Contents of summary
Part 1 Basics
Chapter 1. Definition
NISHIYAMA Toshio (Tokyo University of Agriculture and Technology)

Chapter 2. Collagen Family of Proteins
MIZUNO Kazunori (Nippi Research Institute of Biomatrix)
Chapter 3. The Structure and Physical Properties of Collagen
NOMURA Yoshihiro (Tokyo University of Agriculture and Technology)
K. L. Goh (Newcastle University in Singapore)
Chapter 4. Diverse Biological Functions of the Collagen Family
MIYATA Shinji (Tokyo University of Agriculture and Technology)
Chapter 5. Collagen Biosynthesis (1) Overview,~A Molecular Ensemble 2.0: the Complexity of Collagen Biosynthesis in therER~
ISHIKAWA Yoshihiro (Department of Ophthalmology, University of California, San
Francisco, School of Medicine)
Chapter 6. Collagen Biosynthesis (2) Post-translational Modifications
TAGA Yuki (Nippi Research Institute of Biomatrix)
Chapter 7. Collagen Biosynthesis (3) Collagen Cross-linking
YAMAUCHI Mitsuo, TERAJIMA Masahiko (Division, Oral and Craniofacial Health
Sciences University of North Carolina at Chapel Hill)
Chapter 8. Collagen Degradation and Matrix Metalloproteinase
INADA Masaki (Tokyo University of Agriculture and Technology)
Chapter 9. Abnormal Collagen Metabolism and Related Diseases
ITOH Yoshifumi (Kennedy Institute of Rheumatology, University of Oxford)

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Chapter 10. Synthetic Collagen
Kazuki C. KURODA, KOIDE Takaki (Department of Chemistry and Biochemistry,
School of Advanced Science and Engineering, Waseda University)
Chapter 11. Digestion and Absorption of Collagen and Its Derivatives
SATO Kenji (Marine Biological Function, Division of Applied Biosciences, Graduate
School of Agriculture, Kyoto University)
SHIGEMURA Yasutaka (Department of Food & Nutritional Science, Tokyo Kasei
University)
Chapter 12. Mammalian Collagen
TANAKA Keisuke, HATTORI Shunji (Nippi Research Institute of Biomatrix)
Chapter 13. Fish and Shellfish Collagen
ISHIHARA Kenji (National Research Institute of Fisheries Science, Fisheries Researchand Education Agency of Japan)
HIRAOKA Yoshinobu (Ehime Institute of Invention)
Chapter 14. Lower animal Collagen
ARAI Katsuhiko (Scleroprotein and Leather Research Institute, Faculty of Agriculture,
Tokyo University of Agriculture and Technology)

Part 2 Application
Chapter 15. Application of Collagen, Overview
NOMURA Yoshihiro (Scleroprotein and Leather Research Institute, Faculty ofAgriculture, Tokyo University of Agriculture and Technology)
Chapter 16. Leather and Leather Goods
YOSHIMURA Keijia (Japan Leather and Leather Goods Industries Association)
Chapter 17. Animal Glue and Industrial Gelatin
DOI Masahiro (Asahi Gelatine Industrial Co., Ltd)
Chapter 18. Inkstick and Classical Animal GlueUDAKA Kentaro (Independent Administrative Institution National Institutes for
Cultural Heritage, Tokyo National Research Institute for Cultural Properties)

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Chapter 19. Foods Using Collagen
SUZUKI Satoshi (Nippi, incorporated Fuji Factory)
Chapter 20. Functional Food
KOIZUMI Seiko, MATSUSHITA Aya, DAIMON Mona, HIMENO Ai (Research andDevelopment Center, Nitta Gelatin Inc.)
Chapter 21. Collagen in the Cosmetic Field
AMANO Satoshi (Shiseido Global Innovation Center)
Chapter 22. Characteristics and Applications of Medical Collagen Products
FUJIMOTO Ichiro (Koken Research Center, Koken Co., Ltd.)

