@article { ISI:000243176500006,
	title = {Application of cellulases from an alkalothermophilic thermomonospora sp in biopolishing of denims},
	journal = {Biotechnology and Bioengineering},
	volume = {96},
	number = {1},
	year = {2007},
	month = {JAN},
	pages = {48-56},
	publisher = {JOHN WILEY \& SONS INC},
	type = {Article},
	address = {111 RIVER ST, HOBOKEN, NJ 07030 USA},
	abstract = {<p>Use of cellulase for denim washing is a standard eco-friendly technique to achieve desirable appearance and softness for cotton fabrics and denims. But enzymatic washing of denim till date involved acid cellulase (Trichoderma reesei) and neutral cellulase (Humicola isolens) the use of which has a drawback of backstaining of the indigo dye on to the fabric. Though it has been suggested that pH is a major factor in controlling backstaining there are no reports on use of cellulase under alkaline conditions for denim washing. In this study for the first time an alkali stable endoglucanase from alkalothermophilic Thermomonospora sp. (T-EG) has been used for denim biofinishing under alkaline conditions. T-EG is effective in removing hairiness with negligible weight loss and imparting softness to the fabric. Higher abrasive reactivity with lower backstaining was a preferred property for denim biofinishing exhibited by T-EG. The activities were comparable to acid and neutral cellulases that are being regularly used. The enzyme was also effective under non-buffering conditions which is an added advantage for use in textile industry. A probable mechanism of enzymatic finishing of cotton fabric has been represented based on the unique properties of T-EG.</p>},
	keywords = {alkaline conditions, biopolishing, Cellulase, denim, Thermomonospora sp},
	issn = {0006-3592},
	doi = {10.1002/bit.21175},
	author = {Anish, Ramakrishnan and Rahman, Mohammad Safikur and Rao, Mala}
}
@article { ISI:000272174500004,
	title = {Fluorescence study on interactions of alpha-crystallin with the molten globule state of 1, 4-beta-D-glucan glucanohydrolase from thermomonospora sp induced by guanidine hydrochloride},
	journal = {Journal of Fluorescence},
	volume = {19},
	number = {6},
	year = {2009},
	month = {NOV},
	pages = {967-973},
	publisher = {SPRINGER/PLENUM PUBLISHERS},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>In this paper, the interaction between alpha- crystallin and molten globule structure of 1,4-beta-D-Glucan Glucohydrolase (TSC) from an alkalothermophilic Thermomonospora sp. was investigated mainly by fluorescence quenching spectra, circular dichroism and three dimensional fluorescence spectra under simulative physiological conditions. Denaturation studies using GdnCl indicated that TSC folds through a partially folded state that resembles molten globule at 1.8 M GdnCl. The chaperone activity of alpha- crystallin was employed to study refolding of TSC. Here we studied the refolding of GdnCl denatured TSC from its molten globule state (TSC-m complex) in the presence and absence of alpha-crystallin to elucidate the molecular mechanism of chaperone-mediated in vitro folding. Our results, based on intrinsic tryptophan fluorescence and ANS binding studies, suggest that alpha-crystallin formed a complex with a putative intermediate molten globule - like intermediate in the refolding pathway of TSC. Reconstitution of the active TSC was observed on cooling the alpha-crystallin aEuro cent TSC -m complex to 4A degrees C. Addition of alpha-crystallin to the molten globule - like intermediate of TSC (TSC-m complex) complex initiated the refolding of TSC with 69 \% recovery of the biological activity of the enzyme.</p>},
	keywords = {ANS, Cellulase, Guanidine hydrochloride, Protein folding},
	issn = {1053-0509},
	doi = {10.1007/s10895-009-0496-5},
	author = {Jagtap, Sharmili and Rao, Mala}
}
