Starch Hydrolysis Products Research Articles

Intestigation of the effect of a mixture of sprouted grains on the quality and nutritional value of bakery products

The object of research in the work is wheat bread, enriched with a mixture of sprouted grains. In sprouted grains due to the technology of soaking, the process of sprouting and drying, natural properties are preserved and multiplied. The protein contained in the sprouted grain of wheat, oats, barley and maize contains all the essential amino acids, which in percentage are up to 30 % of the total protein content. 5...10 times more vitamins of group B, H, E, PP and others. All high molecular weight compounds with high nutritional value are split into sprouted grains and are easily digested. A possible lack of use of sprouted grain in bread technology is high autolytic activity and acidity. This must be considered when improving the process. During the research, a mixture of sprouted grains of the Ukrainian producer LLC «Choice» (Kyiv) was used, which has the appearance of a powder that has a slightly sweet taste. It is established that the use of a mixture of sprouted grains in the technology of wheat bread activates the fermentation activity of the dough microflora, promotes the use of accelerated technology. The introduction of a mixture of sprouted grains increases the shelf life of fresh products. The obtained results are related to the improvement of the nutrition of the yeast microflora of the dough due to the content of sugars introduced with a mixture of sprouted grains. Intense coloring of the products crust is a consequence of the fact that the products of starch hydrolysis more actively react to melanoid formation. The slowing down of the staling of products with a mixture of sprouted grains, apparently, is due to the slowing down in them of the retrogradation of starch and the accumulation of low molecular weight dextrins due to active α-amylase. Due to the dosing of the mixture of sprouted grains in the amount of 5, 10 and 15 % by weight of the flour, the energy value of wheat bread increases in accordance with 252.7, 262.9 and 273.1 kcal, compared with the control – 232.3 kcal. The introduction of bread with a mixture of sprouted grains in the production will contribute to the expansion of the range of bakery products gerodietary destination.

Polyaniline stabilization of magnetic particles and immobilization of α-amylase

Magnetic particles (MAG), obtained by standard procedure of coprecipitation of Fe2+and Fe3+ in an excess of ammonia, and polyaniline modified magnetic particles MAG-PANI were used as carriers for immobilization of ?-amylase from Bacillus licheniformis. The formation of a polyaniline layer (PANI) on MAG particles was achieved by chemical polymerization of aniline. Immobilization was carried out by adsorption, as a simple, inexpensive and fast method that allows retention of a large portion of the initial activity of the immobilized enzyme. FTIR spectroscopy was used to characterize the obtained particles and to confirm changes dueto formation of a PANI layer and conjugation of ?-amylase on the particle surfaces. Particle size distribution was bimodal and three-modal for MAG and MAG-PANI, respectively. Appearance of a fraction of smaller MAG-PANI particles than MAG particles could be attributed to the formation of PANI particles without the MAG core. Measured values of Zeta potential for MAG-PANI were higher as compared to MAG indicating stabilization of particles in the presence of PANI. Relevant kinetic parameters for immobilized enzyme were determined from the Hanes plot. The apparent Km constant was 1.91 and 1.48 g L?1 for MAG-A and MAG-PANI-A, respectively, while ??m was 0.19 g L?1 min?1 for MAG and 0.32 g L?1 min?1 for MAG-PANI. The obtained values of Km indicated that modification of MAG by PANI enhanced kinetic properties of the immobilized enzyme. Moreover, the modification of MAG by PANI showed the increase in both pH and thermal stabilities of the immobilized enzyme. Studies of the operational activity of the immobilized enzyme on MAG-PANI have shown that 98.8% of starch was hydrolyzed over 20.0 min. In the first cycle in the packed bed reactor operated in a recycling mode, but approximately five times longer period was required to hydrolyze 93.5 of starch in the fifth cycle. In the continuous packed bed reactor without recycling, the degree of starch hydrolysis was not changed significantly during 4 h and was 88.8?1.6%, whereas the half-life of the biocatalyst was 6.2 h. Although coating MAG particles with a polyaniline offers many advantages, the main disadvantage is possible appearance of residues of aniline monomers and dimmers. The potential toxicity of these residues requires precise composition analysis of the product of starch hydrolysis catalyzed by ?-amylase adsorbed onto MAG-PANI.