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Chapter 1. Definition
NISHIYAMA Toshio (Tokyo University of Agriculture and Technology)
Collagens are animal-specific proteins and do not exist in plants. They havenot been identified in almost all unicellular organisms. It has still been
investigated what multicellular animals are the first to acquire collagens.
The tissues of the most ancient animals, Ctenophora and Porifera, were
investigated on type IV collagen expression and basement membrane
formation, since in recent researches type IV collagen revealed as theevolutionarily most ancient member of the vertebrate collagen family. The
results revealed that type IV collagen played a critical role in the transitionof unicellular organisms to multicellular animals. These reports suggestthat collagen is a key protein that enabled the evolution of animals.
Collagens are the most abundant proteins in mammals including human(around 30% of total protein mass). They were thought as proteins
responsible for structural formation and maintenance. Recent research
progress has revealed that they play important roles in biological functions
such as cell adhesion, proliferation, differentiation, signal transduction,
morphogenesis, and wound healing. The collagen superfamily comprises 28
types numbered with Roman numerals (type I collagen to type XXVIII
collagen) that contain at least one triple-helical domain. Each collagenconsists of three polypeptide chains, called α chains, numbered with Arabic
numerals. The three α chains that form the triple helical part of themolecule are composed of repeating peptide triplets of glycine (Gly)-XaaYaa. Xaa is often proline and Yaa is frequently 4-hydroxyproline. The
collagens are classified to several families by function and domain homology.
Keywords: collagen, triple helix, chain, collagen super family, evolution

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Chapter 2. Collagen Family of Proteins
MIZUNO Kazunori (Nippi Research Institute of Biomatrix)
Collagen super family proteins in vertebrates are classified as 28 types ofcollagen. In addition, some other proteins have collagen triple helicalstructure. In this chapter, vertebrate collagen has shortly been reviewed interms of structure, function, and localization. The function of the mostabundant type of collagen, type I, is still largely unknown. Collagen familyof proteins functions not only as the structural scaffold of cells but also as
the regulators of cell differentiation and growth. Each of collagensuperfamily members is responsible for maintaining the structure andfunction of the organism through a variety of functions.
Keywords: fibrillar collagen, FACIT, transmembrane collagen, ficolin, collectin

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Chapter 3. The Structure and Physical Properties of Collagen
NOMURA Yoshihiro (Scleroprotein and Leather Research Institute,
Faculty of Agriculture, Tokyo University of Agriculture and Technology)
K. L. Goh (Newcastle University in Singapore)
Study on the structure of collagen has been carried out from X-ray
diffraction images of biological samples that is a structural protein with aclear molecular orientation without crystallization. In 1955,
Ramachandran and Karha proposed the triple helix model of tropocollagen.
Then, in 1961, Rich and Crick proposed a new collagen structural model of
10/3-helix. Okuyama showed the 7/3-helix collagen model from structuralmodel from structural analysis using a synthetic peptide of (Pro-Hyp-Gly)9.
The study on the physical properties of collagen was summarized in the
keynote lecture by Goh of the International Union of Leather Technologists
and Chemists Societies (IULTCS) in 2019. This session describes thebiosynthesis, hierarchical structure, three-dimensional structure andphysical properties of collagen.
Keywords: structure, collagen triple helix model, physical properties

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Chapter 4. Diverse Biological Functions of the Collagen Family
MIYATA Shinji (Scleroprotein and Leather Research Institute, Faculty ofAgriculture, Tokyo University of Agriculture and Technology)
Collagens are the most abundant proteins in vertebrates. 28 different
collagen types have been identified so far. Its abundance, tissue distribution,and function can vary widely among collagen types. All collagen members
share a common structural feature, the presence of at least one triple-helicaldomain, which corresponds to a number of (Gly-X-Y)n repeats (X being
frequently proline and Y hydroxyproline) in the amino acid sequence.
Depending on the types of collagen, the triple-helices are formed by threeidenticalchains (homotrimers), or by two or more different chains(heterotrimers). Some collagens, such as type I collagen, consist entirely of
the triple-helical repeats; others contain nonhelical domains in addition to
the triple-helical domain. Classical fibril-forming collagens are well-known toplay structural roles and contribute to mechanical properties, organization,and shape of tissues. Recent studies have also revealed the functional
importance of other collagens that do not form fibers by themselves. The
physiological roles of the various types of collagen have been discovered
through studies using genetically modified mouse models. Moreover, recent
large-scale genome-wide association studies have revealed that the mutations
in collagen genes cause a variety of human diseases. In this article, we review
the functions of collagen, which have been obtained from studies mainly inmice and humans.
Keywords: collagen super family, non-fibrous collagen, molecular species,
genetically modified mice, collagen-related diseases

