Α-amylase Production Research Articles

Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2

Abstract A psychrophilic and halophilic bacterial isolate, Shewanella sp. ISTPL2, procured from the pristine Pangong Lake, Ladakh, Jammu and Kashmir, India, was used for the production and characterization of the psychrophilic and alkalophilic α-amylase enzyme. The α-amylase is a critical enzyme that catalyses the hydrolysis of α-1,4-glycosidic bonds of starch molecules and is predominately utilized in biotechnological applications. The highest enzyme activity of partially purified extracellular α-amylase was 10,064.20 U/mL after 12 h of incubation in a shake flask at pH 6.9 and 10 °C. Moreover, the maximum intracellular α-amylase enzyme activity (259.62 U/mL) was also observed at 6 h of incubation. The extracellular α-amylase was refined to the homogeneity with the specific enzyme activity of 36,690.47 U/mg protein corresponding to 6.87-fold purification. The optimized pH and temperature for the α-amylase were found to be pH 8 and 4 °C, respectively, suggesting its stability at alkaline conditions and low or higher temperatures. The amylase activity was highly activated by Cu2+, Fe2+ and Ca2+, while inhibited by Cd2+, Co2+ and Na2+. As per our knowledge, the current study reports the highest activity of a psychrophilic α-amylase enzyme providing prominent biotechnological potential.

Use of deproteinised leaf juice of Medicago sativa L. for the production of α-amylase

Leaf protein concentration (LPC) is a good source of cyanocobalamine (B12), ascorbic acid (vitamin C) and folic acid (vitamin B9). After isolation of LPC from leaves the remaining by product is deproteinised leaf juice (DPJ) which is rich in water soluble carbohydrates, free amino acids, minerals, lipids and vitamins. The dry matter (DM) and nutrient composition of DPJ varies from species to species. The DM content in this fraction was found between 1.2 to 4.0%. Six fungi were grown on the DPJ expressed from Medicago sativa, Anethum graveolens, Spinacia oleracea, Trigonella foenium-graecum, Coriandrum sativum and also on conventional GN medium to evaluate the suitability of DPJ as a medium for fungal growth and subsequent production of ∝-amylase. The efficiency of DPJ as a medium for fungal growth was evaluated and its value in microbial biotechnology for the production of ∝-amylase was tested. Increase in concentrate of flour in the DPJ there was simultaneous increase in the mycelial dry weight (MDW) production of the six fungi under investigation. On DPJ alone, the yield of MDW was between 76.0 and 89.5 mg which increased to 164.5, 131.0 and 117.0 mg respectively under the influence of the flours of wheat, sorghum and maize respectively. Maximum response to the enrichment of DPJ by flour was noticed with A. niger. As with the increase in growth of fungi with increasing concentration of flour, the activity of amylase also increased. On an average it was 34 - 96 U/ml when the fungi were grown on DPJ alone, which increased to 301, 265 and 276 U/ml under the influence of flours.
 J. bio-sci. 26: 07-14, 2018

Sirtuin SirD is involved in α-amylase activity and citric acid production in Aspergillus luchuensis mut. kawachii during a solid-state fermentation process

Sirtuins are understood to play a significant role in growth phase-dependent gene expression. In the study presented here, we examined the sirtuins in the white koji fungus, Aspergillus luchuensis mut. kawachii (Aspergillus kawachii), to examine their role in the regulation of amylolytic enzymes and citric acid production during solid-state culture (koji). Characterization of rice koji made using five sirtuin gene disruptants indicated that these genes are involved in the amylolytic activity and acidity of rice koji; the sirD disruptant in particular showed lower levels of acid-stable α-amylase activity and citric acid production per mycelial weight in koji compared to the control strain. The sirD disruptant also showed a change in mycelial pigmentation, and had higher sensitivity to cell wall biogenesis inhibitors such as calcofluor white and Congo red and reduced conidia formation. These results indicate that SirD is required for secondary metabolism, cell wall integrity, and conidial development. Cap analysis gene expression (CAGE) and quantitative RT-PCR analysis indicated that transcriptional changes were related to the characteristic phenotype of the sirD disruptant, including a reduced transcript level of the acid-stable α-amylase gene and a citric acid exporter in rice koji. These results indicate that SirD has a significant role in global transcriptional regulation, including the production of acid-stable α-amylase and citric acid, in A.kawachii during the solid-state fermentation process.