The “Food Polymer Science” approach to the practice of industrial R&D, leading to patent estates based on fundamental starch science and technology

ABSTRACTThis article reviews the application of the “Food Polymer Science” approach to the practice of industrial R&D, leading to patent estates based on fundamental starch science and technology. The areas of patents and patented technologies reviewed here include: (a) soft-from-the-freezer ice creams and freezer-storage-stable frozen bread dough products, based on “cryostabilization technology” of frozen foods, utilizing commercial starch hydrolysis products (SHPs); (b) glassy-matrix encapsulation technology for flavors and other volatiles, based on structure-function relationships for commercial SHPs; (c) production of stabilized whole-grain wheat flours for biscuit products, based on the application of “solvent retention capacity” technology to develop flours with reduced damaged starch; (d) production of improved-quality, low-moisture cookies and crackers, based on pentosanase enzyme technology; (e) production of “baked-not-fried,” chip-like, starch-based snack products, based on the use of commercial modified-starch ingredients with selected functionality; (f) accelerated staling of a starch-based food product from baked bread crumb, based on the kinetics of starch retrogradation, treated as a crystallization process for a partially crystalline glassy polymer system; and (g) a process for producing an enzyme-resistant starch, for use as a reduced-calorie flour replacer in a wide range of grain-based food products, including cookies, extruded expanded snacks, and breakfast cereals.

Taste cell-expressed α-glucosidase enzymes contribute to gustatory responses to disaccharides

The primary sweet sensor in mammalian taste cells for sugars and noncaloric sweeteners is the heteromeric combination of type 1 taste receptors 2 and 3 (T1R2+T1R3, encoded by Tas1r2 and Tas1r3 genes). However, in the absence of T1R2+T1R3 (e.g., in Tas1r3 KO mice), animals still respond to sugars, arguing for the presence of T1R-independent detection mechanism(s). Our previous findings that several glucose transporters (GLUTs), sodium glucose cotransporter 1 (SGLT1), and the ATP-gated K(+) (KATP) metabolic sensor are preferentially expressed in the same taste cells with T1R3 provides a potential explanation for the T1R-independent detection of sugars: sweet-responsive taste cells that respond to sugars and sweeteners may contain a T1R-dependent (T1R2+T1R3) sweet-sensing pathway for detecting sugars and noncaloric sweeteners, as well as a T1R-independent (GLUTs, SGLT1, KATP) pathway for detecting monosaccharides. However, the T1R-independent pathway would not explain responses to disaccharide and oligomeric sugars, such as sucrose, maltose, and maltotriose, which are not substrates for GLUTs or SGLT1. Using RT-PCR, quantitative PCR, in situ hybridization, and immunohistochemistry, we found that taste cells express multiple α-glycosidases (e.g., amylase and neutral α glucosidase C) and so-called intestinal "brush border" disaccharide-hydrolyzing enzymes (e.g., maltase-glucoamylase and sucrase-isomaltase). Treating the tongue with inhibitors of disaccharidases specifically decreased gustatory nerve responses to disaccharides, but not to monosaccharides or noncaloric sweeteners, indicating that lingual disaccharidases are functional. These taste cell-expressed enzymes may locally break down dietary disaccharides and starch hydrolysis products into monosaccharides that could serve as substrates for the T1R-independent sugar sensing pathways.

A comparative study on normal and high sugary corn genotypes for evaluating enzyme consumption during dry-grind ethanol production

The necessity of amylolytic enzymes to convert starch into glucose during ethanol production is considered one of the cost increasing factors for corn ethanol. Enzyme consumption could be decreased partially by increasing free sugar contents in corn kernels that will be released and fermented simultaneously with the product of starch hydrolysis, producing an additional amount of ethanol without consuming any enzyme. The present work was conducted to evaluate the effects of grain sugar on the fermentable sugar and ethanol yields as well as enzyme requirement using four high sugary corn genotypes (HSGs) and their parent field corn lines (PFCs). The reducing sugar yield in HSGs did not vary significantly above the enzyme load of 1.5kg/MT of dry corn, while PFCs showed a range between 2.0 and 2.5kg/MT. The average final ethanol concentrations in HSGs and PFCs ranged from 15.25% to 17.5%(v/v) and 11.66% to 13.65%, respectively with the enzyme load at 1.5kg/MT, which reached to 16.49–17.94% in HSGs and 14.32–16.85% in PFCs as the enzyme load increased to 2.0kg/MT. These results suggest that high sugar content in corn kernels has the potential for decreasing enzyme consumption during dry-grind ethanol production with higher yields.