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Chapter 5. Collagen Biosynthesis (1): Overview,
A Molecular Ensemble 2.0: the Complexity of Collagen Biosynthesis in therER
ISHIKAWA Yoshihiro (Department of Ophthalmology, University of California, San
Francisco, School of Medicine)Collagen is a unique molecule because a very complicated biosynthesis process generates
this most abundant protein in humans with a relatively simple structure. This
complicated process is carried out by over twenty molecules, including various enzymes
and molecular chaperones, and which terms a molecular ensemble. In this review, tounderstand this sophisticated process, a molecular ensemble is classified into three
individual steps 1) translation and post-translational modification, 2) triple helix
formation, and 3) transport. Each step includes recent findings and updated information
describing an expanded molecular ensemble, which calls a molecular ensemble 2.0.
Keywords: endoplasmic reticulum (ER), protein biosynthesis, protein folding, protein
trafficking, quality control

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Chapter 6. Collagen Biosynthesis (2): Post-translational Modifications
TAGA Yuki (Nippi Research Institute of Biomatrix)
Collagen extensively receives a series of highly organized enzymatic posttranslational modifications, including prolyl hydroxylation and lysylhydroxylation/glycosylation. These collagen-specific post-translational
modifications play various roles in the structure and function of collagen,such as stabilization of collagen triple helix, regulation of cross-linkformation, and contribution to interaction of collagen with cells. The
importance of collagen post-translational modifications is evidenced fromthe fact that abnormalities of specific modification enzymes lead to severe
connective tissue diseases. However, there are several minor modifications
whose function is still unclear. In this chapter, I review studies about the
enzymatic post-translational modifications determining the quality ofcollagen and also introduce chemical modifications (glycation andcarbamylation), which accumulate in tissue collagen with aging and certain
diseases.
Keywords: post-translational modification, hydroxylation, glycosylation,
glycation, carbamylation

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Chapter 7. Collagen Biosynthesis (3) Collagen Cross-linking
YAMAUCHI Mitsuo, TERAJIMA Masahiko (Division, Oral and
Craniofacial Health Sciences University of North Carolina at Chapel Hill)
The main functions of connective tissues, i.e. providing support, form andconnectivity, highly depend on the physicochemical properties of fibrillar
collagens, especially its major component, type I collagen. During thebiosynthesis, type I collagen undergoes various intra- and extracellularpost-translational modifications, and the molecules are packed into a fibril
and stabilized by covalent intra- and intermolecular cross-linking. Crosslinking is initiated by the conversion of the lysine and hydroxylysine
residues in the amino- and carboxy-termini of the molecule i.e. telopeptides,
to aldehydes by the action of lysyl oxidases. Then, the aldehydes can trigger
a series of condensation reactions with the adjacent amino acids to form bi-,tri- and tetra-valent cross-links. The quantity, type and maturation of crosslinking vary depending on tissues, aging and pathological state. Recently,
the regulatory mechanisms of lysine modifications relevant to cross-linking
and how abnormal cross-linking is associated with various pathologies suchas fibrosis, osteogenesis imperfecta and cancer development/metastasis
have been gradually deciphered. In this chapter, we will overview the basics
of collagen cross-linking and recent advancement in this field.
Keywords: cross-link, post-translational modification, lysyl hydroxylase,chaperone, cancer

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Chapter 8. Collagen Degradation and Matrix Metalloproteinase
INADA Masaki (Department of Biotechnology and Life Science, Tokyo
University of Agriculture and Technology)
Collagen is a major component of extracellular matrix (ECM) and is broadly
present in skin, cartilage, skeleton, and various organs. Therefore, its
production and degradation are strictly regulated to maintain tissue
structures and homeostasis. Type I collagen is mainly produced in
hypodermis, tendons, ligaments, and bones. Type II and X collagens areproduced in cartilages, and type-IV collagen consists of basement
membranes of epithelial tissues.
Matrix metalloproteinases (MMPs) are the family of ECM-degrading
enzymes including collagenases such as MMP-1, MMP-8, and MMP-13. In
addition, MMP-2, membrane-type MMPs (MT-MMPs), and a serine
protease of cathepsin K are also collagen-degrading enzymes. These
enzymes have been shown to express during organ formation, tissue
destruction, and wound healing, and many molecular biologists haveinvestigated this topic all over the world.
During 1980s to 1990s, the initial studies of the enzymatic activities ofcollagenases were studied using purified recombinant proteins. In 2000s,
the gene recombination technique was used in mice to evaluate thephenotype, and these were inserted gene mutation in the active site of
MMPs, MMPs gene transgenic mice, and gene knockout mice.
Collagen degradation has been shown to play a role in different pathologicalconditions, including osteochondral-bone destruction, inflammatory
diseases, cancer invasion, neo-angiogenesis in which all of them wereassociated with enzymatic activities of MMPs for tissue destruction. In thisreview, we summarize the knowledge of type I collagen degradation bycollagen-degrading MMPs and describe the research transition of thetechniques.
Keywords: matrix metalloproteinase, collagenase, gelatinase, geneticallymodified mouse