Production, characterization and application of thermostable, alkaline α-amylase (AA11) from Bacillus cereus strain SP-CH11 isolated from Chilika Lake

An alkaliphile bacterial strain designated as CH11 was isolated from the sediments of Chilika Lake, Odisha. The isolate showed stupendous growth and production of α-amylase at pH 10.0. Through 16S rRNA gene based molecular technique this isolate was identified as Bacillus cereus strain SP-CH11 having GenBank Accession No. KT992791. Homogenous ~55 kDa extracellular α-amylase was extracted with 241.304, 26.26 and 3.2-fold acceleration in specific activity, purification fold and yield respectively. The alkaline α-amylase AA11 was further characterized. At pH 9.0 the purified enzyme AA11 was highly stable while retaining 88–100% functional viability at temperature range from 35 to 65 °C, confirming its thermostability nature. It showed stability with powdered and liquid detergents at 7 mg/mL and 100-fold dilutions respectively. AA11 efficiently removed the starch stain from cotton fabrics. The findings of this study indicate that the isolate CH11 is a source of novel alkaline α-amylase that has promising application in food and detergent industries.

Optimization of Aspergillus niger α-amylase Activity for Enhanced Glucose Production from Cassava Starch

The aim of this study was to optimize the hydrolytic activity of A. niger α-amylase on cassava starch. Isolation of Aspergillus niger, determination of α-amylase activity, α-amylase production and extraction were performed using standard protocols. Parameters such as pH, temperature, substrate concentration were studied using unifactorial approach. pH was varied from 3.6-5.6, temperature 30-80ºC, substrate concentration 0.3-1.5 g/l. In conclusion, for optimal utilization of α-amylase in the production of numerous products of economic significance, the outcome of this work can be relied upon to boost production of glucose and accessory products from starch.

Pola Pertumbuhan dan Produksi -Amilase Bacillus amyloliquefaciens pada Substrat Pati Jagung dengan Variasi pH Awal Media dan Waktu Inkubasi

The aims of this study were to identify the growth curve of B. amyloliquefaciens on corn-starch and non corn starch addition media, number of cells and production of a-amylase on variety initial pH during the stationary phase. The growth curve of B. amyloliquefaciens was made using the water optical density on both medium which has inoculated by microbes. The experimental design for the a-amylase production was factorial completely randomized design (6 x 3 x 3). There were two factors included in this study i.e. initial pH of the media ( 5, 5.5, 6, 6.5, 7 and 7.5) and incubation times (16, 18 and 20 hours). The results showed that B. amyloliquefaciens growth curve on medium with corn starch was slower than on medium without corn starch. Production of a-amylase and number of cells were having similar patterns in all treatments, i.e. increased until optimum pH and incubation time were reached. The number of cells and a-amylase production were optimal at pH 6.5 for 18 hours incubation whereas the number of cells (about 2.8542 x 108 cells/ml) and a-amylase production (1.4467 units/ml) were optimal at pH 6.5 for 18 hours incubation.

Application of one –factor- at-a-time and statistical designs to enhance α-amylase production by a newly isolate Bacillus subtilis strain-MK1

Abstract α-amylase is a starch hydrolyzing enzyme which has many industrial applications. In the present study, α-amylase producers were isolated from farm soil in Egypt (Sadat City). Screening was done by iodine test, based on the clear zone around the sample in starch agar plates. The most potent isolate MK1 was identified (morphologically and biochemically) and confirmed by 16S rRNA gene sequence method. This sequence was deposited to the GenBank under accession number, B. subtilis strain-MK1 (MF614924). α-Amylase production parameters were optimized using one-factor-at-a-time (OFAT) and Response Surface methodology (RSM). The result obtained from OFAT showed 72.4U/ml of amylase activity which was 1.8- fold higher as compared to unoptimized conditions (40.3 U/ml). The most significant factors were identified and its values were optimized using Plackett-Burman (PB) and Central Composite (CC) design, respectively. Among thirteen independent variables tested in PB design, beef extract, MgSO4·7H2O, K2HPO4 and incubation time were the most significant on α-amylase production and showed positive effect. Whereas MnCl2·4H2O, soluble starch and culture pH showed negative effect on α-amylase production. The model validation was clear up on comparing the statistical predicted yield (140.14 U/ml) with the actual experimental yield (145.4 U/ml) of α-amylase which was closely related. The model showed higher amylase activity of 3.6 and 7.5-fold as compared to the basal and the initial media, respectively. Optimized medium by OFAT and RSM enhanced enzyme production by 7.5-folds confirming the need to optimize the production parameters to achieve maximum yield.

