Nam Lee

Bio: Nam Lee is an academic researcher from Yonsei University. The author has contributed to research in topics: Cobb angle & Laminoplasty. The author has an hindex of 7, co-authored 15 publications receiving 450 citations.

Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe

Abstract: A native-feather-degrading thermophilic anaerobe was isolated from a geothermal hot stream in Indonesia. Isolate AW-1, identified as a member of the species Fervidobacterium islandicum, was shown to degrade native feathers (0.8%, w/v) completely at 70 °C and pH 7 with a maximum specific growth rate (0.14 h–1) in Thermotoga-Fervidobacterium (TF) medium. After 24 h of culture, feather degradation led to an increase in free amino acids such as histidine, cysteine and lysine. Moreover, nutritionally essential amino acids such as tryptophan and methionine, which are rare in feather keratin, were also produced as microbial metabolites. A homomultimeric membrane-bound keratinolytic protease (>200 kDa; 97 kDa subunits) was purified from a cell extract of F. islandicum AW-1. The enzyme exhibited activity toward casein and soluble keratin optimally at 100 °C and pH 9, and had a half-life of 90 min at 100 °C. The enzyme showed higher specific activity for the keratinous substrates than other proteases and catalyzed the cleavage of peptide bonds more rapidly following the reduction of disulfide bridges in feather keratin by 10 mM dithiothreitol. Therefore, the enzyme from F. islandicum AW-1 is a novel, thermostable keratinolytic serine protease.

Feasibility Study of Utilization of Action Camera, GoPro Hero 4, Google Glass, and Panasonic HX-A100 in Spine Surgery:

Abstract: Study design Study for feasibility of commercially available action cameras in recording video of spine. Objective Recent innovation of the wearable action camera with high-definition video recording enables surgeons to use camera in the operation at ease without high costs. The purpose of this study is to compare the feasibility, safety, and efficacy of commercially available action cameras in recording video of spine surgery. Summary of background data There are early reports of medical professionals using Google Glass throughout the hospital, Panasonic HX-A100 action camera, and GoPro. This study is the first report for spine surgery. Methods Three commercially available cameras were tested: GoPro Hero 4 Silver, Google Glass, and Panasonic HX-A100 action camera. Typical spine surgery was selected for video recording; posterior lumbar laminectomy and fusion. Three cameras were used by one surgeon and video was recorded throughout the operation. The comparison was made on the perspective of human factor, specification, and video quality. Results The most convenient and lightweight device for wearing and holding throughout the long operation time was Google Glass. The image quality; all devices except Google Glass supported HD format and GoPro has unique 2.7K or 4K resolution. Quality of video resolution was best in GoPro. Field of view, GoPro can adjust point of interest, field of view according to the surgery. Narrow FOV option was the best for recording in GoPro to share the video clip. Google Glass has potentials by using application programs. Connectivity such as Wi-Fi and Bluetooth enables video streaming for audience, but only Google Glass has two-way communication feature in device. Conclusion Action cameras have the potential to improve patient safety, operator comfort, and procedure efficiency in the field of spinal surgery and broadcasting a surgery with development of the device and applied program in the future. Level of evidence N/A.

Microbial keratinases and their prospective applications: an overview.

Abstract: Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide “keratin” recalcitrant to the commonly known proteolytic enzymes trypsin, pepsin and papain. These enzymes are largely produced in the presence of keratinous substrates in the form of hair, feather, wool, nail, horn etc. during their degradation. The complex mechanism of keratinolysis involves cooperative action of sulfitolytic and proteolytic systems. Keratinases are robust enzymes with a wide temperature and pH activity range and are largely serine or metallo proteases. Sequence homologies of keratinases indicate their relatedness to subtilisin family of serine proteases. They stand out among proteases since they attack the keratin residues and hence find application in developing cost-effective feather by-products for feed and fertilizers. Their application can also be extended to detergent and leather industries where they serve as specialty enzymes. Besides, they also find application in wool and silk cleaning; in the leather industry, better dehairing potential of these enzymes has led to the development of greener hair-saving dehairing technology and personal care products. Further, their prospective application in the challenging field of prion degradation would revolutionize the protease world in the near future.

