Hu Hou

Effects of Collagen and Collagen Hydrolysate from Jellyfish (Rhopilema esculentum) on Mice Skin Photoaging Induced by UV Irradiation

Collagen (JC) was extracted from jellyfish (Rhopilema esculentum) and hydrolyzed to prepare collagen hydrolysate (JCH). The protective effects of JC and JCH against UV-induced damages to mice skin were evaluated and compared in this article. JC and JCH could alleviate the UV-induced abnormal changes of antioxidative indicators, including the superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and catalase (CAT) activities and the contents of glutathione (GSH) and malondiaidehyde (MDA). JC and JCH could protect skin lipid and collagen from the UV radiation damages. Furthermore, the changes of total ceramide and glycosaminoglycan in skin were recovered significantly by JC and JCH. The action mechanisms mainly involved the antioxidative properties and the repairing to endogenous collagen synthesis of JC and JCH in vivo. JCH with the lower molecular weight showed much higher effects than JC. The results indicated that JCH was a novel antiphotoaging agent from natural resources.

Moisture absorption and retention properties, and activity in alleviating skin photodamage of collagen polypeptide from marine fish skin

Collagen polypeptides were prepared from cod skin. Moisture absorption and retention properties of collagen polypeptides were determined at different relative humidities. In addition, the protective effects of collagen polypeptide against UV-induced damage to mouse skin were evaluated. Collagen polypeptides had good moisture absorption and retention properties and could alleviate the damage induced by UV radiation. The action mechanisms of collagen polypeptide mainly involved enhancing immunity, reducing the loss of moisture and lipid, promoting anti-oxidative properties, inhibiting the increase of glycosaminoglycans, repairing the endogenous collagen and elastin protein fibres, and maintaining the ratio of type III to type I collagen.

Purification and identification of immunomodulating peptides from enzymatic hydrolysates of Alaska pollock frame

To prepare immunomodulating peptides from Alaska pollock frame (APF) hydrolysates, trypsin was employed for enzymatic hydrolysis, and the immunomodulating activities of the hydrolysates were studied using splenic lymphocytes proliferation assay. The highest activity of the hydrolysates was reached when DH ranged from 15% to 18%. The peptide fractions which exhibited the highest activity were further purified using ion exchange chromatography, gel filtration chromatography, and RP-HPLC. The peptides were identified using nano-LC-ESI mass spectrometry. Finally, three immunomodulating peptides were obtained, and the amino acid sequences were Asn-Gly-Met-Thr-Tyr, Asn-Gly-Leu-Ala-Pro, and Trp-Thr, respectively. The lymphocyte proliferation rates were 35.92%, 32.96%, and 31.35% in the presence of 20 μg/ml purified peptides, respectively. Therefore, the results demonstrated that the APF proteins hydrolysates prepared by trypsin could serve as a source of peptides with immunomodulating activity. It provided a scientific basis for the preparation of immunomodulating peptides.

Fractionation and identification of Alaska pollock skin collagen-derived mineral chelating peptides

Peptides with the ability to chelate dietary minerals have been reported to have potential as functional food ingredients. A collagen tryptic hydrolysate (CTH), previously shown to chelate iron, was further investigated for the presence of Ca, Fe and Cu chelating peptides. Sequential purification steps, including immobilised metal affinity chromatography (IMAC) and gel permeation chromatography (GPC) were employed for the separation of chelating peptides. GPC analysis showed that the mineral chelating peptides were mainly between 500 and 2000 Da. Subsequent identification was carried out using UPLC-ESI-QTOF MS/MS. Overall, 10 sequences were identified as potential chelating peptides. The Ca, Fe and Cu chelating activity of GPAGPHGPPG was 11.52±2.23 nmol/μmol, 1.71±0.17 nmol/μmol and 0.43±0.02 μmol/μmol, respectively. This study identifies collagen as a good source of peptides with potential applications as functional ingredients in the management of mineral deficiencies.