Physical properties of maltodextrin DE 10: Water sorption, water plasticization and enthalpy relaxation

Maltodextrins are hydrolysis products of starch. The present research aimed to study physical properties of maltodextrins (water sorption, water plasticization behavior and enthalpy relaxation) and highlighting their functions as food components. The GAB and GT equation were fitted successfully to water sorption and water plasticization data of maltodextrin DE 10. The critical water content and critical water activity values at 25 °C were 14 g water/100 g dry solid and 0.68 aw, respectively. The Kohlrausch–Williams–Watt (KWW model) and extended Adam-Gibbs model fitted well the enthalpy relaxation kinetics data. The non-exponential parameter, β value of maltodextrin DE 10 was within in the range of 0.15–0.93 and its value was dependent on the water activity. At 25 °C, Maltodextrin with aw <0.43 was stable glassy as indicated by very long enthalpy relaxation time. The KWW model gave a more accurate fit than the extended Adam-Gibbs model. Arrhenius model fitted well to enthalpy relaxation data and gave a free activation energy (Ea) of 459.5 kJ/mol.

On the use of differential solubility in aqueous ethanol solutions to narrow the DP range of food-grade starch hydrolysis products

Considerable research is focused on understanding the functionality of starch hydrolysis products (SHP) consisting of glucose, maltose, maltooligosaccharides (MOS), and maltopolysaccharides (MPS). A confounding factor in this research is the high molecular dispersity of commercially available SHP. The study presented herein characterizes a flexible fractionation approach for lowering the dispersity of such products. This was accomplished by fractionating a corn syrup solids (CSS) preparation based on the differential solubility of its component saccharides in aqueous-ethanol solutions. Products obtained from selected fractionations were characterized with respect to degree of polymerization (DP; liquid chromatography), dextrose equivalency (reducing sugar assays), and prevalence of branching (NMR). Glucose and maltose were preferentially removed from CSS using high (⩾90%) ethanol extractants. Preparations with relatively narrow ranges of MOS, lower DP MPS, and higher DP MPS were obtained through repetitive 70%-ethanol extractions. Linear, as opposed to branched, MOS and MPS were preferentially extracted under all conditions tested.

A novel saccharifying α‐amylase of Antarctic psychrotolerant fungi Geomyces pannorum: Gene cloning, functional expression, and characterization

A DNA segment encoding a novel α‐amylase was cloned from the Antarctic psychrotolerant fungi Geomyces pannorum. The gene has an open reading frame of 1761 bp, deduced 586 amino acids, revealing a relatively low homology to α‐amylases from diverse fungal genera. The α‐amylase gene was overexpressed in Pichia pastoris, and the recombinant α‐amylase was purified and characterized. Enzymatic activity was optimal at pH 6.0 and 70°C, and the specific activity was 9.78 × 103 U/mg when using soluble starch as substrate. Moreover, the enzyme retained more than 90% of its maximum activity over a wide pH range (6.0–9.0). Exceptionally, the main hydrolysis products of soluble starch catalyzed by the enzyme were glucose and maltose, of which glucose reached a concentration of 68.8% (w/w). This is the first report on identifying thermophilic fungal amylase from psychrotolerant fungi. Also, the preliminary study on the high‐glucose‐producing α‐amylase with detailed enzymatic properties shows a potential application prospect in syrup industry.

Physicochemical properties of whey protein conjugated with starch hydrolysis products of different dextrose equivalent values

Conjugation of whey protein with maltodextrin (MD) or corn syrup solids (CSS) having dextrose equivalent (DE) values in the range 6–38 was achieved by heating solutions of 5% whey protein isolate and 5% MD or CSS, initial pH 8.2, at 90 °C for up to 24 h. Maximum conjugation, with production of limited colour and advanced Maillard products was achieved after 8 h of heating. The extent of conjugation increased with increasing DE value of the MD and CSS ingredients. Conjugation increased whey protein solubility at pH 4.5 from 9% for whey protein heated alone to 24% for whey protein heated in the presence of CSS38 at 90 °C for 8 h. Conjugation of whey proteins with MD6 or CSS38 enhanced the stability to heating of protein solutions at 85 °C for 3 min with 50 mm added NaCl.

