Bacillus sp. KCA102 capable of producing thermostable amylase in a short fermentation time (∼18-20 h) has been isolated from a soil sample. The performance of amylase during hydrolysis of starch has been studied using response surface methodology. The parameters under study have been categorized into two, viz., physical parameters (pH, temperature and time) and chemical parameters (amounts of substrate and enzyme). The optimal conditions of pH, temperature and time at which maximum amount of glucose formed were found to be 7.1, 57.5°C and 25 min, respectively. The optimal amounts of substrate and enzyme for maximum hydrolysis were found to be 0.5% starch and 94 mU/ml of amylase, respectively. © 2004 Elsevier Ltd. All rights reserved.

Chandraraj Raj Krishnan

Department Of Biotechnology

Sathyanarayana Naidu Gummadi

Enzymes

Fermentation

glucose

Hydrolysis

pH effects

Soils

Statistical methods

Surface chemistry

amylase

Response surface methodology

Starch

BACILLUS SP.

IIT Madras is a public technical and research university located in Chennai, Tamil Nadu. Founded in 1959, it is recognised as an Institute of National Importance.

IIT Madras has been ranked as the top engineering institute in India for four years in a row by the National Institutional Ranking Framework of the MHRD

It currently offers undergraduate, postgraduate and research degrees across 16 disciplines in Engineering, Sciences, Humanities and Management. About 596 faculty belonging to science and engineering departments and centres of the Institute are engaged in teaching, research and industrial consultancy.

IIT Madras

Process Biochemistry

Debaryomyces nepalensis was previously isolated, which is capable of producing pectin lyase and pectate lyase using pectin as sole source of carbon. The parameters affecting the activity of these enzymes are categorized into two, viz., chemical (amount of substrate and enzyme) and physical (pH of reaction mixture and temperature of incubation). The effect of these parameters on pectin lyase and pectate lyase was studied using central composite design. The optimal conditions of amount of substrate and enzyme (culture broth) were found to be 545 μl (∼1 g/l pectin) and 123 μl for pectin lyase and 707 μl (∼1.1 g/l polygalacturonic acid) and 96 μl for pectate lyase. The optimum pH and temperature for reaction was found to be 6.4 and 35 °C for pectin lyase and 7.5 and 32 °C for pectate lyase. After optimization, the activity of pectin lyase and pectate lyase was increased by 1.3- and 1.4-fold, respectively. © 2006 Elsevier B.V. All rights reserved.

Biochemical Engineering Journal

Optimization of chemical and physical parameters affecting the activity of pectin lyase and pectate lyase from Debaryomyces nepalensis: A statistical approach

The objective of the present study was to isolate halotolerant bacteria from the sediment sample collected from Marakanam Solar Salterns, Tamil Nadu, India using NaCl supplemented media and screened for amylase production. Among the 22 isolates recovered, two strains that had immense potential were selected for amylase production and designated as P1 and P2. The phylogenetic analysis revealed that P1 and P2 have highest homology with Pontibacillus chungwhensis (99%) and Bacillus barbaricus (100%). Their amylase activity was optimized to obtain high yield under various temperature, pH and NaCl concentration. P1 and P2 strain showed respective, amylase activity maximum at 35 °C and 40 °C; pH 7.0 and 8.0; 1.5 M and 1.0 M NaCl concentration. Further under optimized conditions, the amylase activity of P1 strain (49.6 U mL-1) was higher than P2 strain. Therefore, the amylase enzyme isolated from P. chungwhensis P1 was immobilized in sodium alginate beads. Compared to the free enzyme form (49.6 U mL-1), the immobilized enzyme showed higher amylase activity as 90.3 U mL-1. The enzyme was further purified partially and the molecular mass was determined as 40 kDa by SDS-PAGE. Thus, high activity of amylase even under increased NaCl concentration would render immense benefits in food processing industries. © 2012 .

Fulltext

Journal of Genetic Engineering and Biotechnology

Optimization and immobilization of amylase obtained from halotolerant bacteria isolated from solar salterns

The reaction conditions were optimized for enzymatic hydrolysis of pectic substances using pectolytic enzymes produced by Aspergillus niger NCIM 548. Response surface methodology was used to optimize the reaction parameters and the central composite design was employed for this purpose. Pectin was used as the substrate for polymethylgalacturonase and pectinlyase, whereas polygalacturonic acid was the substrate for polygalacturonase. The volume ratio of reactants for maximum hydrolysis was determined under the assay conditions. The optimum amount of substrate and enzyme were found to be 0.2 cm3 and 0.074 cm3 for polymethylgalacturonase, 0.4 cm3 and 0.086 cm3 for polygalacturonase, and 0.63 cm3 and 0.7 cm3 for pectinlyase. The pH and temperature optima were found to be 5.3 and 30°C for polymethylgalacturonase, 6.6 and 26°C for polygalacturonase, and 4.8 and 35°C for pectinlyase. Under optimized conditions the enzyme activities were higher when compared to unoptimized conditions. Copyright (C) 1999 Elsevier Science Inc.The reaction conditions were optimized for enzymatic hydrolysis of pectic substances using pectolytic enzymes produced by Aspergillus niger NCIM 548. Response surface methodology was used to optimize the reaction parameters and the central composite design was employed for this purpose. Pectin was used as the substrate for polymethylgalacturonase and pectinlyase, whereas polygalacturonic acid was the substrate for polygalacturonase. The volume ratio of reactants for maximum hydrolysis was determined under the assay conditions. The optimum amount of substrate and enzyme were found to be 0.2 cm3 and 0.074 cm3 for polymethylgalacturonase, 0.4 cm3 and 0.086 cm3 for polygalacturonase, and 0.63 cm3 and 0.7 cm3 for pectinlyase. The pH and temperature optima were found to be 5.3 and 30°C for polymethylgalacturonase, 6.6 and 26°C for polygalacturonase, and 4.8 and 35°C for pectinlyase. Under optimized conditions the enzyme activities were higher when compared to unoptimized conditions.

Enzyme and Microbial Technology

Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: A statistical approach

Hydrolysis of starches by the action of an α-amylase from Bacillus subtilis

Journal of Molecular Structure: THEOCHEM

α-Amylases of medical and industrial importance

A solid state fermentation based bacterial α-amylase and fungal glucoamylase system and its suitability for the hydrolysis of wheat starch

Microbial α-amylases: a biotechnological perspective

Hydrolysis of starch by amylase from Bacillus sp. KCA102: A statistical approach

Journal	Process Biochemistry
ISSN	13595113
Open Access	No