Characterization of plant growth-promoting traits and antagonistic potentials of endophytic bacteria from bean plants against Pseudomonas syringae pv. phaseolicola

Pseudomonas syringae pv. phaseolicola (Psp) is a seed-borne bacterium which causes halo blight disease in common bean. This study aimed the determination of plant growth-promoting traits (such as IAA, phosphate solubilization) and antagonistic potentials (such as siderophore and ammonia productions) of endophytic plant growth-promoting bacteria (PGPB) from healthy bean plants growing in different regions against Psp in vitro conditions. A total of 131 bacteria were primarily characterized as putative PGPB and tested for antagonist activity against Psp in dual culture tests. Seventy-one bacterial isolates demonstrated antagonistic activities against Psp isolate in varying ratios. Among these 71 isolates, 30 representative bacterial isolates from the different regions/fields were selected. On the basis of morphological, physiological, biochemical characteristics and confirmation by MALDI-TOF analyses, 30 endophytic antagonist isolates were identified as belonging to 10 genera, 24 different species. According to results obtained, 10 isolates belong to Bacillus spp., 6 isolates belong to Pseudomonas spp., 4 isolates belong to Rhizobium radiobacter, 2 isolates belong to Arthrobacter spp., 2 isolates belong to Achromobacter spanius, 2 isolates belong to Serratia liquefaciens, 1 isolate belongs to Acinetobacter calcoaceticus, Exiguobacterium sp., Microbacterium hydrocarbonoxydans, and Ochrobactrum anthropi. The largest and lowest inhibition zone was produced by endophytic bacterial isolates Pseudomonas gessardii (4.85) and Bacillus licheniformis (1.35). Among the tested antagonist bacterial isolates, 10 isolates were positive for the production of α-amylase, 7 isolates positive for phosphate solubilization, 29 isolates positive for siderophore production, 11 isolates positive for protease production. All selected bacterial isolates produced IAA and ammonia in relatively varying amounts. P. gessardii produced a relatively large amount of extracellular siderophore (5.83), Exiguobacterium sp. produced a relatively large amount of extracellular protease (5.25), P. gessardii and O. anthropi produced a relatively large amount of extracellular IAA (161.39 µg/ml) and Acinetobacter calcoaceticus produced a relatively large amount of phosphatase (2.63). This is the first study reporting bean plants harbor endophytes having plant growth promoting activities with antagonistic potential against Psp.

In silico analysis of signal peptides for secretory production of a-amylase in Bacillus subtilis

α-Amylases are important commercial enzymes and have a broad application in industrial processes and medicine. Gram-positive bacteria such as Bacillus subtilis are possible host organisms for α-amylases secretory production. Secretion of α-amylases to the culture medium versus intracellular production has several advantages such as prevention of inclusion bodies accumulation, higher product stability and solubility. Signal peptides are considered as one of the most essential elements for successful secretory synthesis of the recombinant proteins. Therefore, by the selection of an efficient signal peptide, secretion of the recombinant protein can be enhanced. The goal of this investigation was the in silico evaluation of several peptides to find the most suitable leader peptides for secretory production of α-amylase in B. subtilis. In present work, 30 signal peptides were selected, and numerous online servers such as SignalP, ProtParam, SOLpro, PRED-TAT and ProtComp was used for investigation of suitable signal peptides. According to in silico predictions all other signal peptides connected to α-amylase were stable and soluble except PPBD_BACSU. PPBD_BACSU because of having D-score below cut-off could not be recognized as a suitable signal peptide for α-amylase. Computational analysis identified QOX2_BACSU may direct protein into transmembrane location and was ignored. All 28 remained were predicted as secretory signal peptides which can excrete protein out of the bacteria. The signal peptides recommended by the present study are valuable for rational designing of secretory soluble α-amylase. Although, such information can be useful for future experimental production of these mentioned secretory proteins.

