Preparation,characterization and antioxidant activity analysis of three Maillard glycosylated bone collagen hydrolysates from chicken,porcine and bovine

Bone collagen hydrolysates(peptides)derived from byproduct of animal product processing have been used to produce commercially valuable products due to their potential antioxidant activity.Maillard glycosylated reaction is considered as a promising method to enhance the antioxidant activity of peptides.Hence,this research aims at investigating the Maillard glycosylation activity and antioxidant activity of bone collagen hydrolysates from different sources.In this study,3 glycosylated bone collagen hydrolysates were prepared and characterized,and cytotoxicity and antioxidant activity were analyzed and evaluated.The free amino groups loss,browning intensity,and fluorescence intensity of G-Cbcp(glycosylated chicken bone collagen hydrolysates(peptides))were the heaviest,followed by G-Pbcp(glycosylated porcine bone collagen hydrolysates(peptides))and G-Bbcp(glycosylated bovine bone collagen hydrolysates(peptides)).The results of amino acid analysis showed that amino acid composition of different bone collagen hydrolysates was significantly different and the amino acid decreased to different degrees after Maillard glycosylated reaction,which may lead to differences in Maillard glycosylated reaction activity.Furthermore,the 3 glycosylated hydrolysates showed no significant cytotoxicity.The results showed that glycosylation process significantly increased the antioxidant activity of bone collagen hydrolysates,and G-Cbcp showed the strongest antioxidant activity,followed by G-Pbcp and G-Bbcp.Therefore,compared with the bone collagen hydrolysates,3 glycosylated hydrolysates showed significant characteristic and structural changes,and higher antioxidant activity.

Analysis of Molecular Weight Distribution and Antioxidant Activities of Cirrhinus molitorella Skin Collagen Hydrolysates

[Objective] The aim of this work was to identify molecular weight （MW） distribution and antioxidant activity of fish skin col agen hydrolysates. [Method] The MW distribution of hydrolysates was determined using both size exclusion chromatography and matrix-assisted laser desorption ionization time-of-flight mass spec-trometry （MALDI-TOF-MS）. Fish skin were treated by the alkaline protease 2709. [Result] The optional conditions for hyerolysis were time 3 h, temperature 55 ℃, pH 10.0, substrate concentration 80 g/L and E/S 4%. The results of both methods indi-cated that the molecular weight of col agen hydrolysates was from 400 to 1 800 Da, and the peptides’ molecular weight was less than 1 400 Da mostly. The reducing power and antioxidant/radical scavenging activity [1, 1-diphenyl-2-picryl-hydrazyl （DPPH） free radical scavenging activity] were determined. [Conclusion] The results reveal that the fishskin hydrolysate is a potential source of antioxidants.

Developments for collagen hydrolysates as a multifunctional antioxidant in biomedical domains

Antioxidant collagen hydrolysates refers to the peptides mixture with antioxidant properties identified from hydrolyzed collagen.Due to its specific structural,biological and physicochemical properties,collagen hydrolysates have been explored as a multifunctional antioxidant in the biomedical field.In this review,we summarize recent advances in antioxidant collagen hydrolysates development.Initially,the preparation process of antioxidant collagen hydrolysates is introduced,including the production and separation methods.Then the effects and the mechanisms of amino acid composition and collagen peptide structure on the antioxidant activity of collagen hydrolysates are reviewed.Finally,the applications of antioxidant collagen hydrolysates in biomedical domains are summarized,with critical discussions about the advantages,current limitations and challenges to be resolved in the future.

Study on Enzymatic Hydrolysis of Gadus morrhua Skin Collagen and Molecular Weight Distribution of Hydrolysates

Process parameters on enzymatic hydrolysis and molecular weight （MW） distribution of collagen hydrolysates from Gadus morrhua skin were investigated. The optimal process parameters were obtained by the single-factor and orthogonal experiments. The molecular weight distribution of hydrolysates was determined using both Sephadex G25 partition and high speed liquid chromatography electricity spray mass spectrum （HPLC-ESI-MS）. Collagen hydrolysates were first gained by an alkaline protease ＂alcalase＂ for 3 h at temperature （50~C）, pH （10.0）, substrate concentration （75 g L-~）, and E/S （3%）. The molecular weight distribution of collagen hydrolysates ranged from 300 to 1 500 Da, and most of peptides were under 1 200 Da. Sephadex G25 partition and HPLC-ESI-MS should be successfully employed to determine the molecular weight distribution of collagen hydrolysates.