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Chapter 9. Abnormal Collagen Metabolism and Related Diseases
ITOH Yoshifumi (Kennedy Institute of Rheumatology, University of Oxford)
Fibrillar collagens, such as type I collagen, are major components of bone,skin, and interstitial matrix of different organs. The levels of the collagens
in the tissue are regulated precisely by the production and the degradation.
Once this balance is disrupted and the production of collagens exceeds thedegradation, it would result in fibrotic conditions, leading to organ
malfunction. On the other hand, if the degradation exceeds production, it
causes tissue destruction. When cells migrate within a tissue, regardless ofpathological or physiological conditions, fibrillar collagen that acts as aphysical barrier needs to be locally degraded. But in the event found in
disease conditions including cancer cell invasion and growth or
inflammatory arthritis such as rheumatoid arthritis, the cell migration
associating fibrillar collagen degradation is highly upregulated. Anothertype of collagen that can be a physical barrier for cell migration is nonfibrillar type IV collagen. Type IV collagen is a major component of thebasement membrane of epithelial and endothelial cells, and it needs to be
degraded when epithelial cancer cells grow or invade. Therefore, controlling
abnormal collagen metabolism would lead to the discovery of therapeutics
for the diseases. In this section, collagen metabolism and the disorders
related to abnormal collagen metabolism will be discussed.
Keywords: collagen, collagenase, fibrosis, tissue damage, cell invasion

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Chapter 10. Synthetic Collagen
Kazuki C. KURODA, KOIDE Takaki (Department of Chemistry andBiochemistry, School of Advanced Science and Engineering, Waseda
University)
In this review, we describe design, synthesis, and applications of synthetic
collagens. The so-called synthetic collagens include collagen-mimetic
peptides (CMPs) and collagen-like polymeric or supramolecular materials.
CMPs are soluble mimics for small parts of natural collagen triple helices.
CMPs are generally prepared chemically, and they are utilized in structuraland biochemical studies on collagen. In the molecular design of CMPs,
providing enough thermal stability to the triple helix is particularly
important, and many concepts have been tested for the purpose. The use of
appropriately designed CMPs has enabled easy access to the essence ofcollagen, avoiding difficulty in handling of insoluble and multifaceted
natural collagen with huge molecular size. Polymeric or supramolecularmaterials based on CMP are promising biomaterials for both in vitro and invivo applications. They are free from contamination of zoonotic pathogens.
The synthetic collagen-like materials are not only the surrogates for natural
collagen, but also used as artificial extracellular matrices with tunablephysical properties and physiological activities.
Keywords: collagen-mimetic peptide (CMP), molecularsupramolecular material, artificial extracellular material

