[신간의 별자리x] 우리/미술, 그리고 ‘슬픔의 박물관’

Evolution of Protein Molecules

Pretreatment technologies are aimed to increase enzyme accessibility to biomass and yields of fermentable sugars. In general, pretreatment methods fall into four different categories including physical, chemical, physico-chemical, and biological. This paper comprehensively reviews the lignocellulosic wastes to bioethanol process with a focus on pretreatment methods, their mechanisms, advantages and disadvantages as well as the combinations of different pretreatment technologies. Moreover, the new advances in plant “omics” and genetic engineering approaches to increase cellulose composition, reduce cellulose crystallinity, produce hydrolases and protein modules disrupting plant cell wall substrates, and modify lignin structure in plants have also been expansively presented.

Lignocellulosic biomass to bioethanol, a comprehensive review with a focus on pretreatment

Manual for the Identification of Medical Bacteria.

A review of lignocellulose bioconversion using enzymatic hydrolysis and synergistic cooperation between enzymes--factors affecting enzymes, conversion and synergy.

A novel phytase with preferable characteristics from Yersinia intermedia.

Characterization of three novel thermophilic xylanases from Humicola insolens Y1 with application potentials in the brewing industry.

An α-galactosidase from an acidophilic Bispora sp. MEY-1 strain acts synergistically with β-mannanase

A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: Direct cloning, expression and enzyme characterization

We have identified a highly pH-adaptable and stable xylanase (XynA4) from the thermoacidophilic Alicyclobacillus sp. A4, a strain that was isolated from a hot spring in Yunnan Province, China. The gene (xynA4) that encodes this xylanase was cloned, sequenced, and expressed in Escherichia coli. It encodes a 338-residue polypeptide with a calculated molecular mass of 42.5 kDa. The deduced amino acid sequence is most similar to (53% identity) an endo-1,4-β-xylanase from Geobacillus stearothermophilus that belongs to family 10 of the glycoside hydrolases. Purified recombinant XynA4 exhibited maximum activity at 55°C and pH 7.0, had broad pH adaptability (>40% activity at pH 3.8–9.4) and stability (retaining >80% activity after incubation at pH 2.6–12.0 for 1 h at 37°C), and was highly thermostable (retaining >90% activity after incubation at 60°C for 1 h at pH 7.0). These properties make XynA4 promising for application in the paper industry. This is the first report that describes cloning and expression of a xylanase gene from the genus Alicyclobacillus.

A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability.

Huiying Luo

Papers

A novel phytase with preferable characteristics from Yersinia intermedia.

Characterization of three novel thermophilic xylanases from Humicola insolens Y1 with application potentials in the brewing industry.

An α-galactosidase from an acidophilic Bispora sp. MEY-1 strain acts synergistically with β-mannanase

A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: Direct cloning, expression and enzyme characterization

A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability.