BACKGROUND Starch, a homopolysaccharide is an important and an abundant food reserve and energy source. Starches are processed to yield different products which find many industrial applications. Alpha-amylases hydrolyze starch by cleaving α-1,4-glucosidic bonds and have been used in food, textile and pharmaceutical industries [Sun et al. 2010]. Enzymatic conversion of starch with amylase prese...

Two different xylanases, CX-I and CX-II, from an alkalophilic fungus, Cephalosporium sp. strain RYM-202, have been purified to homogeneity. The enzymes had similar pH (7.5 to 8.0) and temperature (50(deg)C) optima and were stable over a wide pH range of 5.5 to 12.0. Both enzymes were shown to be cellulase-free endoxylanases with transglycosidation activity.

This paper reports high level production of a cellulase-free xylanase using wheat bran, a cost-effective substrate, under submerged fermentation by alkalophilic Bacillus subtilis ASH. Production of xylanase was observed even at alkaline pH up to 11.0 and temperature 60 °C, although the highest enzyme titer was recorded at neutral pH and 37 °C. The enzyme production under optimized fermentation ...

In an effort to improve the properties of cyclodextrin glucanotransferase (CGTase) as an antistaling enzyme, error-prone PCR was used to introduce random mutations into a CGTase cloned from alkalophilic Bacillus sp. I-5 (CGTase I-5). A mutant CGTase[3-18] with the three mutations M234T, F259I and V591A was selected by agar plate assay. Sequence alignment of various CGTases indicated that M234 a...

An alkalophilic bacterium, Bacillus cereus produced an extracellular alkaline protease, which was found to be active at high temperature and pH range, suitable for commercial laundry detergents. B. cereus protease was partitioned in different aqueous two-phase systems such as PEG/dextran, PEG/potassium phosphate, PEG/sodium citrate, PEG/magnesium sulphate and PEG/sodium dihydrogen phosphate and...

To understand the molecular basis of higher pH catalytic adaptation of family 11 xylanases, we compared the structures of alkaline, neutral, and acidic active xylanases and analyzed mutants of xylanase Xyn11A-LC from alkalophilic Bacillus sp. SN5. It was revealed that alkaline active xylanases have increased charged residue content, an increased ratio of negatively to positively charged residue...

A gene coding for xylanase activity, xynA, from the anaerobic ruminal bacterium Butyrivibrio fibrisolvens 49 was cloned into Escherichia coli JM83 by using plasmid pUC19. The gene was located on a 2.3-kilobase (kb) DNA insert composed of two adjacent EcoRI fragments of 1.65 and 0.65 kb. Expression of xylanase activity required parts of both EcoRI segments. In E. coli, the cloned xylanase enzyme...