Heat Stable α- and Glucoamylase Performing Deep Enzymatic Hydrolysis of Starch to Fermentable Glucose

The temperature optimum for thermophilic strains, selected α-amylase producers has been studied in the cultural liquids obtained after their submerged cultivation in the temperature range 30-45°C, at 5 °C intervals. The temperature optimum of the strains was established to be within the range 68- 72 °C, making possible to use them in bio- and enzymatic technologies to diminish the pollution of the reaction medium while conducting the fermentation process at pasteurization temperature (65 °C). Consequently, the selection of stable, operable at pasteurization and higher temperatures amylase preparation is of great importance. Proposed technology is cost-effective, ecologically safe and competitive and provides deep hydrolysis of starch to fermentable sugar at the elevated temperature (68-72 °C) in one-step, by means of only one, stable amylase preparation. Exhaustive hydrolysis process of starch solutions of different concentrations (15, 30, and 40 %) with cultural liquid and technical preparation of Aspergillus niger p8-3 enzyme was studied. In case of low concentrations exhaustive hydrolysis of starch lasts 40-60 minutes, in case of high concentrations hydrolysis takes longer time. 98,6% Yield of glucose can be reached at incubation during 12 hours with enzyme cultural liquid and 8 hours incubationwith technical preparation of the enzyme at gradual increase of temperature from 50°C to 82°C during the first 20 minutes and further decrease of temperature to 70°C. Temperature setting for high yield of glucose and high hydrolysis (pasteurizing), optimal for activity of these strains is the prerequisite to be able to carry out hydrolysis of starch to glucose in one step, and, consequently, using one strain, what will be economically justified.

A STATISTICAL STRATEGY FOR THE PRODUCTION OF CELLULASE, XYLANASE AND -AMYLASE BY CLADOSPORIUM CLADOSPORIOIDES.

Agro wastes such as carrot peels are economical abundantly and naturally available easily. The present study was aimed for the production of cellulase, xylanase and a-amylase simultaneously using carrot peels. Cladosporium cladosporioides was isolated from soil. It was observed that the fungi displayed high production of cellulase, xylanase and a-amylase using economical substrate such as carrot peel. Cellulase increased up to 1.74U/mL with an approximate of 2.8 fold improvement over the previous production of 0.62 U/mL and xylanase increased up to 19.2 U/mL with an approximate of 2.2 fold over the previous production of 8.43 U/mL. The optimization of media led to 2.5 fold increased in a-amylase activity up to 0.639U/mL over the previous production 0.24 U/mL.

Purification and characterization of α-amylase from Paenibacillus sp. D9 and Escherichia coli recombinants

The aim of this study was to purify and characterize α-amylase of Paenibacillus species D9 and cloned α-amylase in Escherichia coli transformants. Optimal growth and production of D9 α-amylase were obtained after the 24-h incubation period, at pH 7, 30 °C and 200 rpm, using starch as the sole carbon source. Sodium nitrate stimulated α-amylase production by 3 folds while urea had an inhibitory effect comparing with yeast extract as the control. Characterization results of the crude and purified enzyme were similar. Purified D9 α-amylase possessed 97% residual activity after incubation at 30 °C for 120 min while 50% at 45 °C and 27% at 60 °C, respectively, under the same condition. The presence of Ca2+ ions enhanced the activity, while EDTA and Fe3+ had an inhibitory effect. Kinetic parameters were obtained having values of 37.3 mM, 19.8 U/mg and 4.84 s−1 for Km, Vmax and kcat, respectively. The α-amylase gene (amyS) of Paenibacillus sp. D9 was amplified using polymerase chain reaction (1482 bp), cloned into PSF-OXB20 vector and expressed in E. coli BL21 DE3 (pLysS) after transformation. The α-amylase purified from the transformant using a Hispur Cobalt column possessed 1.4 folds (450.8 U/mg) higher specific activity than the purified α-amylase from the wild type. Cloned α-amylase was more thermostable at 45 °C and at 60 °C, but less pH stable at pH 5 and 6. All other biochemical properties of the native and recombinant α-amylase show no significant differences. In conclusion, α-amylase of Paenibacillus sp. D9 was purified, cloned and characterized. The potential biotechnological application(s) of α-amylase may be explored.

