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Literature summary for 3.2.1.1 extracted from

  • Shukla, R.J.; Singh, S.P.
    Structural and catalytic properties of immobilized alpha-amylase from Laceyella sacchari TSI-2 (2016), Int. J. Biol. Macromol., 85, 208-216 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Triton X 100 the immobilized enzyme shows improved catalysis in presence of Triton X-100 Laceyella sacchari
Tween 20 the immobilized enzyme shows improved catalysis in presence of Tween 20 Laceyella sacchari

Application

Application Comment Organism
industry possible applications of the immobilized alpha-amylase in the starch processing industry Laceyella sacchari

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the alpha-amylase from Laceyella sacchari TSI-2 via entrapment, ionic binding and surface adsorption using 6 different matrices (Agar Agar, hydroxyapatite, Seralite SRA and SRC, silica + glutaraldehyde, and DEAE cellulose + glutaraldehyde), method evaluation, overview. The DEAE anion exchange cellulose with glutaraldehyde crosslinking method appears most effective for the immobilization with high operational stability. While the temperature optima and thermal stability of the immobilized alpha-amylase shift from 60°C to 70°C with increased half-life, the pH optimum remains unaltered while pH stability is shifted from pH 6.0 to pH 7.0. The stability of the immobilized enzyme improves in solvents. The enzyme catalysis in surfactants enhances, while the Km and Vmax are reduced after immobilization. Role of aliphatic amines, esters and alkenes in immobilization, structure analysis. Starch hydrolysis efficiency of the immobilized enzyme is 15.55% Laceyella sacchari

Inhibitors

Inhibitors Comment Organism Structure
Tween 80 adversely affects alpha-amylase in the immobilized state as compared to the free enzyme Laceyella sacchari

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Lineweaver-Burke double reciprocal plot Laceyella sacchari

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Laceyella sacchari
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + H2O Laceyella sacchari
-
?
-
?
starch + H2O Laceyella sacchari TSI-2
-
?
-
?

Organism

Organism UniProt Comment Textmining
Laceyella sacchari A0A2I7SX03 i.e. Thermoactinomyces thalpophilus
-
Laceyella sacchari TSI-2 A0A2I7SX03 i.e. Thermoactinomyces thalpophilus
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information bacterial strain TSI-2 is Gram-positive, with long and branching, filamentous hyphae. It grows optimally in the range of 45-60°C and pH 6-8, and it secretes alpha-amylase optimally at 50°C, pH 7.0, and 2 days of incubation time Laceyella sacchari
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O
-
Laceyella sacchari ?
-
?
starch + H2O 0.1-2.0% starch solution Laceyella sacchari ?
-
?
starch + H2O
-
Laceyella sacchari TSI-2 ?
-
?
starch + H2O 0.1-2.0% starch solution Laceyella sacchari TSI-2 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Laceyella sacchari

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
half-life of free enzyme is 23 h, of immobilized enzyme 28 h Laceyella sacchari
60
-
half-life of free enzyme is 27 h, of immobilized enzyme 31 h Laceyella sacchari
70
-
half-life of free enzyme is 24 h, of immobilized enzyme 38 h Laceyella sacchari
80
-
half-life of free enzyme is 20 h, of immobilized enzyme 24 h Laceyella sacchari

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Laceyella sacchari

pH Range

pH Minimum pH Maximum Comment Organism
5 9 over 80% of maximal activity within this range for free and immobilized enzyme Laceyella sacchari

pH Stability

pH Stability pH Stability Maximum Comment Organism
6
-
the free enzyme shows maximum stability at pH 6.0 with the residual activity at 68% after 12 h, while the immobilized enzyme at pH 7.0 retaining 80% of activity after 12 h. Overall, a 10% enhancement in the residual activities is evident for the immobilized alpha-amylase compared to the free enzyme Laceyella sacchari