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design,Chapter 11. Digestion and Absorption of Collagen and Its Derivatives
SATO Kenji (Marine Biological Function, Division of Applied Biosciences,
Graduate School of Agriculture, Kyoto University)
SHIGEMURA Yasutaka (Department of Food & Nutritional Science Tokyo
Kasei University)
There was limited information on structure and quantity of food-derived
collagen peptides in human blood before 2000. In the last two decades, morethan 15 collagen di- and tri-peptides have been demonstrated to increase in
human peripheral blood after ingestion of gelatin, a denature form ofcollagen, and its enzymatic hydrolysate, namely collagen peptide. Amongthe food-derived collagen peptides in human blood, Pro-Hyp and Hyp-Gly
are main constituents. Period of ingestion of collagen peptides andmolecular weight of collagen peptide for ingestion affect the ratio of ProHyp and Hyp-Gly in human blood. Part of collagen dipeptides is converted
to cyclic di-peptide, diketopiperazine, in human body possibly via enzymatic
reaction. While Pro-Hyp and Hyp-Gly resist to exo peptidases in blood, ProHyp can be cleaved in the tissue under inflammation, indicating somespecific peptidase are induced at inflammatory tissue. Majority of collagendipeptides are excreted into urine. However, part of Pro-Hyp has been
demonstrated to be incorporated into some cells and further metabolized.
In the primary cultured mouse skin fibroblasts, Pro-Hyp is specificallyincorporated into the fibroblasts expressing mesenchymal stem cell marker,
p75NTR, which triggers growth of the fibroblasts attached on collagen
fibrils. While target molecule of Pro-Hyp or its metabolites in the cellremains to be elucidated, the food-derived Pro-Hyp and related compounds
in cells might be responsible for the beneficial activities upon the ingestionof gelatin and collagen peptide.
Keywords: collagen peptide, Pro-Hyp, Hyp-Gly, diketopiperazine, fibroblast

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Chapter 12. Mammalian Collagen
TANAKA Keisuke, HATTORI Shunji (Nippi Research Institute of
Biomatrix)
Collagen is the major protein of the extracellular matrix and is the mostabundant protein found in mammals, comprising approximately 30% of thetotal protein. At present, 28 types of collagen have been identified, andtypes I, II, and III are the main types of collagen found in connective tissue.
Collagen exists in mammalian body as bundles called collagen fibers, andhas great tensile strength to maintain the architecture of skin, bone,cartilage, tendon and others. In addition to supporting most tissues,collagen plays a large part in cellular activity through interactions withreceptors on the surfaces of cells. Collagen can be extracted and purified
from a variety of sources such as species and tissues for many applications
in food, cosmetic, pharmaceutical and medical industries. Mammaliancollagen (e.g., bovine and porcine collagen) shows high sequence homology
to human collagen, and has similar properties to human collagen in termsof its thermal stability and ability of self-assembly into fibrils in vitro. In
addition to these advantages, it offers low immunogenicity, good
biocompatibility and moderate biodegradability as a biomaterial.
Therefore, mammalian collagen can be suitable for medical use.
Keywords: mammal, structural protein, cell function, thermal stability, selfassembly

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Chapter 13. Fish and Shellfish Collagen
ISHIHARA Kenji (National Research Institute of Fisheries Science, Fisheries Researchand Education Agency of Japan)
HIRAOKA Yoshinobu (Ehime Institute of Invention)
Fish are divided into cyclostomes, cartilaginous fish, and teleosts, all of which havetype I collagen as their main collagen. Their collagen molecules are mainly of (α1) 2α2
type, but some teleosts have species with α1α2α3 molecular species. Unlike livestock
animals, fish are poikilothermal animals, so the denaturation temperature of theircollagen is generally lower than that of livestock-derived collagen. Denaturation
temperature is related to the hydroxyproline content in the collagen molecule. Collagenis related to the quality of raw fish meat. A correlation is observed between the collagencontent in muscle and the hardness of sashimi. Invertebrate collagen has also beenshown to be related to meat water retention and breaking strength. The cnidarianjellyfish are mostly made of collagen, except for water and ash. Echizen jellyfish is alarge jellyfish that come to the coast of the Sea of Japan and cause great damage to thefishery. When powder containing mainly collagen was prepared from Echizen jellyfish
and administered to rats, the possibility of promoting lipid metabolism was observed.
We also introduced a technique for extracting collagen from the backbones of large fish
such as cultured yellowtail and skipjack as a collagen raw material. We prepared apeptide with enhanced ACE inhibitory activity using an enzyme. The prepared peptide
showed hypotensive activity on spontaneously hypertensive rats and contained a novel
peptide having ACE inhibitory activity.
Keywords: fish, invertebrate, denaturation temperature, ACE inhibitory activity

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Chapter 14. Lower animal Collagen
Katsuhiko Arai (Scleroprotein and Leather Research Institute, Faculty of Agriculture,
Tokyo University of Agriculture and Technology)
As known for connective tissue or extracellular matrix, the original function of collagenmolecule is a filler material of the intercellular space and the adhesive bond to tie cells
together. A kind of collagen molecule appeared when unicellular organism evolved intoa certain multicellular animal, thus collagen-like protein is found even in the lowest
animal, a genus of Porifera.
In this section, characteristics of collagen molecules found in the cnidarian belonging
to the diploblastic animals in addition to a family of lower triploblastic animals
including the mollusks (shell, squid and octopus), the arthropod (shrimp and insect)
and the echinoderm (sea cucumber, sea urchin and starfish) will be introduced.
Keywords: Embryo-like animal, Sponge phylum, Porifera, Mollusk,
Arthropod, Echinodermata

