Abstract
In 1961, Campbell and Manning provided one clue to elucidate the molecular basis for thermostability of the enzyme from thermophile(1–3). They reported that the α-amylase of B. stearothermophilus in the native state exists in a semi-random or random coiled and well hydrated molecule with slight extent of secondary structure formed by disulfide bonds (2). This less-ordered structure was postulated as the reason for thermostability of the enzyme.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
