Jeng-Jie Wang

Works (9)

Updated: July 5th, 2023 16:02

2006 article

Keratinase technology: from feather degradation and feed additive,to prion destruction.

Shih, J. C. H., & Wang, J. J. (2006, November 8). CABI Reviews.

By: J. Shih* & J. Wang*

topics (OpenAlex): Animal Genetics and Reproduction; Enzyme Production and Characterization; Cancer Research and Treatments
Source: NC State University Libraries
Added: August 6, 2018

2006 article

Sup35NM-His6 aggregates: A prion-like protein useful in prion degradation studies

Wang, J.-J., Borwornpinyo, R., & Shih, J. C. H. (2006, October 2). Enzyme and Microbial Technology.

By: J. Wang*, R. Borwornpinyo & J. Shih n

author keywords: yeast prion; Sup35NM-His6 proteases; prion degradation
topics (OpenAlex): Prion Diseases and Protein Misfolding; Trace Elements in Health
TL;DR: It is suggested that Sup35NM-His6 could be a useful tool to assess the effectiveness of prion degradation for the prevention of TSE. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2005 article

Development of an asporogenic Bacillus licheniformis for the production of keratinase

Wang, J.-J., Greenhut, W. B., & Shih, J. C. H. (2005, February 16). Journal of Applied Microbiology.

By: J. Wang*, W. Greenhut n & J. Shih n

author keywords: asporogenic Bacillus; Bacillus licheniformis; keratinase
MeSH headings : Bacillus / genetics; Bacillus / metabolism; Bacillus / physiology; Bioreactors; Genes, Bacterial; Genetic Engineering; Hot Temperature; Industrial Microbiology; Microscopy, Electron; Peptide Hydrolases / biosynthesis; Polymerase Chain Reaction; Spores, Bacterial
topics (OpenAlex): Enzyme Production and Characterization; Phytase and its Applications; Bone and Dental Protein Studies
TL;DR: B. licheniformis PWD‐1 is a keratin‐degrading, spore‐forming bacterium isolated from a poultry waste digester and a sporulation‐deficient mutant of B. lichensiformis WBG was developed and characterized. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2004 article

Extracellular Production of a Functional Soy Cystatin by Bacillus subtilis

Kang, I. S., Wang, J.-J., Shih, J. C. H., & Lanier, T. C. (2004, July 16). Journal of Agricultural and Food Chemistry.

By: I. Kang n, J. Wang n, J. Shih n & T. Lanier n

author keywords: protease inhibitor; cloning; signal peptide; secretion; surimi
MeSH headings : Bacillus subtilis / genetics; Cloning, Molecular; Cystatins / biosynthesis; Cystatins / genetics; Cystatins / metabolism; Escherichia coli / genetics; Glucose / pharmacology; Recombinant Proteins; Soybeans / chemistry; Soybeans / genetics; Transfection
topics (OpenAlex): Enzyme Production and Characterization; Studies on Chitinases and Chitosanases; Bacterial Genetics and Biotechnology
TL;DR: A recombinant Bacillus subtilis producing soy cystatin was developed by subcloning with a soy cysteine protease gene cloned in Escherichia coli and two gene fragments of signal peptides from kerA and sacB were introduced and compared for secretion efficiency of Cystatin. (via Semantic Scholar)
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14. Life Below Water (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2004 article

Increased production of Bacillus keratinase by chromosomal integration of multiple copies of the kerA gene

Wang, J. J., Rojanatavorn, K., & Shih, J. C. H. (2004, July 22). Biotechnology and Bioengineering.

By: J. Wang*, K. Rojanatavorn n & J. Shih n

author keywords: keratinase; chromosomal integration; hyperproduction; Bacillus licheniformis
MeSH headings : Bacillus / enzymology; Bacillus / genetics; Bacillus subtilis / enzymology; Bacillus subtilis / genetics; Cell Proliferation; Chromosomes, Bacterial / genetics; Cloning, Molecular; Enzyme Activation; Gene Dosage; Gene Expression Regulation, Bacterial / physiology; Gene Expression Regulation, Enzymologic / physiology; Genetic Enhancement / methods; Mutagenesis, Site-Directed / genetics; Peptide Hydrolases / biosynthesis; Peptide Hydrolases / chemistry; Peptide Hydrolases / genetics; Promoter Regions, Genetic; Protein Engineering / methods; Recombinant Proteins / metabolism; Substrate Specificity
topics (OpenAlex): Enzyme Production and Characterization; Animal Genetics and Reproduction; Cancer Research and Treatments
TL;DR: The strong constitutive promoter P43 not only increased the keratinase production in plasmid‐based expression in DB104 but also improved the enzyme yield of the integrants of T399D. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2003 article

Keratinase in starter diets improves growth of broiler chicks

Odetallah, N. H., Wang, J. J., Garlich, J. D., & Shih, J. C. (2003, April 1). Poultry Science.