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Chapter 15. Application of Collagen, Overview
NOMURA Yoshihiro (Scleroprotein and Leather Research Institute,
Faculty of Agriculture, Tokyo University of Agriculture and Technology)
Collagen, gelatin, glue and hydrolyzed collagen are used as functional
materials. Collagen prepared as a by-product of meat products has a long
history and is closely related to our lives. This chapter outlines collagen as
a functional material.
Keywords: by-product, functional material

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Chapter 16. Leather and Leather Goods
YOSHIMURA Keiji (Japan Leather and Leather Goods Industries
Association)
Leather has been the most used in considering the use of collagen. The
leather derived as a by-product of meat production is processed into leather.
The production volume in 2015 was 22.27 billion m2, which is used for
footwear, automobiles, clothing, furniture and gloves. This chapter
describes the history of leather and the leather manufacturing process.
Keywords: leather, by-product, history of leather, leather manufacturing
process

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Chapter 17. Animal Glue and Industrial Gelatin
DOI Masahiro (Asahi Gelatine Industrial Co., Ltd)In Japan, glue is divided into Japanese glue and Western glue (gelatin).
Japanese glue is a product obtained by degreasing and dehairing the skinunder relatively mild conditions filtering the solution extracted with warm
water and drying. On the other hand, Western glue is a purified gelatinfrom which impurities have been removed, and is produced in large
quantities with the use of bovine bone and hide as a raw material for fixing
silver for photography. Animal glue has higher viscosity and adhesiveness.
In this chapter, the history and characteristics of the use of animal glue andindustrial gelatin are explained.
Keywords: animal glue, industrial gelatin, viscosity, adhesiveness

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Chapter 18. Inkstick and Classical Animal GlueUDAKA Kentaro (Independent Administrative Institution National
Institutes for Cultural Heritage, Tokyo National Research Institute forCultural Properties)
Inkstick (sumi/ 墨) is a traditional material that has been widely used for
paintings and calligraphies in East Asia throughout the ages. It is acomposite material mainly of soot and animal glue. Soot is a pigment thatis basically hydrophobic, and can be dispersed in water by the function ofanimal glue. Depending on these raw materials and the blending conditions,the properties of inksticks vary.
For traditional East Asian paintings, there are various techniques thatutilize the interaction of inkstick, water, and the base. Different properties
of inkstick affect the appearances of the works.
Soot is mainly composed of carbon. The properties of soot, such as color,
texture, diameter of primary particles, aggregate and agglomerate size, andamount and types of surface functional groups, depend on the raw materials
and production conditions.
Animal glue is composed mainly of gelatin, and contains a small amount of
fat and ash. Gelatin is a polymer formed from several hundreds of aminoacid residues, and is an amphoteric surfactant and an adhesive. Molecularweight, components, and physicochemical properties of animal glue dependon the raw materials and production conditions. In addition, reflecting them,applicability and interaction with other materials are also diverse. Animalglue is classified into industrial animal glue (洋膠), domestic animal glue(和膠), and classical animal glue (古典的膠).
Inkstick is a complex research subject involving diverse materials andtechnologies. In recent years, systematization of these elements has
advanced, and the research results are being used in various applications.
Keywords: inkstick, soot, animal glue, cultural properties, dispersion

