processing, medicines, and biological control in agriculture.Some bacteria can uptake and utilize chitin as carbon source by secreting chitinase.The chitin is degraded into chito-oligosaccharides [(GlcNAc) n ] or N-acetylglucosamine (GlcNAc) by chitinases, and then the chitin derivatives are transferred into cells by specific transport systems of bacteria.The intracellular chitin derivatives activate or suppress the transcription of a series of chi genes and affect the amount of chitinase.The expression of chitinase genes are strictly regulated by various regulatory factors and responsive cis-acting elements.The present review will focus on the transport system and the regulation of chitinase genes expression in bacteria.
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Thermostability
Thermus
Thermus thermophilus
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