Advances in Bioscience and Biotechnology

Volume 4, Issue 2 (February 2013)

ISSN Print: 2156-8456   ISSN Online: 2156-8502

Google-based Impact Factor: 1.18  Citations  h5-index & Ranking

A monograph on amylases from Bacillus spp.

HTML  XML Download Download as PDF (Size: 305KB)  PP. 227-241  
DOI: 10.4236/abb.2013.42032    7,409 Downloads   15,025 Views  Citations

ABSTRACT

Owing to the production of alpha, beta and gamma amylase subtypes; starch degrading microbes, especially bacteria have an invincible role in the food, fermentation, textile and paper industries. Of them, α-amylases from Bacillus spp. have contributed tremendous advancements in bio-industry, especially in starch, detergent and pharmaceutical arena. Though general reviews are seen in literature on amylases, no focused review is available yet solely on α-amylases produced by Bacillus spp. Hence, this focused review on α-amylases from the genus Bacillus is designed in such a way that it should give a vivid picture on most of the aspects on bacillial α-amylases in a handy module with an industrial perspective. With a short introduction on amylases in general, α-amylases from various species of Bacillus reviewed herein encompasses production of α-amylases by submerged and solid-state fermentations; nutrients and other factors required for maximizing production; immobilization strategies for whole cells or purified enzyme; an overview on the molecular weight of the enzyme; followed by distinct sections for purification, characterisation, stability and crystal structure; and concluded with a section on industrial applications of the α-amylases from Bacillus spp.

Share and Cite:

Benjamin, S. , Smitha, R. , Jisha, V. , Pradeep, S. , Sajith, S. , Sreedevi, S. , Priji, P. , Unni, K. and Josh, M. (2013) A monograph on amylases from Bacillus spp.. Advances in Bioscience and Biotechnology, 4, 227-241. doi: 10.4236/abb.2013.42032.

