scholarly journals Bioproduction of High-Concentration 4-Vinylguaiacol Using Whole-Cell Catalysis Harboring an Organic Solvent-Tolerant Phenolic Acid Decarboxylase From Bacillus atrophaeus

2019 ◽  
Vol 10 ◽  
Author(s):  
Lulu Li ◽  
Liangkun Long ◽  
Shaojun Ding
Keyword(s):  
Organic Solvent ◽  
Phenolic Acid ◽  
Acid Decarboxylase ◽  
Bacillus Atrophaeus ◽  
High Concentration ◽  
Whole Cell ◽  
Organic Solvent Tolerant ◽  
Phenolic Acid Decarboxylase ◽  
Whole Cell Catalysis ◽  
Solvent Tolerant

Production and Characteristics of the Whole-Cell Lipase from Organic Solvent Tolerant Burkholderia sp. ZYB002

2011 ◽  
Vol 166 (3) ◽  
pp. 536-548 ◽  
Author(s):  
Zheng-Yu Shu ◽  
Ji-Guang Wu ◽  
Lan-Xing Cheng ◽  
De Chen ◽  
Yong-Mei Jiang ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Whole Cell ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant

scholarly journals Biochemical and Structural Characterization of Cross-Linked Enzyme Aggregates (CLEAs) of Organic Solvent Tolerant Protease

Catalysts ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 55 ◽  
Author(s):  
Muhammad Syafiq Mohd Razib ◽  
Raja Noor Zaliha Raja Abd Rahman ◽  
Fairolniza Mohd Shariff ◽  
Mohd Shukuri Mohamad Ali
Keyword(s):  
Structural Analysis ◽  
Organic Solvent ◽  
Average Diameter ◽  
Relative Activity ◽  
Biochemical Properties ◽  
Biochemical Interaction ◽  
Organic Solvent Tolerant ◽  
Random Aggregate ◽  
Solvent Tolerant ◽  
The Stability

Cross-linked enzyme aggregates (CLEAs) is an immobilization technique that can be used to customize enzymes under an optimized condition. Structural analysis on any enzyme treated with a CLEA remains elusive and has been less explored. In the present work, a method for preparing an organic solvent tolerant protease using a CLEA is disclosed and optimized for better biochemical properties, followed by an analysis of the structure of this CLEA-treated protease. The said organic solvent tolerant protease is a metalloprotease known as elastase strain K in which activity of the metalloprotease is measured by a biochemical interaction with azocasein. Results showed that when a glutaraldehyde of 0.02% (v/v) was used under a 2 h treatment, the amount of recovered activity in CLEA-elastase was highest. The recovered activity of CLEA-elastase and CLEA-elastase-SB (which was a CLEA co-aggregated with starch and bovine serum albumin (BSA)) were at an approximate 60% and 80%, respectively. The CLEA immobilization of elastase strain K allowed the stability of the enzyme to be enhanced at high temperature and at a broader pH. Both CLEA-elastase and CLEA-elastase-SB end-products were able to maintain up to 67% enzyme activity at 60 °C and exhibiting an enhanced stability within pH 5–9 with up to 90% recovering activity. By implementing a CLEA on the organic solvent tolerant protease, the characteristics of the organic solvent tolerant were preserved and enhanced with the presence of 25% (v/v) acetonitrile, ethanol, and benzene at 165%, 173%, and 153% relative activity. Structural analysis through SEM and dynamic light scattering (DLS) showed that CLEA-elastase had a random aggregate morphology with an average diameter of 1497 nm.

Enhancing Volatile Phenol Concentrations in Wine by Expressing Various Phenolic Acid Decarboxylase Genes inSaccharomyces cerevisiae

2003 ◽  
Vol 51 (17) ◽  
pp. 4909-4915 ◽  
Author(s):  
Annél Smit ◽  
Ricardo R. Cordero Otero ◽  
Marius G. Lambrechts ◽  
Isak S. Pretorius ◽  
Pierre van Rensburg
Keyword(s):  
Phenolic Acid ◽  
Acid Decarboxylase ◽  
Volatile Phenol ◽  
Phenolic Acid Decarboxylase
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