Evaluation of high sugar containing corn genotypes as viable feedstocks for decreasing enzyme consumption during dry-grind ethanol production

Requirement of costly enzymes (α-amylase and glucoamylase) for converting starch into glucose before fermentation is considered one of the cost increasing factors for corn ethanol. Enzyme consumptions can possibly be reduced during dry-grind ethanol production by increasing free sugar contents in corn kernels that will be released and fermented simultaneously with the product of starch hydrolysis, producing an additional amount of ethanol without consuming any enzyme. A comparative study was conducted to evaluate the effect of kernel sugars on enzyme requirement and yields of both hydrolysis and fermentation, using four high sugary corn genotypes (HSGs) and their parent field corns (PFCs). Enzymatic hydrolysis of the genotypes with four enzyme loads (1, 2, 3 and 4 kg MT−1 of dry corn) showed that HSGs produced higher proportions of reducing sugars (RS) in all conditions than PFCs did. Sufficient amounts of RS were produced by HSGs utilizing an enzyme load of 3 kg MT−1, whereas, PFCs consumed 4 kg MT−1 for their best yields. Likewise, HSGs produced higher concentrations of ethanol consuming lower amount of enzymes during fermentation. Therefore, HSGs could be considered as potential feedstocks for enhancing ethanol yield and reducing enzyme consumptions during dry-grind ethanol production.

Production and characterization of raw starch degrading enzyme from a newly isolated thermophilic filamentous bacterium, Laceyella sacchari LP175

Medium optimization for production of raw starch degrading enzyme (RSDE) from a newly isolated thermophilic filamentous bacterium, Laceyella sacchari LP175, is described. Yeast extract and raw cassava starch were found to be the best nitrogen and carbon sources, respectively, for enzyme production. Response surface methodology with Plackett–Burman design and central composite design showed that an optimized concentration of 4.93 g/L raw cassava starch and 2.8 g/L yeast extract in basal medium yielded 181.1 U/mL RSDE activity in a shaking flask at 50°C and pH 7.0 after 48 h. Maximum RDSE activity in crude enzyme was achieved at pH 6.5 and 50°C. The major end product of raw cassava starch hydrolysis was maltose (88%). The Km and Ki values of raw cassava starch and maltose, respectively, were found to be 2.85 mg/mL and 1.04 mg/mL. Raw cassava starch at 100 g/L was hydrolyzed with 200 U/mL RSDE for 12 h, yielding 36.8% hydrolysis. The addition of commercial glucoamylase (1.6 U/mL) synergistically enhanced the hydrolysis reaction, yielding 70% hydrolysis (equivalent to 78.0 g/L glucose). The high efficiency of RSDE produced from L. sacchari LP175 could be useful for replacing conventional enzymes currently used in various raw starch processing industries.

Gene cloning and characterization of a thermostable organic-tolerant α-amylase from Bacillus subtilis DR8806

The gene encoding an extracellular α-amylase from Bacillus subtilis DR8806 was cloned into pET28a(+) vector and expressed in Escherichia coli BL21 (DE3). The recombinant enzyme with molecular mass of 76kDa exhibited optimal activity at pH 5.0 and 70°C with high stability in pH and temperature ranges of 4.0–9.0 and 45–75°C. The enzyme showed a half-life of 125min at 70°C. The α-amylase activity enhanced in the presence of Na+, K+, and Ca2+ ions, while Zn2+, Pb2+, and Hg2+ ions inhibited the activity. The recombinant α-amylase exhibited high stability towards ioninc detergents sodium dodecyl sulfate (SDS) and cetyl trimethylammonium bromide (CTAB). Organic solvents in reaction media increased the α-amylase activity. TLC analysis showed that maltoriose and maltose were the major end products of enzymatic starch hydrolysis. Presenting various properties of recombinant α-amylase makes it well suited as a potential candidate for industrial usages.