Characterization and phylogenetic analysis of alkaline α-amylase producing Brevibacillus laterosporus from mountain climatic zone of India

α-amylases (EC3.2.1.1) are glycoside hydrolases that breakdown complex starch and maltodextrins into glucose and maltose by acting upon 1,4-glycosidiclinkages. Several amylases have been isolated and purified from members of Bacillus community, which find extensive application in starch processing, textile and pharmaceutical industry. Keeping this in mind we isolated α-amylase producing gram positive bacterium from soils collected from mountain climatic zone of India and identified it as Brevibacillus laterosporus. We further studied the effect of temperature and pH on the amylase activity of this strain and found a very stable activity at alkaline pH of 10 and temperature of 45 ºC. To our knowledge this a first report on characterization and evolutionary analysis of alkaline α-amylase producing Brevibacillus laterosporus isolated from unexplored sites of mountain climatic zone of India.
 Keywords: Climatic zone, Brevibacillus, Amylase, 16S rRNA gene sequencing, Phylogenetic analysis

A Potential Role for α-Amylase in Amyloid-β-Induced Astrocytic Glycogenolysis and Activation.

Astrocytes produce and store the energy reserve glycogen. However, abnormal large glycogen units accumulate if the production or degradation of glycogen is disturbed, a finding often seen in patients with Alzheimer's disease (AD). We have shown increased activity of glycogen degrading α-amylase in AD patients and α-amylase positive glial cells adjacent to AD characteristic amyloid-β (Aβ) plaques. Investigate the role of α-amylase in astrocytic glycogenolysis in presence of Aβ. Presence of α-amylase and large glycogen units in postmortem entorhinal cortex from AD patients and non-demented controls were analyzed by immunohistological stainings. Impact of different Aβ42 aggregation forms on enzymatic activity (α-amylase, pyruvate kinase, and lactate dehydrogenase), lactate secretion, and accumulation of large glycogen units in cultured astrocytes were analyzed by activity assays, ELISA, and immunocytochemistry, respectively. AD patients showed increased number of α-amylase positive glial cells. The glial cells co-expressed the astrocytic marker glial fibrillary acidic protein, displayed hypertrophic features, and increased amount of large glycogen units. We further found increased load of large glycogen units, α-amylase immunoreactivity and α-amylase activity in cultured astrocytes stimulated with fibril Aβ42, with increased pyruvate kinase activity, but unaltered lactate release as downstream events. The fibril Aβ42-induced α-amylase activity was attenuated by β-adrenergic receptor antagonist propranolol. We hypothesize that astrocytes respond to fibril Aβ42 in Aβ plaques by increasing their α-amylase production to either liberate energy or regulate functions needed in reactive processes. These findings indicate α-amylase as an important actor involved in AD associated neuroinflammation.

Evolutionary Trends in Industrial Production of α-amylase.

Amylase catalyzes the breakdown of long-chain carbohydrates to yield maltotriose, maltose, glucose and dextrin as end products. It is present in mammalian saliva and helps in digestion. Their applications in biotechnology include starch processing, biofuel, food, paper, textile and detergent industries, bioremediation of environmental pollutants and in clinical and medical applications. The commercial microbial strains for production of α-amylase are Bacillus subtilis, B. licheniformis, B. amyloliquefaciens and Aspergillus oryzae. Industrial production of enzymes requires high productivity and cannot use wild-type strains for enzyme production. The yield of enzyme from bacteria can be increased by varying the physiological and genetic properties of strains. The genetic properties of a bacterium can be improved by enhancing the expression levels of the gene and secretion of the enzyme outside the cells, thereby improving the productivity by preventing degradation of enzymes. Overall, the strain for specific productivity should have the maximum ability for synthesis and secretion of an enzyme of interest. Genetic manipulation of α-amylase can also be used for the production of enzymes with different properties, for example, by recombinant DNA technology. This review summarizes different techniques in the production of recombinant α- amylases along with the patents in this arena. The washing out of enzymes in reactions became a limitation in utilization of these enzymes in industries and hence immobilization of these enzymes becomes important. This paper also discusses the immobilization techniques for used α-amylases.

Evaluation of brewer's spent grain hydrolysate as a substrate for production of thermostable α-amylase by Bacillus stearothermophilus

In the present study, BSG was hydrolysed using cellulolytic enzymes and used as a growth medium supplement for cultivation of the thermophilic bacterium, Bacillus stearothermophilus in the production of α-amylase. A central composite design involving five parameters and four levels viz. starch, peptone, KCl, and MgSO4 along with BSG hydrolysate was used to derive the optimal media composition. The fermentation was conducted using shake flasks for 36 h at a temperature of 50 °C and pH 7.0 at 220 rpm. Optimization trials revealed that maximal amylase production (198.09 U/ml) occurred with a medium composition of starch (0.2% w/v), peptone (0.2% w/v), KCl·4 H2O (0.02% w/v), MgSO4·7 H2O (0.01% w/v) and hydrolysate (0.22% v/v). A 1.3-fold increase in amylase activity was obtained following novel media composition. All the factors considered in the study were found to be significant. The enzyme was purified by three step purification strategy, characterised and tested for anti-biofilm activity.

