Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

Authors

  • F. Pouryafar Chemical Engineering, Babol Noshirvani University of Technology
  • Ghasem Najafpour Biochemical & Chemical Engineering, Noshirvani University of Technology, Babol
  • N. Noshadi Chemical Engineering, Babol Noshirvani University of Technology
Abstract:

This article doesn't have abstract

Upgrade to premium to download articles

Sign up to access the full text

Already have an account?login

similar resources

Improved thermostable α-amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation.

Thermostable α-amylase is of great importance in the starch fermentation industry; it is extensively used in the manufacture of beverages, baby foods, medicines, and pharmaceuticals. Bacillus amyloliquefaciens produces thermostable α-amylase; however, production of thermostable α-amylase is limited. Ion-beam implantation is an effective method for mutation breeding in microbes. We conduct...

full text

Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1

This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...

full text

High yield recombinant thermostable α-amylase production using an improved Bacillus licheniformis system

BACKGROUND Some strains of Bacillus licheniformis have been improved by target-directed screening as well as by classical genetic manipulation and used in commercial thermostable alpha-amylase and alkaline protease production for over 40 years. Further improvements in production of these enzymes are desirable. RESULTS A new strain of B. licheniformis CBBD302 carrying a recombinant plasmid pHY...

full text

thermal denaturation of α-amylase from bacillus amyloliquefaciens in the presence of sodium dodecyl sulphate*

the thermal denaturation of α-amylase from bacillus amyloliquefaciens has been investigated in the presence and absence of sodium dodecyl sulphate (sds) over the temperature range (293-373) k in 20 mm sodium phosphate buffer, ph 6.9, using temperature scanning spectroscopy. the presence of sds caused the destabilization of α-amylase resulting in a decrease in the temperature of unfolding with a...

full text

Production and biochemical characterization of a thermostable phytase from Bacillus amyloliquefaciens LOR10

Phytase can improve the nutritional value of plant-based foods by enhancing protein digestibility and mineral availability through phytate digestion in the stomach and the food processing industry. Microbial sources are more promising for the production of phytases on a commercial scale. The objectives of this exploration were to screening and isolation of phytase-producing bacteria from hot sp...

full text

Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68

An alkaliphilic and highly thermostable α-amylase producing Bacillus sp. was isolated from Van soda lake. Enzyme synthesis occurred at temperatures between 25°C and 40°C. Analysis of the enzyme by SDS-PAGE revealed a single band which was estimated to be 66 kDa. The enzyme was active in a broad temperature range, between 20°C and 90°C, with an optimum at 50°C; and maximum activity was at pH 10....

full text

My Resources

Save resource for easier access later

Save to my library Already added to my library

{@ msg_add @}


Journal title

volume 30  issue 8

pages  1110- 1117

publication date 2017-08-01

By following a journal you will be notified via email when a new issue of this journal is published.

Hosted on Doprax cloud platform doprax.com

copyright © 2015-2023