Halophilic alkali- and thermostable amylase from a novel polyextremophilic Amphibacillus sp. NM-Ra2

Extracellular gluco-amylo-pullulanase from Amphibacillus sp. NM-Ra2 was purified to homogeneity by ethanol precipitation, anion exchange chromatography and gel filtration chromatography. Molecular mass of the enzyme was 50kDa (SDS-PAGE). The enzyme showed maximal activity at 1.9M NaCl, pH50°C 8.0 and 54°C and was active from 0 to 4.3M NaCl and 37 to 65°C. The enzyme was inhibited by EDTA and was stable and active in the presence of PMSF, DTT, H2O2, Triton-X-100, Tween 20 and Tween 80. Ca2+ is inessential for activity. The amylase was stimulated with K+ and inhibited with Cu2+ and Mg2+. Hg2+, Zn2+ and Fe2+ had no effect on activity. Amylase was stable and active in the presence of ethanol, methanol and benzene (25%, v/v). The enzyme hydrolyzed linear and branched polysaccharides including pullulan, glycogen and amylopectin, and hydrolyzed raw wheat starch and raw corn starch (14.6% and 13.5% over 2h). Amylase activity was inhibited by soluble starch concentrations greater than 0.3%. The major products of soluble starch hydrolysis were maltose and maltotriose. The amylase, being halophilic and alkali-thermostable, in addition to being resistant to surfactants, oxidizing agents and organic solvents, can find applications in the starch processing, pharmaceutical, food and paper/pulp industries.

Regulation of β-amylase activity by alkylresorcinols

The effects of two alkylresorcinols, namely, methylresorcinol (MR) and hexylresorcinol (HR), which are chemical analogues of the natural anabiosis factors of some bacteria, on the catalytic activity of β-amylase has been investigated. When water-soluble potato starch is used as a substrate, MR in a concentration ranging from 0.8 to 12.9 mmol/L raises the activity of β-amylase to 170%. HR at a concentration ranging from 0.05 to 0.35 mmol/L stimulates a weak increase in the activity of β-amylase to 115%. A further increase in the concentration (0.75 mmol/L) leads to inhibition by 50%. The interaction of MR with β-amylase allows one to increase the general yield of the hydrolysis products of potato and malt starch by 1.5 to 1.6 times, to enhance the rate of hydrolysis by 4 to 5 times, and to extend the temperature and pH ranges of catalysis. Non-competitive activation in the presence of MR and non-competitive inhibition in the presence of HR are observed upon determining the kinetic parameters of the starch hydrolysis by β-amylase modified with alkylresorcinols.

A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some α-amylases from Bacillus sp. isolated in Serbia

Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown on two different temperatures in submerged fermentation for the raw-starch-digesting a-amylases production. All strains except Bacillus sp. 18 produced more ?-amylase on 37?C. The hydrolysis of raw corn starch followed same pattern. Efficient hydrolysis was obtained with ?-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown on 37?C and Bacillus sp. 18 grown on 50?C. Zymography after isoelectric focusing shown that ?-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 ?C, while growing at 50?C induced only 1 or 2 isoforms. TLC analysis of hydrolysis products of raw corn and soluble starch by ?-amylases revealed production of various mixtures of oligosaccharides. In most cases G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that obtained a-amylases can be used for starch liquefying or short-chain-oligosaccharide forming, depending on what type of starch (raw or soluble) was used for the hydrolysis.

Glucoamylase from a newly isolated Aspergillus niger FME: Detergent-Mediated production, purification, and characterization

Glucoamylase (EC 3.2.1.3) is an important group of enzymes in starch processing, also referred to as amyloglucosidases, which are exo-acting amylases that release glucose from the nonreducing end of starch and related oligosaccharides. The glucoamylase newly isolated from the Aspergillus niger FME) was reported for the first time. This enzyme was produced by detergent-mediated release and purified to ∼9.11 fold using Sephadex-G 100 and ion-exchange chromatography. Molecular mass of the glucoamylase was ∼36 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The product of starch hydrolysis, analysed by thin-layer chromatography, showed the presence of glucose. The optimum pH and temperature for glucoamylase activity was 5.0 and 45°C, respectively. The Km and Vmax values of the enzyme were also determined using soluble starch as substrate as 94 μg/mL and 39.02 U/mg, respectively. Moreover, glucoamylase was slightly activated by presence of Na and K ions and 10–20% inhibition was observed in presence of Zn2+, Sn2+, Mg2+, Ni2+, Mn2+, and almost 80% with Cu2+ ions, whereas the presence of ethylene diamine tetra acetic acid (EDTA) did not show significant inhibition. Glucoamylase, also assayed for surfactant property, shows significant surfactant tolerance at high concentrations of detergent and can retain 90% of its activity. Finally, secondary structure analysis of glucoamylase by circular dichroism spectroscopy showed the presence of 48% α-helix, 11% β-sheet, and 41% random structure.