Biochemical features of microbial keratinases and their production and applications.

Abstract: Keratinases are exciting proteolytic enzymes that display the capability to degrade the insoluble protein keratin. These enzymes are produced by diverse microorganisms belonging to the Eucarya, Bacteria, and Archea domains. Keratinases display a great diversity in their biochemical and biophysical properties. Most keratinases are optimally active at neutral to alkaline pH and 40–60°C, but examples of microbial keratinolysis at alkalophilic and thermophilic conditions have been well documented. Several keratinases have been associated to the subtilisin family of serine-type proteases by analysis of their protein sequences. Studies with specific substrates and inhibitors indicated that keratinases are often serine or metalloproteases with preference for hydrophobic and aromatic residues at the P1 position. Keratinolytic enzymes have several current and potential applications in agroindustrial, pharmaceutical, and biomedical fields. Their use in biomass conversion into biofuels may address the increasing concern on energy conservation and recycling.

Keratin: dissolution, extraction and biomedical application

Abstract: Keratinous materials such as wool, feathers and hooves are tough unique biological co-products that usually have high sulfur and protein contents A high cystine content (7–13%) differentiates keratins from other structural proteins, such as collagen and elastin Dissolution and extraction of keratin is a difficult process compared to other natural polymers, such as chitosan, starch, collagen, and a large-scale use of keratin depends on employing a relatively fast, cost-effective and time efficient extraction method Keratin has some inherent ability to facilitate cell adhesion, proliferation, and regeneration of the tissue, therefore keratin biomaterials can provide a biocompatible matrix for regrowth and regeneration of the defective tissue Additionally, due to its amino acid constituents, keratin can be tailored and finely tuned to meet the exact requirement of degradation, drug release or incorporation of different hydrophobic or hydrophilic tails This review discusses the various methods available for the dissolution and extraction of keratin with emphasis on their advantages and limitations The impacts of various methods and chemicals used on the structure and the properties of keratin are discussed with the aim of highlighting options available toward commercial keratin production This review also reports the properties of various keratin-based biomaterials and critically examines how these materials are influenced by the keratin extraction procedure, discussing the features that make them effective as biomedical applications, as well as some of the mechanisms of action and physiological roles of keratin Particular attention is given to the practical application of keratin biomaterials, namely addressing the advantages and limitations on the use of keratin films, 3D composite scaffolds and keratin hydrogels for tissue engineering, wound healing, hemostatic and controlled drug release

Bacterial Keratinases: Useful Enzymes for Bioprocessing Agroindustrial Wastes and Beyond

Abstract: Keratin-rich wastes in the form of feathers, hair, nails, and horn are highly available as byproducts of agroindustrial processing. The increased needs for energy conserving and recycling, summed with the huge increase in poultry industry, have strongly stimulated the search for alternatives for the management of recalcitrant keratinous wastes. Keratinases, which are produced by several bacteria that have been often isolated from soils and poultry wastes, show potential use in biotechnological processes involving keratin hydrolysis. Although these isolates are mostly restricted to the genera Streptomyces and Bacillus, the diversity of keratinolytic bacteria is significantly greater. Bacterial keratinases are mostly serine proteases, although increased information about keratinolytic metalloproteases, particularly from Gram-negative bacteria, became available. These enzymes are useful in processes related with the bioconversion of keratin waste into feed and fertilizers. Other promising applications have been associated with keratinolytic enzymes, including enzymatic dehairing for leather and cosmetic industry, detergent uses, and development of biopolymers from keratin fibers. The use of keratinases to enhance drug delivery in some tissues and hydrolysis of prion proteins arise as novel outstanding applications for these enzymes.