Publications by authors named "Yoon-Hyeok Kang"
The production of recombinant proteins in Escherichia coli is often challenged by cytoplasmic expression due to proteolytic degradation and inclusion body formation. Extracellular expression can overcome these problems by simplifying downstream processing and improving protein yields. This study aims to compare the efficiency of two Bacillus subtilis chitosanase signal peptides in mediating extracellular secretion in E.
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- * The team optimized conditions for extracting peptone from cutlassfish head muscle, achieving a nitrogen content indicative of effective breakdown and confirming its ability to support microbial growth comparable to and even better than commercial alternatives.
- * Test results showed that peptone from cutlassfish heads led to significantly higher expression levels of specific proteins in E. coli, highlighting its potential for biotechnological applications while promoting sustainable waste management in the fish processing sector.
We recently identified a β-agarase, Gaa16B, in the marine bacterium JEA5. Gaa16B, belonging to the glycoside hydrolase 16 family of β-agarases, shows less than 70.9% amino acid similarity with previously characterized agarases.
View Article and Find Full Text PDFCharacterization of glycoside hydrolase family 11 xylanase from Streptomyces sp. strain J103; its synergetic effect with acetyl xylan esterase and enhancement of enzymatic hydrolysis of lignocellulosic biomass.
Microb Cell Fact
July 2021
Article Synopsis
- Xylanase-containing enzyme cocktails, particularly the xynS1 gene from Streptomyces sp. J103, are effective in hydrolyzing xylan for industrial applications.
- The xynS1 gene encodes a protein that exhibits optimal activity at pH 5.0 and 55°C, with its activity significantly enhanced by certain metal ions.
- When combined with acetyl xylan esterase (AXE) and commercial cellulase, the rXynS1 enzyme showed a 2.3-fold improvement in lignocellulosic biomass hydrolysis compared to using cellulase alone.
Background: Acetyl xylan esterase plays an important role in the complete enzymatic hydrolysis of lignocellulosic materials. It hydrolyzes the ester linkages of acetic acid in xylan and supports and enhances the activity of xylanase. This study was conducted to identify and overexpress the acetyl xylan esterase (AXE) gene revealed by the genomic sequencing of the marine bacterium Ochrovirga pacifica.
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