In vitro assessment of the multifunctional bioactive potential of Alaska pollock skin collagen following simulated gastrointestinal digestion

BACKGROUND Dietary mineral deficiency, hypertension and diabetes have become serious human health problems. Dietary approaches are increasingly being investigated to address these issues. Identification of food-derived biological peptides has become an important approach to control such diseases. Peptides generated from aquatic byproducts have been shown to possess biological activities. RESULTS Significantly higher copper-chelating activity was observed on simulated hydrolysis of intact collagen. The collagen hydrolysate generated in the gastric stage exhibited moderate angiotensin-converting enzyme (ACE)-inhibitory activity with an IC50 value of 2.92 ± 0.22 mg mL(-1), which significantly decreased to 0.49 ± 0.02 mg mL(-1) after intestinal digestion. The dipeptidyl peptidase (DPP) IV-inhibitory potency of the collagen hydrolysate generated directly following simulated gastrointestinal digestion (SGID) (IC50 2.59 ± 0.04 mg mL(-1)) was significantly lower than that of the collagen tryptic hydrolysate (CTH) (IC50 1.53 ± 0.01 mg mL(-1)). The antioxidant activities of collagen and CTH using the ferric-reducing antioxidant power (FRAP) assay were 0.87 ± 0.10 and 1.27 ± 0.03 µmol Trolox equivalent (TE) g(-1) respectively after SGID. CONCLUSION This study identifies collagen as a good and inexpensive substrate for the generation of biologically active peptides with potential applications as functional ingredients in the management of chronic illness and mineral deficiency problems.

Preparation of immunomodulatory hydrolysates from Alaska pollock frame

BACKGROUND Immunomodulatory peptides can enhance body immunity. There have been few systematic investigations on preparing immunomodulatory peptides from Alaska pollock frame. The aim of this study was to obtain such peptides from Alaska pollock frame and determine their properties. RESULTS Trypsin protein hydrolysate (TPH) significantly enhanced the proliferation of spleen lymphocytes, T cells and peritoneal macrophages (P < 0.05). Compared with TPH with molecular weight (MW) > 2 kDa, TPH with MW < 2 kDa showed higher lymphocyte proliferation activity at 10, 50 and 500 µg ml(-1). The optimised hydrolysis conditions were a temperature of 50 °C, an enzyme dose of 24 U mg(-1) and a time of 290 min. The proliferation rate and degree of hydrolysis were 28.45 ± 1.79% and 16.87 ± 0.15% respectively. The main amino acids in TPH were proline, aspartate, glutamic acid and leucine. TPH had high solubility and low viscosity. TPH showed high stability under both acid and alkaline conditions or when digested by trypsin and/or pepsin. CONCLUSION TPH showed high immunomodulatory activity, with molecular weight and amino acid composition being the important factors affecting this activity. TPH had high solubility, low viscosity and high stability. As a good immunomodulator, TPH may therefore have wide application.

Characterization of acid- and pepsin-soluble collagen extracted from the skin of Nile tilapia (Oreochromis niloticus)

Acid-soluble (ASC) and pepsin-soluble (PSC) collagen were extracted from the skin of Nile tilapia (Oreochromis niloticus), purified and physicochemically examined. Amino acid content analyses revealed that glycine accounted for approximately one-third of the total amino acid residues. The proline and hydroxyproline contents of Nile tilapia ASC and PSC were 189 residues and 205 residues/1000 residues, respectively, and the rate of proline hydroxylation was found to be 41.8% and 42.0%, respectively. Denaturation temperatures (Td), as measured by an Ubbelohde viscometer, were 35.2°C and 34.5°C, respectively, 6°C lower than that of the type I collagen found in calf skin. In this study, we measured the intrinsic viscosity, circular dichroism (CD) and, X-ray diffraction (XRD), and employed Fourier transform infrared spectroscopy (FTIR) analyses to confirm that the ASC and PSC samples from Nile tilapia skin were native and undenatured, and therefore, maintained their original, intact triple helical structure. Our SDS-PAGE results showed that the extracted ASC and PSC peptides were in their native molecular form; (α1)2α2 (type I collagen). Furthermore, the loose, fibrous, and porous structures, shown in the cross-sections of ASC and PSC, indicate that Nile tilapia skin collagen represents a powerful physical foundation for further use in biomaterial applications.

