An overview of the enzyme: Amylase and its industrial potentials

Ahmad, Mahnaz; Isah, U.; Raubilu, I.A.; Muhammad, Sanusi; Demirtaş, İbrahim

doi:10.4314/bajopas.v12i1.53s

Cited by 10 publications

(5 citation statements)

References 5 publications

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“…Moreover, the accumulation of waste‐water pollution and eutrophication problems in a river could be minimized by the utilization of enzymatic detergent, which can be easily broken down in the water. The α‐amylase from Bacillus or Aspergillus spp is used in the detergent formulation which can work at alkaline pH, lower temperature, and oxidative conditions (Ahmad et al, 2019). The α‐amylase from these species is environmentally friendly, and work in mild condition.…”

Section: Application Of α‐Amylasementioning

confidence: 99%

Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

Shad

Hussain

Usman

et al. 2023

Biotech & Bioengineering

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Amylases are biologically active enzymes that can hydrolyze starch to produce dextrin, glucose, maltose, and oligosaccharides. The amylases contribute approximately 30% to the global industrial enzyme market. The globally produced amylases are widely used in textile, biofuel, starch processing, food, bioremediation of environmental pollutants, pulp, and paper, clinical, and fermentation industries. The purpose of this review article is to summarize recent trends and aspects of α-amylases, classification, microbial production sources, biosynthesis and production methods, and its broad-spectrum applications for industrial purposes, which will depict the latest trends in α-amylases production. In the present article, we have comprehensively compared the biodiversity of α-amylases in different model organisms ranging from archaea to eukaryotes using in silico structural analysis tools. The detailed comparative analysis: regarding their structure, function, cofactor, signal peptide, and catalytic domain along with their catalytic residues of α-amylases in 16 model organisms were discussed in this paper. The comparative studies on alpha (α) amylases' secondary and tertiary structures, multiple sequence alignment, transmembrane helices, physiochemical properties, and their phylogenetic analysis in model organisms were briefly studied. This review has documented the recent trends and future perspectives of industrially important novel thermophilic α-amylases. In conclusion, this review sheds light on the current understanding and prospects of α-amylase research, highlighting its importance as a versatile enzyme with numerous applications and emphasizing the need for further exploration and innovation in this field.

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Section: Application Of α‐Amylasementioning

confidence: 99%

Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

Shad

Hussain

Usman

et al. 2023

Biotech & Bioengineering

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“…Cellulase has novel application in the production of fermentable sugars and ethanol, detergents and other chemicals (Jayasekara and Ratnayake, 2019). Similarly, Amylase is widely used for biotechnology processes including starch degradation, pharmaceutical applications, food liquefaction and saccharification, clinical, medical, analytical chemistry, paper manufacturing, baking and bread industry (Ahmad et al, 2019). Enzyme can be obtained from plants as well as microorganisms.…”

Section: Introductionmentioning

confidence: 99%

Production of multi enzyme preparation by Bacillus subtilis using mosambi peel as substrate

Singh¹,

Garg²,

Mathur³

et al. 2022

JEB

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Aim: To determine feasibility of using mosambi peel as substrate for multi enzyme production through microbial intervention. Methodology: Thirty-three bacterial isolates were isolated from biodegradable organic substrates and investigated in-vitro their biodegradable activities viz. pectinolytic, cellulolytic and amylolytic. The best performing bacterial isolate, exhibiting aforesaid activities were selected and identified using 16S rRNA technique. The factors, that influenced the fermentation, viz. temperature, pH and incubation period of bacterial culture were optimized for maximum production of multi enzymes viz. pectinase, cellulase and amylase using mosambi peel as substrate under solid-state fermentation conditions. Molecular weights of different enzymes present in multi-enzyme preparation were determined by SDS PAGE. The juice extraction efficiency of crude multi enzyme preparation was compared with that of pure commercial enzyme. Results: Out of thirty-three bacterial isolates, after primary and secondary screening, the best performing bacterial isolate was identified as Bacillus subtilis strain NG 105 (Genbank accession number MN493055). Higher enzyme activities were observed at pH 7.0, incubation temperature of 35°C and incubation period of 10 days for pectinase, cellulase and amylase using mosambi peel as substrate. The purified enzymes characterized by SDS-PAGE, revealed to have molecular mass of 65 kDa for pectinase, 50 kDa for cellulase and 55 kDa for amylase. Bagasse fibre was found to be the most suited matrix for immobilization. The juice extraction efficiency of partially purified crude multienzyme preparation was 88% of commercial pectinase. Interpretation: Mosambi peel is a suitable substrate for multienzyme production using Bacillus subtilis under solid-state fermentation condition.

