Described herein are methods of producing transgenic Bombyx mori by targeting and modifying genomic regions associated with sericin proteins. Embodiments include vectors utilized for modifying one or more sericin genes. Embodiments include plasmid constructs utilized for molecular cloning of donor sequences configured for replacement of or insertion into a targeted sericin gene and utilized for transfection of Bombyx mori with the donor sequences. Embodiments include transgenic Bombyx mori that have been transfected with the donor sequences and are capable of producing a non-native protein product with minimized or prevented production of sericin.

A keratin hydrolysate including at least 88% by weight of free amino acids relative to the total weight of the amino acids of the hydrolysate, the remainder of the hydrolysate being peptides having a molecular mass of less than or equal to 800 Dalton, the hydrolysate also including L-cystine in a content ranging from 4% to 6%, cysteine in a content of less than or equal to 0.1%, and tyrosine in a content of less than or equal to 0.6% by weight, relative to the total weight of the hydrolysate. Also, a process for preparing the hydrolysate, the oral cosmetic use of the hydrolysate for improving the appearance of the nails and/or of the hair, and a dietary supplement including the hydrolysate and optionally vitamins, zinc and/or L-cystine.

Described herein are methods to produce keratin protein-based biomaterials, the parameters required to achieve improved extraction, the parameters required to improve isolation, the parameters of lyophilization and the grinding process to achieve consistent particulate sizes of protein materials.

The present disclosure relates to methods of preparing an ultra-low molecular weight keratin peptide and use thereof. In particular, the present disclosure relates to a method of preparing an ultra-low molecular weight keratin peptide using culturing a microorganism having keratinolytic activity in a medium including keratin, ultrafiltration, ion exchange chromatography and gel filtration chromatography, a peptide prepared by the method, and a cosmetic and food composition for preventing or improving skin aging or skin wrinkles including the same. According to the method of preparing a keratin peptide of the present invention, it is possible to eco-friendly biologically treat waste resources and efficiently purify and recover anti-aging functional ultra-low molecular weight keratin peptides. In addition, the keratin peptide of the present disclosure breaks down collagen to have abilities to inhibit MMP-1 expression and activity, which is an enzyme that causes skin aging, which has an excellent effect on anti-skin aging and skin wrinkle improvement and has no toxicity to skin cells. It is suitable for use as a cosmetic, pharmaceutical or food composition for preventing, improving or treating skin aging or skin wrinkles, thereby being effectively used for the efficient and rapid production and development of high value-added functional cosmetic substances.

The present disclosure provides methods and uses for keratin hydrolysates (e.g. feathers hydrolysates).

The invention is a non-hydrated, keratin wound dressing film comprising a fraction of keratins isolated from a solution of extracted keratins. Said fraction enables the formation of film with greater flexibility that can be achieved in film made from the unfractionated keratin extract. Also disclosed is a process of forming wound dressings and a method of obtaining said keratin fraction from an extract of human hair or other keratin raw materials.

A three-dimensional cell culture system that includes a keratin-based hydrogel precursor solution and a cell culture vessel is provided. The precursor solution includes solubilized keratin that has been functionalized to include a crosslinking moiety. The crosslinking moiety exhibits controllable crosslinking, e.g., a photopolymerizable crosslinking moiety. The crosslinking functionality is bonded to the keratin via cysteines following reduction of disulfide bonds of the native keratin. The precursor solution can be combined with cells to form a cell suspension that is disposed on a surface of the cell culture vessel. Alternatively, the cells can be added to a surface of a keratin-based hydrogel that has been formed on a surface of the cell culture vessel. The resulting three-dimensional cell culture system is a biomimetic/biologic, trypsin-degradable cell culture system for expansion of mammalian cells. The expanded cells are expected to possess a morphology similar to the primary cells prior to cultivation.

Methods are provided to produce optimal fractionations of charged keratins that have superior biomedical activity. Also provided are medical implants coated with these keratin preparations. Further provided are methods of treating blood coagulation in a patient in need thereof.

A keratin hydrolysate including at least 88% by weight of free amino acids relative to the total weight of the amino acids of the hydrolysate, the remainder of the hydrolysate being peptides having a molecular mass of less than or equal to 800 Dalton, the hydrolysate also including L-cystine in a content ranging from 4% to 6%, cysteine in a content of less than or equal to 0.1%, and tyrosine in a content of less than or equal to 0.6% by weight, relative to the total weight of the hydrolysate. Also, a process for preparing the hydrolysate, the oral cosmetic use of the hydrolysate for improving the appearance of the nails and/or of the hair, and a dietary supplement including the hydrolysate and optionally vitamins, zinc and/or L-cystine.

The present invention relates to a polypeptide solution in which polypeptide including an amino acid sequence derived from type I keratin that belongs to Cluster Ia is dissolved in a solvent including a formic acid or a solvent including an aprotic polar agent having a dipole moment of 3.0 D or more and an inorganic salt.