Osteogenic peptides in collagen hydrolysates:Stimulate differentiation of MC3T3-E1 cells viaβ1 integrin-FAK-ERK1/2 signaling pathway and Smad1 protein

Our previous study demonstrated that orally administration of collagen hydrolysates from silver carp skin(SCH)could increase bone remodeling in chronologically aged mice.However,the active compounds and molecular mechanism were still unclear.In this study,SCH showed strong activity in promoting osteogenic differentiation of MC3T3-E1 cells and the active components in it were separated by ultrafiltration and YMC ODS-A C18 column.And then,a series of peptides containing potential osteogenic sequences were identified by LC-MS/MS and two novel peptides,GARGDKGETGEAGE(GE-14)and TGPRGPVGPA(TA-10),were synthesized for further investigation.The results indicated that peptides GE-14 and TA-10 could promote the differentiation and mineralization of MC3T3-E1 cells by positively regulatingβ1 integrin-FAK-ERK1/2 and Smad1 pathway,which might be due to the RGD or GPR sequences in them.These findings suggest that SCH has the potential to be developed as an effective diet supplement to prevent osteoporosis.

Toxicity evaluation of collagen hydrolysates from chrome shavings and their potential use in the preparation of amino acid fertilizer for crop growth

Resource utilization of chrome shavings(CS)has attracted a lot of attention from scientists and technologists in leather industry.Especially,the collagen hydrolysates extracted from CS are expected to find potential application values in agricultural field.However,there is no biotoxicity analysis of collagen hydrolysates from CS.Herein,the collagen hydrolysates with different molecular weights were produced from CS by three hydrolysis dechroming methods including alkaline hydrolysis,enzymatic hydrolysis and alkaline-enzymatic synergistic hydrolysis,and the optimal hydrolysis process of CS was designed and conducted.To evaluate their toxicity,the three collagen hydrolysates were formulated into a nutrient solution for zebrafish development.The obtained results indicated that the hydrolysates with low concentrations(less than 0.6 mg/mL)were safe and could promote the development for zebrafish embryos.Furthermore,the three collagen hydrolysates were utilized as organic nitrogen sources and formulated into amino acid water-soluble fertilizers(AAWSF)including alkaline type fertilizer(OH),enzymatic type fertilizer(M)and alkaline-enzymatic type fertilizer(OH-M)for the early soilless seeding cultivation of wheat,soybean and rapeseed.It is worth mentioning that the chromium contents in the prepared AAWSF were less than 10 mg/kg,which is far less than the limit value in the standard(China,50 mg/kg).The growth and development of seedlings(germination rate,plant height,fresh weight of leaves,soluble sugar content and chlorophyll content)were investigated.The corresponding results showed that the growth of seedlings watered with AAWSF was better compared with the other treatments,and the OH-M fertilizer had the best promoting effect on the seedlings growth and development,followed by the M and OH fertilizers.The safe toxicity assessment of the collagen hydrolysates will expand their application scope,and the use of collagen hydrolysates extracted from CS for seedlings growth also provides an effective and reason-able way to deal with the chromium-containing leather solid waste,which is an effective way to realize its resource utilization.

Supplementation with yak (Bos grunniens) bone collagen hydrolysate altered the structure of gut microbiota and elevated short-chain fatty acid production in mice

In this study, yak bone collagen hydrolysate(YBCH)was produced by mixed proteases and provided to standard-diet mice at a different dose(low dose(LD), medium dose(MD), and high dose(HD))to investigate its effects on the composition of gut microbiota and short-chain fatty acids(SCFA)production. It was found that YBCH was mainly composed of small molecular peptides whose molecular weight below 2 000 Da. Notably, supplementation with different doses of YBCH could significantly downregulate the ratio of Firmicutes to Bacteroidetes in the fecal microbiota. At the family level, the Lachnospiraceae abundance was significantly reduced in the YBCH gavage groups(mean reduction ratio 41.7 %, 35.2%, and 36.4% for LD, MD, and HD group, respectively). The predicted functions of gut microbes in the MD group were significantly increased at “lipid metabolism” and “glycan biosynthesis and metabolism”. Moreover, the SCFA production in the YBCH groups was elevated. Especially, the concentration of acetic acid, propionic acid, and butyric acid in the MD group was separately increased 79.7%, 89.2%, and 78.8% than that in the NC group. These results indicated that YBCH might be applied in the development of functional food for intestinal microecological regulation.