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“…Also, amylase is one of the widely used enzymes during the preparation of fermented foods (Sharma et al 2020). Besides food and starch industry, they are also used in various other manufacturing companies such as paper and pulp, textiles and more (Ahmad et al 2019).…”

Section: Introductionmentioning

confidence: 99%

Mycelial Amylase and Cellulase Characterization as Well as Basidioma Physicochemical Analysis of Lingzhi Mushroom

Soeka

Ilyas

2021

J Bioteknol Biosains Indones

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Karakterisasi Amilase dan Selulase Miselial Serta Analisis Fisikokimia Basidioma Jamur Lingzhi (Ganoderma lucidum) Lingzi mushroom (Ganoderma lucidum) synthesizes enzymes which have anti-hyperglycemic and anti-diabetic activities. This preliminary study aims to characterize the amylase and cellulase activities of mycelial culture, and to analyze the physicochemical compounds in the basidioma of G. lucidum InaCC F11 and G. lucidum InaCC F106. The enzymes were characterized spectrophotometrically using DNS method, and the basidioma was subjected to proximate and high performance liquid chromatography (HPLC) analysis, as well as microstructural observation using scanning electron microscope. Results showed both strains demonstrated amylase activity, but not cellulase activity. The optimum activity of amylase in G. lucidum InaCC F11 mycelial cultures was achieved on the 3rd incubation day, at pH 5.5, 35 ºC temperature, and 1.5% substrate concentration, whereas that of G. lucidum InaCC F106 on the 7th incubation day, at pH 5, 40 ºC temperature, and 1.75% substrate concentration. Dried basidioma of G. lucidum InaCC F11 contained 93.72% carbohydrates, 3.06% protein, 0.85% fat, 0.768% crude fiber, 0.54% ash, and 1.83% moisture. In addition, HPLC detected the presence of phenols (0.036%), steroids (0.014 mg 100 mL-1), and active triterpenoid compounds. Jamur lingzi (Ganoderma lucidum) mensintesis enzim yang memiliki aktivitas anti-hiperglikemik dan anti-diabetes. Studi pendahuluan ini bertujuan mengkarakterisasi aktivitas amilase dan selulase kultur miselium, serta menganalisis senyawa fisikokimia pada basidioma G. lucidum InaCC F11 dan G. lucidum InaCC F106. Enzim dikarakterisasi secara spektrofotometri menggunakan metode DNS. Basidioma dianalisis secara proksimat, menggunakan kromatografi cair kinerja tinggi (KCKT), serta diamati mikrostrukturnya menggunakan mikroskop elektron. Hasil menunjukkan kedua strain tersebut memiliki aktivitas amilase, dan tidak ada aktivitas selulase. Aktivitas amilase optimum pada kultur miselium G. lucidum InaCC F11 dicapai pada inkubasi hari ke-3, pH 5,5, suhu 35 ºC, dan konsentrasi substrat 1,5%, sedangkan pada kultur miselium G. lucidum InaCC F106 dicapai pada inkubasi hari ke-7, pH 5, suhu 40 ºC, dan konsentrasi substrat 1,75%. Basidioma kering G. lucidum InaCC F11 mengandung karbohidrat 93,72%, protein 3,06%, lemak 0,85%, serat kasar 0,768%, abu 0,54%, dan kadar air 1,83%. Selain itu, KCKT mendeteksi adanya fenol (0,036%), steroid (0,014 mg 100 mL-1), dan senyawa triterpenoid aktif.

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An overview of the enzyme: Amylase and its industrial potentials

Cited by 10 publications

References 5 publications

Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

Production of multi enzyme preparation by Bacillus subtilis using mosambi peel as substrate

Mycelial Amylase and Cellulase Characterization as Well as Basidioma Physicochemical Analysis of Lingzhi Mushroom

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