@article { ISI:000237610600013,
	title = {Purification, characterization and substrate specificity of thermostable alpha-galactosidase from Bacillus stearothermophilus (NCIM-5146)},
	journal = {Process Biochemistry},
	volume = {41},
	number = {6},
	year = {2006},
	month = {JUN},
	pages = {1311-1317},
	publisher = {ELSEVIER SCI LTD},
	type = {Article},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>An extracellular thermostable alpha-galactosidase from Bacillus stearothermophilus (NCIM-5146) has been purified to homogeneity by chromatographic step, using Phenyl Sepharose CL-4B column. The specific activity of the enzyme was increased approximately 389-fold, from 1.03 U/mg protein to 400 U/mg protein. The molecular mass of the purified enzyme as determined by SDS-PAGE and gel filtration was 79.9 and 165.9 kDa, respectively, suggesting dimeric nature. The purified alpha-galactosidase is a non-glycosylated protein with a pI of 4.9. The pH and temperature optima for the purified enzyme are 6.5-7.0 and 65 degrees C, respectively. The alpha-galactosidase is stable over a broad pH range (3-9) and its half-life of inactivation (t(1/2)) at 70 degrees C is 30 min. The partial N-terminal sequence of alpha-galactosidase showed remarkable homology (80\% similarity) with earlier reported alpha-galactosidase from B. stearothermophilus NUB 3621. The secondary structure of the enzyme determined by circular dichroism (CD) spectroscopy exhibited alpha/beta class of protein and showed temperature induced conformational forms below and above the transition temperature. The purified enzyme showed biphasic Arrhenius plot with break point at 55 degrees C for pNPG and 50 degrees C for melibiose, raffinose and stachyose. The enzyme hydrolyzes alpha-1-3, alpha-1-4, and alpha-1-6 galactosidic linkages and not the beta-galactosidic linkages. Synthetic substrates pNPG and oNPG had lower K-m and higher K-cat as compare to natural substrates, melibiose, raffinose, and stachyose. (c) 2006 Elsevier Ltd. All rights reserved.</p>},
	keywords = {alpha-galactosidase, Bacillus stearothermophilus (NCIM-5146), Purification, Secondary structure, thermostable enzyme},
	issn = {1359-5113},
	doi = {10.1016/j.procbio.2006.01.003},
	author = {Gote, M. M. and Khan, Mohammad Islam and Gokhale, D. V. and Bastawade, Kulbhushan B. and Khire, Jayant Malhar}
}
@article { ISI:000243572800014,
	title = {Purification and characterization of a lectin from endophytic fungus fusarium solani having complex sugar specificity},
	journal = {Archives of Biochemistry and Biophysics },
	volume = {457},
	number = {2},
	year = {2007},
	month = {JAN},
	pages = {243-251},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>A lectin from the mycelial extract of an endophytic strain of Fusarium solani was purified. Its hemagglutinating activity was inhibited by glycoproteins possessing N-linked as well as O-linked glycans. The thermodynamics and kinetics of binding of glycans and glycoproteins to F. solani lectin Was Studied using SUH ace plasmon resonance. The lectin showed high affinity for asialofetuin, asia-lofibrinogen, asialofibrinogen, and thyroglobulin: and comparatively low affinity for mucin, fetuin, fibrinogen, and holotransferrin. Glycoproteins showed glycans with significant contribution from enthalpy and positive entropy, suggesting several fold higher affinity than their corresponding g the involvement of non-polar protein-protein interaction. Moreover, the higher affinity of the glycoproteins was due to their faster association rates and low activation energy. (c) 2006 Elsevier Inc. All rights reserved.</p>},
	keywords = {endophytic fungus, Fusarium solani, Lectin, Purification, SPR, Thermodynamic properties},
	issn = {0003-9861},
	doi = {10.1016/j.abb.2006.10.019},
	author = {Khan, Feroz and Ahmad, Absar and Khan, Mohammad Islam}
}
