Thermostable amylases from hyper‐thermal springs of Ethiopia

Haki, Gulelat Desse; Rakshit, SK

doi:10.1002/ts.135

Cited by 5 publications

(9 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Performing enzymatic reactions at high temperatures allows higher reaction rates and process yields because of: (i) a decrease in viscosity, (ii) an increase in the diffusion coefficient of substrates, (iii) an increase in the solubility of substrates and products, and (iv) a favourable equilibrium displacement in endothermal reactions [37]. Moreover, the risk of contamination by common mesophiles decreases with increases in the reaction temperature.…”

Section: Advantages Of Working With Thermostable Enzymesmentioning

confidence: 99%

“…The enzymatic starch conversion process involves three steps: (i) gelatinization: the dissolution of starch granules, forming a viscous suspension; this step is achieved by heating starch with water at high temperatures; the use of a thermostable enzyme would save a lot of cooling time, this allowing to proceed directly with the hydrolysis after gelatinization; (ii) liquefaction: partial hydrolysis of starch, with a loss of viscosity and, (iii) saccharification: the production of glucose and maltose via further hydrolysis [37].…”

Section: Starch Degradationmentioning

confidence: 99%

“…They are rapidly becoming the most important industrial enzymes, constituting more than 65% of the world market [59], and this biotechnological interest has further driven the search for thermostable proteases able to withstand the harsh conditions of industrial processes [37,60]. They are rapidly becoming the most important industrial enzymes, constituting more than 65% of the world market [59], and this biotechnological interest has further driven the search for thermostable proteases able to withstand the harsh conditions of industrial processes [37,60].…”

Section: Proteasesmentioning

confidence: 99%

See 2 more Smart Citations

Industrial Applications of Hyperthermophilic Enzymes: A Review

Miguel

Barros‐Velázquez²,

Villa

2006

PPL

View full text Add to dashboard Cite

Over the past two decades, research scientists have been involved in the investigation of thermophilic and hyperthermophilic microorganisms owing to the unique features of their enzymic systems. Such in-depth investigations are now on their way to mastering the cloning and industrial exploitation of a broad variety of genes encoding enzymes involved in starch hydrolysis, amino acid biosynthesis, protein hydrolysis, etc. In this work, we review the state of the art and future perspectives of industrial applications of enzymes from hyperthermophilic and extreme thermophilic microorganisms, special attention being paid to the biotechnological methods involved in their industrial exploitation.

show abstract

Section: Advantages Of Working With Thermostable Enzymesmentioning

confidence: 99%

Section: Starch Degradationmentioning

confidence: 99%

Section: Proteasesmentioning

confidence: 99%

See 1 more Smart Citation

Industrial Applications of Hyperthermophilic Enzymes: A Review

Miguel

Barros‐Velázquez²,

Villa

2006

PPL

View full text Add to dashboard Cite

show abstract

“…Similar values were reported for amylase production by other B. stearothermophilus strain (Wind et al, 1994). The optimum temperature for the α-amylase activity (partially purifi ed) produced by B. stearothermophilus GRE 1 is 60˚C (Haki and Rakshit, 2003b). absorption was measured at 580 nm after which reducing sugar was estimated.…”

Section: Optimization Of Fermentation Temperaturementioning

confidence: 86%

Optimum Production and Characterization of Thermostable Amylolytic Enzymes from B. stearothermophilus GRE1

2006

View full text Add to dashboard Cite

Optimum production of extracellular, thermostable amylolytic enzymes (α and β‐amylase) by a newly isolated bacterium, Bacillus stearothermophilus, was investigated in a batch bioreactor. Starch and lactose at 1.0% and 3.0% (w/v) respectively were found to be optimum for maximum enzyme production. Optimization of cultural conditions (pH 7.0 and temperature 45°C) resulted in high bacterial specific growth rate (0.64 h−1), yielding 2.20 gL−1 biomass, 11.43 UmL−1 α‐amylase and 10.04 UmL−1 of β‐amylase. Hydrolysis of native starches from wheat, cassava, corn and potato at 60°C using the crude enzyme showed 60‐80% saccharification with potato starch showing the least and wheat starch showing the greatest hydrolysis. The Km and Vmax values of the crude α‐amylase for starch were 4.78 mg starch/mL and 6.67 mg/mL.min respectively.

show abstract

“…Thermostable enzymes are widely used in basic molecular biology and for the various industrial applications . The microbial diversity is one of the major rich sources for the production of enzymes either by cultivation of the wild‐type strain or by genetically engineering the strain for the expression of enzyme .…”

Section: Introductionmentioning

confidence: 99%

Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

Kumar

Rather

Gurramkonda

et al. 2015

Biotech and App Biochem

View full text Add to dashboard Cite

The uses of thermostable starch hydrolytic biocatalysts are steadily increasing for the industrial application because of their obvious need for biocatalytic performance at elevated temperatures. The starch liquefaction and saccharification can be carried out simultaneously by the use of thermostable starch hydrolytic biocatalysts, thus minimizing the unit operations, time, and efforts. The cost factor hampers the industrialization of expensive soluble (free) enzymes for biocatalytic applications and the immobilization of enzymes offers promising alternative to the hurdle. The present investigation was aimed for immobilization of thermostable α-amylase using calcium alginate, and statistical optimization studies were carried out for enhanced biocatalytic performance. Initially, one-parameter at a time optimization studies were carried out for identification of significant factors influencing the immobilization. Furthermore, a statistical approach, response surface methodology, was applied for immobilization of α-amylase. The immobilized α-amylase in alginate microbeads showed enhanced stability to temperature and reusable property for up to seven cycles (with the retention of 50% initial activity). Finally, the kinetic behavior of free and immobilized enzyme showed the Km value of 1.2% and 2.6% (w/v) and Vmax of 1,020 and 1,030 U, respectively. Fifty percent reduction in affinity of the immobilized enzyme toward substrate was compensated by its longer stability.

show abstract

Thermostable amylases from hyper‐thermal springs of Ethiopia

Cited by 5 publications

References 5 publications

Industrial Applications of Hyperthermophilic Enzymes: A Review

Industrial Applications of Hyperthermophilic Enzymes: A Review

Optimum Production and Characterization of Thermostable Amylolytic Enzymes from B. stearothermophilus GRE1

Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

Contact Info

Product

Resources

About