Abstract: The present invention provides a mineral-peptide chelate comprising a peptide consisting of 2˜18 amino acids and a mineral chelated to the peptide, wherein the peptide can be a hydrolysate obtained by hydrolyzing soybean or other protein materials with proteases, or a product obtained by hydrolyzing soybean or other protein material with proteases and fermentation. The mineral-peptide chelate of the present invention may further comprise a carrier which covers the peptide and the mineral which is chelated to the peptide.
Abstract: The present invention provides a mineral-peptide chelate comprising a peptide consisting of 2˜18 amino acids and a mineral chelated to the peptide, wherein the peptide can be a hydrolysate obtained by hydrolyzing soybean or other protein materials with proteases, or a product obtained by hydrolyzing soybean or other protein material with proteases and fermentation. The mineral-peptide chelate of the present invention may further comprise a carrier which covers the peptide and the mineral which is chelated to the peptide.
Type:
Application
Filed:
March 2, 2010
Publication date:
March 3, 2011
Applicant:
Nugen Bioscience (Taiwan) Co., Ltd.
Inventors:
Shann-Tzong Jiang, Li-Jung Yin, Hsueh-Ming Tai
Abstract: The present invention relates to a purified sulfite reductase which has the following characteristics: a. It functions to catalyze the reduction of sulfites to sulfides or to recover the sulfhydryl groups from disulfide groups, b. In the aforesaid catalysis of the reduction, reduced nicotinamide dinucleotide phosphate (NADPH), methyl viologen (MVH) or other donors acts as an electron donor, c. Its molecular weight is from 100,000 to 400,000, d. The optimal temperature for its activity is from 20° C. to 30° C., and e. The optimal pH for its activity is from 6.5 to 8.0. The present invention also relates to a process for producing the purified sulfite reductase, and a method for recovering the proteins of denatured fish by using said sulfite reductase in solution or powder form.
Abstract: The present invention relates to a N-glycosylation-modified recombinant chicken cystatin, characterized in that Asn106-Ile108 in its amino acid sequence is modified to Asn106-Thr108. The present invention also relates to a method for producing said N-glycosylation-modified recombinant chicken cystatin, wherein a site-directed mutated cDNA encoding chicken cystatin is cloned in an expression vector, with which a yeast strain is in turn transformed, and the yeast transformant is then cultured for producing a recombinant chicken cystatin wherein the Asn residue in the Asn106-Thr108 of its amino acid sequence that is produced by said site-directed mutagenesis can be modified by N-glycosylation. The N-glycosylation-modified recombinant chicken cystatin disclosed in the present invention has improved stability in a freezing-thawing process and in a heating process.