Effect of calcium-binding peptide from Pacific cod (Gadus macrocephalus) bone on calcium bioavailability in rats

Bone collagen peptide with high affinity to Ca was extracted from Pacific cod (Gadus macrocephalus) bone. FTIR spectra of calcium-binding bone collagen peptide showed that band at 3381cm-1 shifted to 3361cm-1, 1455cm-1 moved to 1411cm-1, and amide II became deeper valley, compared with that of bone collagen peptide. This peptide was sequenced by Q-TOF-MS and sequences of Gly-Pro-Glu-Gly, Gly-Glu-Lys, Gly-Pro-Leu-Gly and Gly-Leu-Pro-Gly appeared repeatedly in some peptides. From SEM, after chelated with calcium, the loose and porous structure turned into granular structure. From the animal experiment, Ca apparent absorption rate, Ca retention rate and femur Ca content of calcium-binding bone collagen peptide group were significantly higher than those of model and CaCO3 groups (P<0.05), while serum ALP was significantly lower than model group (P<0.05) and similar to control group. The results suggested that calcium-binding bone collagen peptide could improve bioavailability of Ca and thus prevented Ca deficiency.

Protective effect of gelatin peptides from pacific cod skin against photoaging by inhibiting the expression of MMPs via MAPK signaling pathway

Chronic exposure to ultraviolet (UV) irradiation causes skin photoaging. This study was undertaken to identify the anti-photoaging mechanisms of gelatin hydrolysate (CH) derived from pacific cod skin. Quantitative real-time reverse transcription-polymerase chain reaction (qRT-PCR) and ELISA assays were used to investigate the effects of CH on matrix metalloproteinases (MMPs) and the signaling pathways after UV irradiation by using a mice skin photoaging model. The average molecular weight of CH was 1200Da, and 273/1000 residues were hydrophobic, Gly-Pro and Gly-Leu sequences and Arg at C-terminus appeared frequently in CH. CH improved pathological changes of collagen fibers and significantly inhibited collagen content reduction in photoaging skin. Moreover, CH blocked the up-regulated expression of interstitial collagenase (MMP-1), stromelysin 1 (MMP-3), and gelatinase (MMP-9) in photoaging skin. Besides, CH suppressed the activities of MMPs by increasing the contents of tissue inhibitors of matrix metalloproteinases (TIMPs). CH significantly reduced the UV irradiation-dependent up-regulated phosphorylation of ERK and p38 in the mitogen-activated protein kinase (MAPK) signaling pathway. Furthermore, it inhibited the activation of activator protein 1 (AP-1) by down-regulating the mRNA level of c-Jun and c-Fos, which are the two transcription factors responsible for the regulation of MMPs expression. CH can effectively protect against UV irradiation-induced skin photoaging by inhibiting the expression and the activity of MMPs.

Protective effect of gelatin and gelatin hydrolysate from salmon skin on UV irradiation-induced photoaging of mice skin

The objective of this study was to investigate the effect of gelatin (SG) isolated from salmon skin and its hydrolysate (SGH) on photoaging skin, and the mechanism responsible for anti-photoaging. The average molecular weights of SG and SGH were 65 kDa and 873 Da, respectively. The amino acid compositions of SG and SGH were similar. Both of them were abundant in hydrophobic amino acids. Twenty-five peptides were identified from SGH. SG and SGH could improve UV irradiation-induced pathological changes of macroscopical tissue texture and skin morphology. Hydroxyproline content is an indicator of matrix collagen content, SG and SGH could inhibit the decrease of hydroxyproline content in photoaging skin in a dose dependent manner. In addition, SG and SGH could alleviate UV irradiation-induced oxidative damages to skin by increasing the activities of total superoxide dismutase (T-SOD), glutathione peroxidase (GSH-Px) and catalase (CAT), increasing the content of glutathione (GSH) and decreasing the content of malonaldehyde (MDA). Moreover, SG and SGH could enhance immune regulation system by increasing the thymus index. Thus, the anti-photoaging mechanisms of SG and SGH were by inhibiting the depletion of antioxidant defense components, involving in the synthesis of collagen and enhancing the function of immune system. Besides, SGH showed a better result in protecting skin from photoaging than SG.