Ảnh hưởng của các yếu tố môi trường lên khả năng sinh tổng hợp chất ức chế α-amylase và α-glucosidase của dòng Streptomyces sp. TVS1

Streptomyces from the saline soil can produce many biologically active substances. In this study, Streptomyces sp. TVS1 from the saline soil of Tra Vinh province was cultured to determine the suitable conditions to produce a-amylase and a-glucosidase inhibitors. The culturing conditions were performed with different media (SCB, R, X and G), pH, and culturing periods. Determination of IC50 values showed that the G medium, which contained oatmeal as the rich nutrient source, had the best inhibitory effects on a-amylase and a-glucosidase about 2.67 and 0.062 mg/mL, respectively. The 5 days of culturing in the G-medium also gave the best IC50 values of about 2.64 and 0.073 mg/mL on a-amylase and a-glucosidase, respectively. G medium also showed that pH 8.0 was the most appropriate for the production of a-amylase and α-glucosidase inhibitors with the IC50 values of 2.66 mg/mL on a-amylase and 0.062 mg/mL on α-glucosidase. These results suggested that the Streptomyces sp. TVS1 was able to secrete the a-amylase and a-glucosidase inhibitors. For further investigation, particular enzyme inhibitors in the culture solution of this Streptomyces species should be identified, and their potential application in diabetes prevention should be explored.

A multicomponent system based on a blend of agroindustrial wastes for the simultaneous production of industrially applicable enzymes by solid-state fermentation

Abstract This study reports the use of statistical mixture design as a tool for the simultaneous production of lipase, CMCase, α-amylase, and β-glucosidase by Aspergillus niger under solid-state fermentation. Wheat bran, soybean meal, cottonseed meal, and orange peel were used as substrates, either individually or combined in different formulations, to study their synergistic or antagonistic effects on production of the enzymes. The highest lipase (323 U g-1) and CMCase (10 U g-1) activities were detected after 48 h, while the maximum activities of α-amylase (18 U g-1) and β-glucosidase (15 U g-1) occurred at 72 and 96 h, respectively. Considering the substrate formulation, the ternary mixture of wheat bran (1/3), soybean meal (1/3), and cottonseed meal (1/3) was the most versatile, showing production of CMCase (>5 U g-1) and α-amylase (>8 U g-1) at 24 h, lipase (>320 U g-1) at 72 h, and β-glucosidase (>10 U g-1) at 48 h.

Production and optimization of \u03b1-amylase from thermo-halophilic bacteria isolated from different local marine environments

BackgroundAmylases are among the most important enzymes which are of great significance for biotechnology and have almost completely replaced chemical hydrolysis of starch in the starch processing industry. The present study was concerned with the production and optimization of extracellular α-amylase from Bacillus sp. NRC22017.ResultsThe effect of various fermentation conditions on α-amylase production through shake-flask culture was investigated. Bacterial strain produces α-amylase was isolated from water in Wadi El-Natron. Based on microbiological, biochemical tests, and 16S rRNA gene sequences, the isolate was identified as Bacillus sp. NRC22017 and was later used for further studies. Maximum yield of α-amylase is 15.15 ± 0.47 U/ml from Bacillus sp. NRC22017; this strain is characterized with high temperature and high salinity in cultivated culture, and achieved maximum yield of α-amylase at pH 6.0 with inoculum size of 500 μl at 45 °C and aerobically incubation period of 72 h. The optimum volume of the fermentation medium was found to be 20 ml in 100 ml Erlenmeyer flask; the best starch and meat extract plus peptone concentration that provided the highest enzyme production from Bacillus sp. NRC22017 were found to be 2% and 1.05% (w/v) respectively.ConclusionEnzyme production was higher after optimizing the production conditions as compared to the basal medium.

Genetic Transformation of Bacillus licheniformis by Gene Responsible for α-Amylase Production in Media Contains Sugar Crops Wastes

Genetic Transformation of Bacillus licheniformis by Gene Responsible for α-Amylase Production in Media Contains Sugar Crops Wastes