By: N. Odetallah*, J. Wang*, J. Garlich* & J. Shih*

author keywords: broiler; protease; keratinase; growth performance; starter feed
MeSH headings : Age Factors; Animal Feed; Animal Nutritional Physiological Phenomena; Animals; Body Weight / drug effects; Chickens / growth & development; Digestive System / chemistry; Dose-Response Relationship, Drug; Female; Male; Peptide Hydrolases / administration & dosage; Peptide Hydrolases / pharmacology; Random Allocation; Soybeans; Viscosity; Weight Gain / drug effects; Zea mays
topics (OpenAlex): Animal Nutrition and Physiology; Aquaculture Nutrition and Growth; Enzyme Production and Characterization
TL;DR: Results of these experiments indicate that the growth of broiler chickens can be significantly improved by dietary supplementation with PWD-1 keratinase. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2003 article

Production and characterization of bio-immobilized keratinase in proteolysis and keratinolysis

Wang, J.-J., Swaisgood, H. E., & Shih, J. C. H. (2003, April 30). Enzyme and Microbial Technology.

By: J. Wang n, H. Swaisgood n & J. Shih n

author keywords: keratinase; bio-immobililzation; streptavidin; fusion protein
topics (OpenAlex): Enzyme Production and Characterization; Animal Genetics and Reproduction; Protein Hydrolysis and Bioactive Peptides
TL;DR: Extracellular production of keratinase–streptavidin fusion protein was accomplished by the cloning of Bacillus subtilis with a transforming plasmid carrying the kerA - stp fusion gene. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2002 article

Bioimmobilization of keratinase using Bacillus subtilis and Escherichia coli systems

Wang, J. J., Swaisgood, H. E., & Shih, J. C. H. (2002, December 17). Biotechnology and Bioengineering.

By: J. Wang n, H. Swaisgood n & J. Shih n

author keywords: keratinase; immobilization; streptavidin; fusion protein
MeSH headings : Bacillus subtilis / classification; Bacillus subtilis / enzymology; Bacillus subtilis / genetics; Cells, Cultured; Enzymes, Immobilized / chemical synthesis; Enzymes, Immobilized / genetics; Enzymes, Immobilized / isolation & purification; Enzymes, Immobilized / metabolism; Escherichia coli / classification; Escherichia coli / enzymology; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Macromolecular Substances; Peptide Hydrolases / classification; Peptide Hydrolases / genetics; Peptide Hydrolases / isolation & purification; Peptide Hydrolases / metabolism; Protein Binding; Protein Engineering / methods; Recombinant Fusion Proteins / biosynthesis; Recombinant Fusion Proteins / genetics; Species Specificity; Streptavidin / biosynthesis; Streptavidin / classification; Streptavidin / genetics; Streptavidin / isolation & purification
topics (OpenAlex): Enzyme Production and Characterization; Animal Genetics and Reproduction; Bone and Dental Protein Studies
TL;DR: A new genetic construct was developed to produce the keratinase-streptavidin fusion protein, so that the purification and immobilization of the fusion protein onto a biotinylated matrix can be accomplished in a single step. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

1999 article

Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29

Wang, J.-J., & Shih, J. C. H. (1999, June 1). Journal of Industrial Microbiology & Biotechnology.

By: J. Wang n & J. Shih n

author keywords: keratinase production; fermentation; Bacillus; recombinant strain
topics (OpenAlex): Enzyme Production and Characterization; Animal Genetics and Reproduction; Phytase and its Applications
TL;DR: After respective optimization of fermentation conditions, keratinase production by B. licheniformis PWD-1 is approximately 40% higher than thatBy B. subtilis FDB-29, a recombinant strain, and control of pH is not necessary. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

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