என்சைம் பொறியியல்

என்சைம் பொறியியல்
திறந்த அணுகல்

ஐ.எஸ்.எஸ்.என்: 2329-6674

சுருக்கம்

Expectation of Michaelis-Menten Constant in Beta-Cellobiosidase's Response with Lactoside as Substrate

Von Ossowski

The Michaelis-Menten steady, Km, is essential to comprehend the attributes of catalyst and its relationship with substrates and various conditions in biochemical responses. Albeit the quick improvement is confirmed in enzymatic examination, the Km esteem in every protein under different conditions actually should be estimated separately. Then again, the cutting edge computational procedures and bioinformatics give the chance to hypothetically foresee Km in compound with various substrates under different conditions. Cellulose 1,4-beta-cellobiosidase is an protein utilized in cellulose hydrolysis for bio-fuel industry, and colossal endeavors are made to improve its productivity through looking for new strains of beta-cellobiosidase just as enzymatic designing. Along these lines it is thought of imperative to create techniques to foresee the Km esteem in beta-cellobiosidase's response. In this examination, the data of amino corrosive properties in beta-cellobiosidase, pH and temperature in response, and lactoside as substrate were picked as indicators to foresee the Km esteems by feedforward backpropagation neural organizations, and the erase 1 folding blade was utilized to approve the prescient model. The outcomes show that 11 of 25 checked amino corrosive properties could go about as indicators, and that the amino-corrosive dissemination likelihood seemed the best indicator. The two-layer construction of neural organization design was adequate for introductory filtering. In steady with past examinations, the Km estimation of enzymatic responses was unsurprising utilizing compound arrangement data and response conditions with neural organization models.

மறுப்பு: இந்த சுருக்கமானது செயற்கை நுண்ணறிவு கருவிகளைப் பயன்படுத்தி மொழிபெயர்க்கப்பட்டது மற்றும் இன்னும் மதிப்பாய்வு செய்யப்படவில்லை அல்லது சரிபார்க்கப்படவில்லை.
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