Midgut morphophysiology in Sitophilus zeamais Motschulsky, 1855 (Coleoptera: Curculionidae)

Sitophilus zeamais is one of the most aggressive pests of stored grains, causing a significant decrease in the nutritional quality of the grains and major losses in economic trade. The foraging capacity of this pest is assigned to its highly efficient digestive system. Investigations on the morphofunctional features of the midgut, which is the most active region of the alimentary canal, are fundamental to understand the feeding habits of this species. In this study, the midgut of adult insects was isolated, processed, and analyzed on light microscopy, scanning and transmission electron microscopy, protein and enzymatic activities determination, including analyses of the starch hydrolysis products. In S. zeamais, the midgut was differentiated into anterior midgut and posterior midgut, and consisted of digestive, regenerative and endocrine cells. The anterior midgut showed high density of regenerative crypts. Cells containing organelles associated with protein synthesis and presence of amylases and lipases indicated that majority of the digestion process occurred in the anterior midgut. The posterior midgut exhibited numerous gastric caeca and peritrophic membrane. Cells with poorly differentiated cytoplasmic into organelles, elongated microvilli, and low enzymatic activities indicated that the posterior midgut was mainly involved in absorption.

A novel glucoamylase activated by manganese and calcium produced in submerged fermentation by Aspergillus phoenicis

This study investigates the production of glucoamylase from Aspergillus phoenicis in Machado Benassi (MB) medium using 1% maltose as carbon source. The maximum amylase activity was observed after four days of cultivation, on static conditions at 30 °C. Glucoamylase production was induced by maltose and inhibited by different glucose concentrations. The optimum of temperature and pH were 60-65 °C, and 4.5 or 5.0 to sodium acetate and Mcllvaine buffers, respectively. It was observed that the enzyme was totally stable at 30-65 °C for 1 h, and the pH range was 3.0-6.0. The enzyme was mainly activated by manganese (176%), and calcium (130%) ions. The products of starch hydrolysis were analyzed by thin layer chromatography and after 3 h, only glucose was detected, characterizing the amylolytic activity as a glucoamylase.

Interaction of wheat -amylase with maltose and glucose as examined by fluorescence

Fluorescence of wheat β-amylase (WBA) was quenched by the interaction with maltose or glucose, which are competitive inhibitors of WBA, suggesting that the states of tryptophan and tyrosine residues could be changed by the interaction. The fluorescence emitted by excitation at 280 and 295 nm was titrated by changing the concentrations of maltose and glucose. The dissociation constant (Kd) values of the WBA-maltose and WBA-glucose complexes were determined to be 0.20 ± 0.12 M for maltose and 0.36 ± 0.11 M for glucose at 25°C, pH 5.4. Maltose exhibited additional binding mode at higher concentration with a distinct Kd value (1.5 ± 0.4 M). The Kd values at various temperatures and pHs are in agreement with the inhibitor constant (Ki) values previously reported. The negative standard enthalpy changes (ΔH°) of the WBA association with glucose and maltose indicate that the associations are exothermic. The association constant (Ka) and ΔG° values of the maltose and glucose binding to WBA decreased slightly with increasing temperature from 25°C to 45°C but not dependent on pH change (pH 3.0, 5.4 and 9.0). Fluorescence of WBA could be used as a structural probe to examine the inhibitory interaction with the products of starch hydrolysis.

Glucose released by hydrolytic activity of amylase influences the pigment synthesis in Penicillium sp NIOM‐02

Carbon catabolite repression is generally considered as a regulatory mechanism to ensure sequential synthesis of secondary metabolites. In this study we made an attempt to understand the influence of amylase activity on pigment synthesis in Penicillium sp NIOM-02. The amylase activity is inversely proportional to pigment production. The high performance liquid chromatography analysis of amylase reaction revealed glucose as the major product of starch hydrolysis. The fungus grown in acarbose (inhibitor of amylase) incorporated media produced higher quantities of pigments. Apparently, glucose released due to amylase activity influenced the pigment synthesis by cAMP signaling pathway.