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PubMed2002

Properties and applications of starch-converting enzymes of the alpha-amylase family.

Starch is a major storage product of many economically important crops such as wheat, rice, maize, tapioca, and potato. A large-scale starch processing industry has emerged in the last century. In the past decades, we have seen a shift from the acid hydrolysis of starch to the use of starch-converting enzymes in the production of maltodextrin, modified starches, or glucose and fructose syrups. Currently, these enzymes comprise about 30% of the world's enzyme production. Besides the use in starch hydrolysis, starch-converting enzymes are also used in a number of other industrial applications, such as laundry and porcelain detergents or as anti-staling agents in baking. A number of these starch-converting enzymes belong to a single family: the alpha-amylase family or family13 glycosyl hydrolases. This group of enzymes share a number of common characteristics such as a (beta/alpha)(8) barrel structure, the hydrolysis or formation of glycosidic bonds in the alpha conformation, and a number of conserved amino acid residues in the active site. As many as 21 different reaction and product specificities are found in this family. Currently, 25 three-dimensional (3D) structures of a few members of the alpha-amylase family have been determined using protein crystallization and X-ray crystallography. These data in combination with site-directed mutagenesis studies have helped to better understand the interactions between the substrate or product molecule and the different amino acids found in and around the active site. This review illustrates the reaction and product diversity found within the alpha-amylase family, the mechanistic principles deduced from structure-function relationship structures, and the use of the enzymes of this family in industrial applications.

Amino Acid Sequence↗
PubMedDate not supplied

[Substrate specificity and action mechanism of glycosidases].

Result of author's research and data from literature have been generalized with respect to hydrolase and transferase activity of glycosidases: alpha-galactosidase and alpha-N-acetylgalactosaminidase--the enzymes which catalyse hydrolysis of natural and synthetic glycosides. Broad variability of action specificity of glycosidases with respect to glycon, aglycon as well as the bond type depending on the enzyme isolation source have been shown. One can suppose that the enzyme action specificity is connected with different formation mechanisms of enzyme-substrate complexes. An idea is discussed concerning the identity of the mechanism of splitting of various glycosidic links by the studied enzymes.

Catalysis↗
PubMed1980

Acid hydrolases in serum from patients with lysosomal disorders.

The activity of acid hydrolases was studied in serum from patients with mucolipidosis (II and III) and other lysosomal disorders. In mucolipidosis II and III all hydrolases examined except alpha-glucosidase, beta-glucosidase and acid phosphatase were greatly increased. High values for beta-galactosidase were seen in mucopolysaccharidosis types I and II, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. N-Acetyl-beta-glucosaminidase activity was high in mucopolysaccharidosis types I, II, III and Gaucher's disease. The activity of beta-glucuronidase was increased in mucopolysaccharidosis types I, II and III, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. Acid phosphatase had increased activity only in Gaucher's disease. In several lysosomal storage disorders no increased values could be found. It is suggested that high values in serum from patients with lysosomal storage disorders (not including mucolipidosis II and III) may depend upon liver cell damage, which disturbs the clearing of acid hydrolases from serum.

Acid Phosphatase↗
PubMed1994

Purification and characterization of an aminopeptidase from tuna (Thunnus albacares) pyloric caeca.

An aminopeptidase was purified from a water soluble fraction of tuna pyloric caeca by heat treatment, Zn2+ fractionation, ion exchange on a DEAE cellulose column, gel filtration on Fractogel TSK-55, and immobilized metal ion affinity chromatography (IMAC) on IDA(Cu2+/Zn2+)-Sepharose 6B. The molecular mass of the enzyme was estimated to be 150,000 on Sephacryl S-300 HR, and was found to be near 72,000 by SDS-PAGE. The aminopeptidase, which is a glycoprotein rich in acidic amino acids, is optimally active at pH 8.8 and 65 degrees C. The enzyme activity was not affected by Mg2+, Zn2+, Ca2+, Mn2+, Co2+, PMSF, iPr2FP, 4-hydroxymercuribenzoic acid, iodoacetamide, puromycin, and cysteine but it was strongly inhibited by metal chelators (EDTA and o-phenanthroline), amastatin, Hg2+, Cd2+, and Cu2+. The enzyme was also inhibited by some L-amino acids. Kinetic parameters of the enzyme were determined with some aminoacyl-p-nitroanilides and aminoacyl-beta-naphthylamides. L-Alanine-p-nitroanilide and L-alanine-beta-naphthylamide were hydrolysed most rapidly while the highest hydrolytic coefficient (kcat/Km) value was obtained with L-methionine-p-nitroanilide. The apoaminopeptidase was prepared and reconstitution of an active enzyme was carried out using metal chelating interaction chromatography on an IDA-Sepharose 6B column charged with a metal ion. Full activity was restored with Zn2+, Co2+, Cu2+ and Al3+. Zn(2+)-Enzyme was the most thermostable form of the aminopeptidase. Reversal inhibition by Cu2+ and Cd2+ was also examined. When the aminopeptidase was partially deglycosylated by a treatment with N-glycosidase F some of its physical properties differed from that of the native enzyme: its electrophoretic mobility was reduced and its stability to denaturation by SDS and by ionic strength were lower than those of the untreated enzyme. All together, our results indicate that the tuna pyloric caeca aminopeptidase is distinct from the peptide hydrolases characterized in the literature.

Amino Acids↗
PubMed1995

Nucleotide sequences of xylan-inducible xylanase and xylosidase/arabinosidase genes from Bacteroides ovatus V975.

The nucleotide sequences of the xylI and xsa genes of Bacteroides ovatus V975, encoding xylanase and xylosidase activities, were determined. Both genes are part of a xylan-inducible operon, the sequenced region of which also contains a partial open reading frame upstream of the xylanase gene. Deduced amino acid sequence similarly analyses indicate that the xylanase belongs to the Family F series of glycosyl hydrolases.

Amino Acid Sequence↗
PubMed2002

Evidence that the putative alpha-glucosidase of Thermotoga maritima MSB8 is a pNP alpha-D-glucuronopyranoside hydrolyzing alpha-glucuronidase.

The gene (agu) encoding p-nitrophenyl alpha-D-glucuronopyranoside (pNP-GUA) hydrolyzing alpha-glucuronidase of the hyperthermophilic bacterium Thermotoga maritima was cloned and expressed in Escherichia coli. The recombinant enzyme was purified and characterized. The gene previously designated as putative alpha-glucosidase was found to code for a protein that had no alpha-glucosidase activity. It showed a rare activity profile with its ability to hydrolyze pNP-GUA, an activity not known in the alpha-glucuronidases from microbial sources. This is the first report on the occurrence of an alpha-glucuronidase which belongs to the family 4 of glycosyl hydrolases.

Dithiothreitol↗
PubMedDate not supplied

Oligogalacturonate hydrolase from carrot roots.

The presence of multiple forms of enzyme with terminal action pattern on pectate was evaluated in the protein mixture obtained from carrot roots. The form with pH optimum 3.8 clearly preferred substrates with a lower degree of polymerization (oligogalacturonates). Its molecular mass, isoelectric point, glycosylation as well as cleavage of pectate from nonreducing end corresponded to an exopolygalacturonase [EC 3.2.2.67]. The affinity of this enzyme to the substrates increased with the increasing degree of polymerization, and the difference was observed only in the maximal ratio of catalysis of oligomeric and polymeric substrates. Sterical hindrance for substrates with more than six D-galactopyranuronic acid units is supposed and an oligogalacturonate hydrolase rather than exopolygalacturonase is considered.

Daucus carota↗