The growing interest in valorizing industrial by-products has led researchers to focus on exploring different sources and optimizing collagen extraction conditions over the past decade.While bovine hide,cattle bones,p...The growing interest in valorizing industrial by-products has led researchers to focus on exploring different sources and optimizing collagen extraction conditions over the past decade.While bovine hide,cattle bones,pork,and pig skins remain the most abundant collagen sources,there is a growing trend in the industrial utilization of collagen from non-mammalian species.This review explores alternative marine collagen sourcesand summarizes emerging trends in collagen recovery from marine sources,with a particular focus on environmentally friendly methods.Additionally,this review covers the colloidal structure-forming properties of marine collagens,including foam,film,gel,and emulsion formation.It also highlights the potential and important applications of marine collagen in various food products.Based on the currently reported marine sources,collagens extracted from fish,jellyfish,and sea cucumbers were found to have the highest yield and mostly comprised type-l collagen,while crustaceans and mollusks yielded lower percentages of collagen.Traditional extraction techniques isolate collagen based on acetic acid and pepsin treatment,but they come with drawbacks such as being time-consuming,causing sample destruction,and using solvents.Conversely,marine collagen extracted using conventional methods assisted with ultrasonication resulted in higher yields and strengthened the triple-stranded helical structures.Recently,an increasing number of new applications have been found in the food industry for marine collagens,such as biodegradable film-forming materials,colloid stabilizers,foaming agents,and micro-encapsulating agents.Furthermore,collagen is a modern foodstuff and is extensively used in the beverage,dairy,and meat industries to increase the stability,consistency,and elasticity of products.展开更多
Lactoferricin,a multifunctional peptide located in the N-terminal region of lactoferrin,has a broad-spectrum bacteriostatic activity.It is a promising candidate as a food additive and immune fortification agent and do...Lactoferricin,a multifunctional peptide located in the N-terminal region of lactoferrin,has a broad-spectrum bacteriostatic activity.It is a promising candidate as a food additive and immune fortification agent and does not have the risks associated with drug residues and drug resistance.First,we performed promoter and host cell screening to achieve the recombinant expression of lactoferricin in Pichia pastoris,showing an initial titer of 19.5 mg/L in P.pastoris X-33 using PAOX1 promoter.Second,we constructed a 0030-α hybrid signal peptide by fusing the 0030 signal peptide with the pro-sequence of α-factor secretory signal peptide.This further increased the production of lactoferricin,with a titer of 28.8 mg/L in the fermentation supernatant in the shaking flask.Next,we increased the expression of lactoferricin by fusing it with anionic antioxidant peptides.The neutralization of positive charges yielded a titer of 55.3 mg/L in the shaking flask,and a highest titer of 193.9 mg/L in a 3-L bioreactor.The antimicrobial activity analysis showed that recombinant-expressed lactoferricin exhibited potent antibacterial activity against Escherichia coli,Bacillus subtilis,and Staphylococcus aureus.This study provides a reference for the construction of microbial cell factories capable of efficiently synthesizing antimicrobial peptides.展开更多
基金funded by the"Pioneer"and"Leading Goose"R&D Program of Zhejiang Province(2023C02044).
文摘The growing interest in valorizing industrial by-products has led researchers to focus on exploring different sources and optimizing collagen extraction conditions over the past decade.While bovine hide,cattle bones,pork,and pig skins remain the most abundant collagen sources,there is a growing trend in the industrial utilization of collagen from non-mammalian species.This review explores alternative marine collagen sourcesand summarizes emerging trends in collagen recovery from marine sources,with a particular focus on environmentally friendly methods.Additionally,this review covers the colloidal structure-forming properties of marine collagens,including foam,film,gel,and emulsion formation.It also highlights the potential and important applications of marine collagen in various food products.Based on the currently reported marine sources,collagens extracted from fish,jellyfish,and sea cucumbers were found to have the highest yield and mostly comprised type-l collagen,while crustaceans and mollusks yielded lower percentages of collagen.Traditional extraction techniques isolate collagen based on acetic acid and pepsin treatment,but they come with drawbacks such as being time-consuming,causing sample destruction,and using solvents.Conversely,marine collagen extracted using conventional methods assisted with ultrasonication resulted in higher yields and strengthened the triple-stranded helical structures.Recently,an increasing number of new applications have been found in the food industry for marine collagens,such as biodegradable film-forming materials,colloid stabilizers,foaming agents,and micro-encapsulating agents.Furthermore,collagen is a modern foodstuff and is extensively used in the beverage,dairy,and meat industries to increase the stability,consistency,and elasticity of products.
基金supported by the National Natural Science Foundation of China(32021005,32270096)the Fundamental Research Funds for the Central Universities(JUSRP222007,JUSRP622004).
文摘Lactoferricin,a multifunctional peptide located in the N-terminal region of lactoferrin,has a broad-spectrum bacteriostatic activity.It is a promising candidate as a food additive and immune fortification agent and does not have the risks associated with drug residues and drug resistance.First,we performed promoter and host cell screening to achieve the recombinant expression of lactoferricin in Pichia pastoris,showing an initial titer of 19.5 mg/L in P.pastoris X-33 using PAOX1 promoter.Second,we constructed a 0030-α hybrid signal peptide by fusing the 0030 signal peptide with the pro-sequence of α-factor secretory signal peptide.This further increased the production of lactoferricin,with a titer of 28.8 mg/L in the fermentation supernatant in the shaking flask.Next,we increased the expression of lactoferricin by fusing it with anionic antioxidant peptides.The neutralization of positive charges yielded a titer of 55.3 mg/L in the shaking flask,and a highest titer of 193.9 mg/L in a 3-L bioreactor.The antimicrobial activity analysis showed that recombinant-expressed lactoferricin exhibited potent antibacterial activity against Escherichia coli,Bacillus subtilis,and Staphylococcus aureus.This study provides a reference for the construction of microbial cell factories capable of efficiently synthesizing antimicrobial peptides.