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Chapter 19. Foods Using Collagen
SUZUKI Satoshi (Nippi, incorporated Fuji Factory)
Collagen has been consumed in a variety of forms. This chapter describes features andexamples of foods in which collagen, gelatin and collagen peptides are utilized. Ediblefilms have the properties of collagen. Sausage casings and water-soluble gelatin films
make up the majority and are in much demand. Collagen used in cooking is mainly
based on the gel properties of heat-modified gelatin and is widely used at home and inrestaurants, for example, in appetizers and jellies. Gelatin has also developed in Europe
as an ingredient in confectionery and desserts. In confectionery making, the physicalcharacteristics of gelatin, such as its high foaming properties and ease of gelation, areused. Very recently, new applications of collagen, especially in Japan, have been used
to maintain the shape of prepared foods in convenience stores and other applications,based on the advanced distribution system. It is also expected to be in demand for foodfor elderly people. Collagen peptides are soluble in cold water, and their demand is
growing for use in beverages and other applications due to their low viscosity and nongelling properties. Among the applications where its chemical properties are exploited
are in microcapsules and for removing turbidity in the sake and wine manufacturing
process. Collagen is also used as a specific amino acid source and seasoning due to its
characteristic amino acid composition. Thus, collagen has been in the diet for a longtime, and its properties, nutritional characteristics and composition have been studied
for a long time. Even today, the various physicochemical properties of collagen, which
are irreplaceable, are still in wide demand as a high-value food material.
Keywords: edible films, seasoning, sausage casing, gelatin, collagen peptide

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Chaper 20. Functional Food
KOIZUMI Seiko, MATSUSHITA Aya, DAIMON Mona, HIMENO Ai(Research and Development Center, Nitta Gelatin Inc.)
Collagen, gelatin or collagen peptide (Collagen Hydrolysate, CH) are used in cosmetics, general
foods and health foods, etc. depending on their physical properties. These materials are eaten sinceancient times and have been confirmed to be safe. Among them, an extensive range of functionality
by CH has been reported in many clinical trials. Thus, it has been widely used in “Foods with
Function Claims system” since 2015. We would introduce the absorption and metabolism of CH,
and function of CH to skin, knee joints, bone, muscle, blood vessels, diabetes, cognitive health, andimmunity reported in clinical trials.

Keywords: absorption, metabolism, skin aging, osteoarthritis, osteoporosis

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Chaper 21. Collagen in the Cosmetic Field
AMANO Satoshi (Shiseido Global Innovation Center)In the cosmetics field, collagen is blended in cosmetics and positioned as amaterial used as a component that enhances the moisturizing effect, andalso has the aspect of being an indispensable biopolymer that exists andfunctions in the skin. In the skin, various types of collagens exist in theepidermis, basement membrane, dermis, and subcutaneous tissue, andwork to keep the skin in good condition. However, this collagen also changes
due to aging and ultraviolet rays, and causes aging changes such as
wrinkles and sagging. Keeping the skin in good condition is one of theimportant roles of basic skin care. Aging is an important research target in
the cosmetics research, and as a result of aging, the internal structure of
the skin and its components changes. It is important to propose a practicalskin care method by finding out what mechanism and how to control theaging process. In this chapter, while briefly touching on the collagen as amaterial and the functional component evaluation system related tocollagen, the main contents are the elucidation of the mechanism of damage
to the epidermis basement membrane during skin aging process using
three-dimensional cultured skin models and human skins and its
development to a skin care method. Moreover, the damage mechanism of
the dermis and the research on its care method were described.
Keywords: basement membrane, dermis, three-dimensional cultured skinmodels24/25

Chaper 22. Characteristics and Applications of Medical Collagen Products
FUJIMOTO Ichiro (Koken Research Center, Koken Co., Ltd.)Collagen has many possibilities as a medical device by taking advantage of
its advantages as a biological material. It can be molded into a variety ofshapes, its biocompatibility, safety, biodegradable is evaluated manycollagen medical devices are manufactured and used in the medical field.
In particular, atelocollagen was removed telo-peptide region by enzymatic
treatment seems to be a useful material as a medical application
antigenicity is suppressed.
Currently, medical collagen products used in Japan are products registeredand managed as medical devices of highly controlled medical devices. As
medical applications for regenerative medicine, skin tissue, periodontal
tissue, neural tissue, cartilage tissue, bone tissue, are used in. Other clinicalapplications, surgical hemostasis, improvement of dry eye, plastic surgery
area, have also spread.
In this chapter, technical information such as the situation of medical
collagen in general, and relationship with collagen characteristics areincluded, and the description of medical equipment and the contents of theclassification are introduced. In the second half, we introduce regenerative
medicine products that use autologous cells or allogenic cells that arerecently newly applied in medical applications in combination with collagenand finally explain the possibilities for medical applications of humancollagen.
Keywords: medical collagen, medical equipment, Japan Pharmaceuticaland Medical Device Act (PMDA), regenerative medicine, biocompatibility

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