Review: cyclodextrins and their interaction with amylolytic enzymes.

This review is concerned with inhibition of amylases by cyclodextrins (cyclic maltooligosaccharides), the interaction that occurs between amylases and cyclodextrins and the application of cyclodextrin affinity chromatography in the purification of amylases. In many cases, amylases that are competitively inhibited by cyclodextrins can be purified by cyclodextrin affinity chromatography with the cyclodextrins interacting with the active site on such enzymes. Interestingly amylases that are not competitively inhibited by cyclodextrins may also be purified by cyclodextrin affinity chromatography.

The amylopullulanase of Bacillus sp. DSM 405.

The amylopullulanse produced by Bacillus sp. DSM 405 was purified to homogeneity. It exhibited dual activity, cleaving the alpha 1-4 bonds in starch, releasing a range of malto-oligosaccharides, and also cleaving the alpha 1-6 bonds in pullulan, releasing maltotriose as the sole end-product.

Effect of growth rate on alpha-amylase production by Streptomyces sp. IMD 2679.

The alpha-amylase of Streptomyces sp. IMD 2679 was subject to catabolite repression. Four different growth rates were achieved when the organism was grown at 40 degrees C and 55 degrees C in the presence and absence of cobalt, with an inverse relationship between alpha-amylase production and growth rate.

The high maltose-producing alpha-amylase of the thermophilic actinomycete, Thermomonospora curvata.

The alpha-amylase of Thermomonospora curvata catalyses the formation of very high levels of maltose from starch (73%, w/w) without the attendant production of glucose. The enzyme was produced extracellularly in high yield during batch fermentation in a 5-1 fermentor. Purification was achieved by ammonium sulphate fractionation, Superose-12 gel filtration and DEAE-Sephacel ion-exchange chromatography.

Investigation of the mechanisms of irreversible thermoinactivation of Bacillus stearothermophilus alpha-amylase.

Bacillus stearothermophilus NCIB 11412 produces a highly thermostable alpha-amylase. The enzyme displayed half-lives of irreversible thermoinactivation at 90 degrees C of 1.9 min and 12.

Dialysis culture for the production of Pseudomonas saccharophila alpha-amylase.

Growth and alpha-amylase synthesis of Pseudomonas saccharophila was shown to be inhibited by the accumulation of a mixture of nonvolatile fatty acids during nondialysis cultivation. Using dialysis culture a 9-fold increase in the level of biomass and an 8.5-fold increase in alpha-amylase yield was achieved.

Production and properties of polygalacturonate lyase by an alkalophilic microorganism Bacillus sp. RK9.

Bacillus sp. RK9 was isolated from soil and produced a constitutive polygalacturonate lyase. Production of the enzyme required the presence of complex nitrogen (peptone and yeast extract).

Production and Purification of Thermostable Amylase and Protease of Thermomonospora viridis.

Maximum yields of amylase were produced by the thermophilic actinomycete Thermomonospora viridis in a modified Simpson and McCoy medium containing 1.5% corn starch and 0.5% mycological peptone with an initial pH 7.

Polygalacturonate lyase production by Bacillus subtilis and Flavobacterium pectinovorum.

Nutritional factors relating to the production of polygalacturonate lyases by strains of Bacillus subtilis and Flavobacterium pectinovorum were examined. Studies were carried out in shake flask cultures. In the case of B.