Production of Thermostable α-amylases by Solid State Fermentation-A Review

Regulapati, Rahul; Malav, N Prem; Gummadi, N Sathyanarayana

doi:10.3923/ajft.2007.1.11

Cited by 22 publications

(5 citation statements)

References 58 publications

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“…Those enzymes belong to the family Glycosyl Hydrolase (GH) 13, the major glycoside hydrolase family acting on substrates containing α-glucoside linkages . Such a type of enzyme catalyzes the hydrolysis of internal 1,4-α- d -glycosidic linkages between adjacent glucose units in the linear amylose chain of starch and related polysaccharide polymers leading to the formation of linear and branched oligosaccharides . Moreover, α-amylases are one of the most widely used with approximately 25–33% of the world market enzymes, applied in various areas such as biotechnology, pharmacology, analytical chemistry, food, and textile industry. , …”

Section: Introductionmentioning

confidence: 99%

“…2 Such a type of enzyme catalyzes the hydrolysis of internal 1,4-α-D-glycosidic linkages between adjacent glucose units in the linear amylose chain of starch and related polysaccharide polymers leading to the formation of linear and branched oligosaccharides. 3 Moreover, α-amylases are one of the most widely used with approximately 25−33% of the world market enzymes, applied in various areas such as biotechnology, pharmacology, analytical chemistry, food, and textile industry. 4,5 However, the more widespread industrial and pharmacological applications of these enzymes are hampered by the general lack of low-cost technology to overcome the restricted conditions of free enzyme applications.…”

Section: Introductionmentioning

confidence: 99%

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Starch Biocatalyst Based on α-Amylase-Mg/Al-Layered Double Hydroxide Nanohybrids

Bruna

Pereira

Polizeli

et al. 2015

ACS Appl. Mater. Interfaces

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The design of new biocatalysts through the immobilization of enzymes, improving their stability and reuse, plays a major role in the development of sustainable methodologies toward the so-called green chemistry. In this work, α-amylase (AAM) biocatalyst based on Mg3Al-layered double-hydroxide (LDH) matrix was successfully developed with the adsorption method. The adsorption process was studied and optimized as a function of time and enzyme concentration. The biocatalyst was characterized, and the mechanism of interaction between AAM and LDH, as well as the immobilization effects on the catalytic activity, was elucidated. The adsorption process was fast and irreversible, thus yielding a stable biohybrid material. The immobilized AAM partially retained its enzymatic activity, and the biocatalyst rapidly hydrolyzed starch in an aqueous solution with enhanced efficiency at intermediate loading values of ca. 50 mg/g of AAM/LDH. Multiple attachments through electrostatic interactions affected the conformation of the immobilized enzyme on the LDH surface. The biocatalyst was successfully stored in its dry form, retaining 100% of its catalytic activity. The results reveal the potential usefulness of a LDH compound as a support of α-amylase for the hydrolysis of starch that may be applied in industrial and pharmaceutical processes as a simple, environmentally friendly, and low-cost biocatalyst.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Starch Biocatalyst Based on α-Amylase-Mg/Al-Layered Double Hydroxide Nanohybrids

Bruna

Pereira

Polizeli

et al. 2015

ACS Appl. Mater. Interfaces

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“…It is well known that complex lignocellulosic wastes are supposed to be the best substrates for the SSF processes [45,46]. Fungi are used in the production of α-amylases under submerged fermentation (SmF), however, the production under solid state fermentation are preferred because of the higher yield, low capital investment, better product recovery and several characteristic advantages it offers [47,48]. In the present investigation, the effect of different substrate concentrations (WHGP) used as a sole carbon source in fermentation medium on amylase(s) productivity by A. lavus, F7 was studied.…”

Section: Resultsmentioning

confidence: 99%

Production of α-amylase(s) by Aspergillus flavus, F7 attacking water hyacinth ground preparation (WHGP) under solid state fermentation

El-Tabakh

Elsoud

Salem

et al. 2020

jibps

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Some environmental and nutritional parameters controlling the biosynthesis of α-amylase from Aspergillus flavus, F7 attacking the water hyacinth have been investigated under solid state fermentation conditions for maximum amylase production. The following optima’s were recorded for the highest α-amylase yield; Incubation period 7 days; temperature, 30oC; pH, 5; inoculum size, 3X108 spores/ml; flask volume 100 ml capacity; hyacinth fresh weight 5 g; tap water, 25 ml. Under these conditions, starch showed remarkable stimulatory effect; nitrogen sources and amino acids have no stimulatory effect. Pyridoxal hydrochloride, B6 at a concentration of 200 ppm exhibited a stimulatory effect on biosynthesis of α-amylase.

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“…These sources were added to the production medium at a concentration of 0.3 %. Results indicated in Figure (5) showed that K2HPO4 was the optimum for isoamylase production, enzyme specific activity was 0.673 U/mg, this may be due to the effect of such concentration of phosphate source on buffering capacity that maintain the pH of the production medium which means more molecules of the buffer components present larger number of H+ and OHˉ ions can be absorbed without changing the pH value [23]. Another study referred that 0.38% KH2PO4 was the optimum for isoamylase production by P. amylodermosa [24].…”

Section: Effect Of Type Of Phosphate Sourcementioning

confidence: 93%

Optimum conditions for isoamylase production by Pseudomonas sp.

Jasim¹,

Abdul-Wahab²

2013

JoBRC

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Different nutritional and cultural factors were studied to determine the optimum conditions for isoamylase production by Pseudomonas sp. in a batch culture of the production medium. These factors include carbon, nitrogen and phosphate sources and their concentrations, temperature and pH. Results showed that the optimum conditions for isoamylase production by Pseudomonas sp. were achieved when the production medium was supplemented with maltose 1%, peptone 0.4%, and K2HPO4 0.4% as a carbon, nitrogen, and phosphate sources respectively, at initial medium pH 6, and incubation at 28°C for 24 hours. Under these conditions isoamylase productivity reaches the maximum, at which enzyme specific activity was 0.85 U/mg proteins.

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Production of Thermostable α-amylases by Solid State Fermentation-A Review

Cited by 22 publications

References 58 publications

Starch Biocatalyst Based on α-Amylase-Mg/Al-Layered Double Hydroxide Nanohybrids

Starch Biocatalyst Based on α-Amylase-Mg/Al-Layered Double Hydroxide Nanohybrids

Production of α-amylase(s) by Aspergillus flavus, F7 attacking water hyacinth ground preparation (WHGP) under solid state fermentation

Optimum conditions for isoamylase production by Pseudomonas sp.

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