Purification and characterization of Rhizoctonia solani AG-4 strain ZB-34 α-amylase produced by solid-state fermentation using corn bran

2017 ◽  
Vol 43 (3) ◽  
pp. 257-267 ◽  
Author(s):  
Umit Uzun ◽  
Erkol Demirci ◽  
Melike Yildirim Akatin

Abstract Background: Aim of the study was to produce α-amylase cheaply from Rhizoctonia solani AG-4 strain ZB-34 by solid-state fermentation and investigate its suitability for some industries. Methods: Rhizoctonia solani AG-4 strain ZB-34 α-amylase was purified with starch affinity method. Results: The best production of enzyme was achieved by using corn bran. Optimum pH and temperature were 5.5 and 50°C, respectively. Vmax and K0.5 were determined as 238.8 U/mg protein and 0.03% from substrate-activity curve. Activity was maintained about 100% in the tested pHs after 1 day incubation. The enzyme conserved full of its activity at 4 and 28°C for 120 min. Mn2+, Ca2+, Tween 20, Triton X-100 and Triton X-114 activated the enzyme. The enzyme was highly active in the presence of some commercial detergents. The chocolate stains on the cotton fabrics were more effectively cleaned with the combination of a commercial detergent and purified enzyme. The purified enzyme also clarified the raw apple juice and desized the cotton fabrics. Conclusion: The results showed that Rhizoctonia solani AG-4 strain ZB-34 α-amylase might have potential application as a detergent additive. In addition, its activity between pH 4.0 and 7.0 may facilitate its use in the food and fruit processing industries.

2019 ◽  
Vol 49 (9) ◽  
pp. 858-867
Author(s):  
Cirium V. Chinmayee ◽  
Cheral Vidya ◽  
Amsaraj Rani ◽  
Sridevi Annapurna Singh

2006 ◽  
Vol 22 (9) ◽  
pp. 991-998 ◽  
Author(s):  
Muhammad Ibrahim Rajoka ◽  
Muhammad Waheed Akhtar ◽  
Atif Hanif ◽  
A. M. Khalid

PLoS ONE ◽  
2021 ◽  
Vol 16 (8) ◽  
pp. e0255899
Author(s):  
Wenhua Yang ◽  
Jianli Zhou ◽  
Jean Damascene Harindintwali ◽  
Xiaobin Yu

Minor ginsenosides (MGs) (include ginsenoside F2, Compound K, PPT, etc), which are generally not produced by ginseng plants naturally, are obtained by deglycosylation of major ginsenosides. However, the conventional processes used to produce deglycosylated ginsenosides focus on the use of intestinal microorganisms for transformation. In this study, an edible and medicinal mushroom Stereum hirsutum JE0512 was screened from 161 β-glucosidase-producing soil microorganisms sourced from wild ginseng using the plate coloration method. Furthermore, JE0512 was used for the production of CK from ginseng extracts (GE) in solid-state fermentation (SSF) using 20 g corn bran as substrate, 4 g GE, and 20% inoculation volume, and the results showed that the highest CK content was 29.13 mg/g. After combining S. hirsutum JE0512 with cellulase (Aspergillus niger), the MGs (F2, CK, and PPT) content increased from 1.66 to 130.79 mg/g in the final products. Our results indicate that the Stereum genus has the potential to biotransform GE into CK and the combination of S. hirsutum JE0512 and cellulase could pave the way for the production of MGs from GE.


2009 ◽  
Vol 63 (4) ◽  
pp. 331-335 ◽  
Author(s):  
Sanja Grbavcic ◽  
Dejan Bezbradica ◽  
Ivanka Karadzic ◽  
Zorica Knezevic-Jugovic

Enzymes produced by indigenous Pseudomonas aeruginosa strain have been subjected to research considering their potential application as detergent additives. As previously noted, lipase produced by Pseudomonas aeruginosa is highly alkaline, thermostable and solvent tolerant. Furthermore, same strain exhibits both lipase and protease activity establishing this lipase as potentially desirable component of enzyme-containing detergents. Further research was carried out to investigate insusceptibility of this lipase against coexisting native protease, several commercial surfactants, oxidizing agents and commercial detergents. Lipases and proteases remained highly active when incubated with several different surfactants and oxidizing agents under washing conditions. Moreover, presence of surfactants and oxidizing agents such as Tween? 20 and Triton? X-100 initially augment lipase and protease activity. Additionally, crude lipase preparation was insusceptible to coexisting native protease hence indicating possible storage stability. Overall, the remarkable properties of these enzymes make them potential detergent additives.


Planta Medica ◽  
2013 ◽  
Vol 79 (13) ◽  
Author(s):  
G Juodeikiene ◽  
D Cizeikiene ◽  
A Maruška ◽  
E Bartkiene ◽  
L Basinskiene ◽  
...  

2020 ◽  
Vol 21 (3) ◽  
pp. 211-220 ◽  
Author(s):  
Chandrasai Potla Durthi ◽  
Madhuri Pola ◽  
Satish Babu Rajulapati ◽  
Anand Kishore Kola

Aim & objective: To review the applications and production studies of reported antileukemic drug L-glutaminase under Solid-state Fermentation (SSF). Overview: An amidohydrolase that gained economic importance because of its wide range of applications in the pharmaceutical industry, as well as the food industry, is L-glutaminase. The medical applications utilized it as an anti-tumor agent as well as an antiretroviral agent. L-glutaminase is employed in the food industry as an acrylamide degradation agent, as a flavor enhancer and for the synthesis of theanine. Another application includes its use in hybridoma technology as a biosensing agent. Because of its diverse applications, scientists are now focusing on enhancing the production and optimization of L-glutaminase from various sources by both Solid-state Fermentation (SSF) and submerged fermentation studies. Of both types of fermentation processes, SSF has gained importance because of its minimal cost and energy requirement. L-glutaminase can be produced by SSF from both bacteria and fungi. Single-factor studies, as well as multi-level optimization studies, were employed to enhance L-glutaminase production. It was concluded that L-glutaminase activity achieved by SSF was 1690 U/g using wheat bran and Bengal gram husk by applying feed-forward artificial neural network and genetic algorithm. The highest L-glutaminase activity achieved under SSF was 3300 U/gds from Bacillus sp., by mixture design. Purification and kinetics studies were also reported to find the molecular weight as well as the stability of L-glutaminase. Conclusion: The current review is focused on the production of L-glutaminase by SSF from both bacteria and fungi. It was concluded from reported literature that optimization studies enhanced L-glutaminase production. Researchers have also confirmed antileukemic and anti-tumor properties of the purified L-glutaminase on various cell lines.


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