Cited by

[1] Diversity and activity of amylase-producing bacteria isolated from mangrove soil in Thailand
Biodiversitas Journal of …, 2022
[2] Fungal cellulases: overview and applications
Microbial Resource …, 2022
[3] The production of α-amylase enzyme from Iraqi isolate of Bacillus thuringiensis using agricultural-based media
2021
[4] Halobacillus blutaparonensis Strain M9 as a Source of Extracellular Serine Peptidases with Properties for Biotechnological Purposes
2021
[5] Adsorption of α-amylase and Starch on Porous Zinc Oxide Nanosheet: Biophysical Study
2021
[6] Nuevos métodos y soportes para la inmovilización de enzimas
2020
[7] Production, purification and characterization of thermostable alpha amylase from Bacillus subtilis Y25 isolated from decaying yam (Dioscorea rotundata) tuber
2020
[8] Extremophilic Amylases: Microbial Production and Applications
2020
[9] Solid state fermentation of keratinolytic proteases production using Bacillus spp. isolated from hair and mud sample of traditional leather processing ponds in North …
2019
[10] Enhancement of α-amylase production in pelleted Aspergillus tamarii through optimization for desizing of cotton fabric
2019
[11] Solid state fermentation of keratinolytic proteases production using Bacillus spp. isolated from hair and mud sample of traditional leather processing ponds in …
2019
[12] Overview of the process of enzymatic transformation of biomass
2019
[13] Effect of Calsporin® (Bacillus subtilis C-3102) addition to the diet on faecal quality and nutrient digestibility in healthy adult dogs
2019
[14] 芽胞杆菌属产 α-淀粉酶的研究进展
2019
[15] Extraction and Partial Purification of α-amylase Produced by Aspergillus niger Cultured on Banana Peel (Musa acumunata)
2018
[16] Column Chromatography Free Purification of Recombinant α-Amylase from Bacillus licheniformis by Tagging with Hydrophobic Elastin Like Polypeptide
Proceedings of the National Academy of Sciences, India Section B: Biological Sciences, 2017
[17] ГИДРОЛИТИЧЕСКИЕ ФЕРМЕНТЫ И ИХ БЕЛКОВЫЕ ИНГИБИТОРЫ В РЕГУЛЯЦИИ ВЗАИМООТНОШЕНИЙ РАСТЕНИЙ С ПАТОГЕНАМИ
2016
[18] Bacillus sp. ZBP10 SUŞU ile DERİN KÜLTÜR FERMANTASYONUNDA AMİLAZ ÜRETİMİ
2016
[19] Thermal Optimization of α-amylase Production in Brevibacillus sp
2016
[20] An Overview on Fungal Cellulases with an Industrial Perspective
Journal of Nutrition & Food Sciences, 2016
[21] Hydrolytic enzymes and their proteinaceous inhibitors in regulation of plant–pathogen interactions
Russian Journal of Plant Physiology, 2016
[22] PRODUCTION of AMYLASE by A NOVEL Bacillus sp. ZBP10 in SUBMERGED FERMENTATION.
GIDA/The Journal of FOOD, 2016
[23] Evaluation of brewer's spent grain as a substrate for production of hydrolytic enzymes by keratinolytic bacteria
Journal of Chemical Technology and Biotechnology, 2016
[24] An overview on fungal cellulases with an industrial perspective.
2016
[25] Production of amylase by a novel Bacillus sp. ZBP10 in submerged fermentation
2016
[26] Batch submerged fermentation in shake flask culture and bioreactor: Influence of different agricultural residuals as the substrate on the optimization of xylanase …
2016
[27] Синтез бактериями Bacillus amyloliquefaciens subsp. amyloliquefaciens ферментов, катализирующих гидролиз растительных полимеров
2015
[28] Purification and characterization of amylase from Bacillus thuringiensis subsp. kurstaki
Bt Research, 2015
[29] Biochemical characterization and industrial application of and# 945; amylases from bacteria
2015
[30] Optimization of Solid State Fermentation Conditions and Characterization of Thermostable Alpha Amylase from Bacillus subtilis (ATCC 6633)
J Bioprocess Biotech, 2015
[31] Aspectos relevantes del uso de enzimas en la industria de los alimentos
2015
[32] Thermo-and Detergent-stable Alkaline Protease from Bacillus thuringiensis Subsp. kurstaki
Bt Research, 2015
[33] СВОЙСТВА α-АМИЛАЗЫ БАКТЕРИЙ BACILLUS AMYLOLIQUEFACIENS SUBSP. AMYLOLIQUEFACIENS
ББК 30.16 я43 М59, 2015
[34] Molecular Mechanics Investigation of Diffrent Temperature Effects on Bacillus licheniformis α-amylase: A Computational Study
2015
[35] Halophilic alkali-and thermostable amylase from a novel polyextremophilic Amphibacillus sp. NM-Ra2
International Journal of Biological Macromolecules, 2014
[36] Optimization of various Nitrogen sources for the production of α–Amylase using Brevibacillus borstelensis R1 by Submerged fermentation
2014
[37] Amylase Production from Bacterial Isolates of Forest Soil, Selected Agricultural Waste and Kitchen Waste
2014
[38] Halophilic alkali-and thermostable amylase from a novel polyextremophilic Amphibacillus sp. NM-Ra2
International journal of biological macromolecules, 2014
[39] Starchy substrates for production and characterization of Bacillus subtilis amylase and its efficacy in detergent and breadmaking formulations
Starch‐St?rke, 2014
[40] Thermal adaptation of α-amylases: a review
Extremophiles, 2014
[41] Solid-State Fermentation for the Concomitant Production of δ-Endotoxin and Endospore from Bacillus thuringiensis subsp. kurstaki
Advances in Bioscience and Biotechnology, 2014
[42] Optimization of various Nitrogen sources for the production of-Amylase using Brevibacillus borstelensis R1 by Submerged fermentation
Int. J. Curr. Microbiol. App. Sci, 2014
[43] Properties, Modifications, and Nutrition
Polysaccharides: Natural Fibers in Food and Nutrition, 2014
[44] Charakterystyka i mozliwosci zastosowania bakterii z rodzaju Bacillus wyizolowanych z gleby
Polish Journal of Agronomy, 2014
[45] Optimization of various nitrogen sources for the production of α-amylase using Brevibacillus borstelensis R1 by submerged fermentation
2014
[46] Potato Starches: Properties, Modications, and Nutrition
Polysaccharides, 2014
[47] An Overview on the Crystal Toxins from Bacillus thuringiensis
Advances in Microbiology, 2013
[48] Dual production of amylase and δ-endotoxin by Bacillus thuringiensis subsp. kurstaki during biphasic fermentation
Microbiology, 2013
[49] 403401. Dual production of amylase and δ-endotoxin by Bacillus thuringiensis subsp. kurstaki during biphasic fermentation
2013
[50] Amylases: A Note on

Copyright © 2024 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.