Extracting Conditions for Megrim (Lepidorhombus boscii) Skin Collagen Affect Functional Properties of the Resulting Gelatin

Various procedures for extracting collagen and/or gelatin from megrim skins were compared on the basis of gelatin functional properties. It was possible to prepare a dry powder of soluble collagen with good viscoelastic and gelling properties, which can be converted into gelatin by dissolving at temperatures above 45 °C. Physical properties of gelatins are influenced more by extracting conditions than by imino acid composition. A high-quality, readily-dissolved gelatin was obtained from megrim skins using a pretreatment of the skins with NaCl and dilute NaOH, then swelling with 0.05 M acetic acid followed by an extraction step in water at 45 °C.     

Bovidae-based gelatin: Extractions method,physicochemical and functional properties,applications, and future trends

Gelatin is one of the most important multifunctional biopolymers and is widely used as an essential ingredient in food, pharmaceutical, and cosmetics. Porcine gelatin is regarded as the leading source of gelatin globally then followed by bovine gelatin. Porcine sources are favored over other sources since they are less expensive. However, porcine gelatin is religiously prohibited to be consumed by Muslims and the Jewish community. It is predicted that the global demand for gelatin will increase significantly in the future. Therefore, a sustainable source of gelatin with efficient production and free of disease transmission must be developed. The highest quality of Bovidae-based gelatin (BG) was acquired through alkaline pretreatment, which displayed excellent physicochemical and rheological properties. The utilization of mammalian- and plant-based enzyme significantly increased the gelatin yield. The emulsifying and foaming properties of BG also showed good stability when incorporated into food and pharmaceutical products. Manipulation of extraction conditions has enabled the development of custom-made gelatin with desired properties. This review highlighted the various modifications of extraction and processing methods to improve the physicochemical and functional properties of Bovidae-based gelatin. An in-depth analysis of the crucial stage of collagen breakdown is also discussed, which involved acid, alkaline, and enzyme pretreatment, respectively. In addition, the unique characteristics and primary qualities of BG including protein content, amphoteric property, gel strength, emulsifying and viscosity properties, and foaming ability were presented. Finally, the applications and prospects of BG as the preferred gelatin source globally were outlined.     

胶原明胶化过程中分子结构的变化

本试验以猪皮胶原为原料,研究胶原明胶化过程微观结构的变化规律。研究表明,8 h的酸处理诱导下,胶原明胶化程度较高,热水提胶后明胶得率可达83.98%,随着酸处理时间进一步延长,明胶得率显著下降;差示量热扫描(DSC)、红外光谱(FTIR)和圆二色谱(CD)研究表明,随酸处理的进行,胶原的三螺旋结构逐渐松散,维系三螺旋结构稳定的价键逐渐被破坏,酸处理8 h后,胶原三螺旋结构被过度破坏,是导致明胶得率降低的主要原因。聚丙烯酰胺凝胶电泳(SDS-PAGE)分析显示,在酸处理的过程中,胶原肽链的降解始终存在,且明胶化胶原中所保留的亚基量直接影响明胶中亚基含量。因此,在明胶化过程中必须在肽链降解和三螺旋结构松散之间寻找平衡点,以获得高得率和高品质明胶。     

H_2O_2在鸡骨明胶提取中的应用

对明胶传统提取工艺进行改良,在骨素吸水膨胀阶段添加微量H2 O2 并直接加热提取明胶,结果表明,骨素中添加0 2 %的H2 O2 ,明胶的提取率提高近3倍,同时明胶的色泽浅,抗菌性好,但明胶的粘度与凝胶强度有所降低。改良的提取工艺极大地缩短了明胶生产时间,减少能耗。通过氨基酸和粘均分子质量的测定结果表明,由于H2 O2 对芳香族氨基酸的破坏,加速胶原链的断裂解聚,因而使明胶的提取率提高,明胶粘均分子质量略有下降。红外光谱显示,该法提取的明胶不存在螺旋结构。     

Effect of extracting time and temperature on yield of gelatin from different fish offal

The aim of the study was to determine the optimal conditions for preparing gelatin from different kinds of fish offal: heads and backbones of Baltic cod, skins of fresh and cold-smoked salmon, and skins of salted and marinated herrings. The yield of gelatin extraction at 45 °C was 71–75% for fresh salmon skins or cod backbones, and 86%, for smoked salmon skins. When heating marinated herring skins for 15 min or salted herring skins for 45 min, about 100% of collagen was converted to gelatin. For fish skins, 45 °C and 15–60 min extraction time, depending on the kind of skins, were established as optimal conditions for preparing gelatin. The yield of gelatin extraction from the cod heads did not exceed 70%, even when a three stages process was used. In the case of backbones, 100% of collagen in the form of gelatin was isolated using this procedure. SDS-PAGE analysis showed that gelatin from fish skins was much less degraded than gelatin from pigskins.     

安康鱼皮明胶的制备及性质研究

以安康鱼皮为原料,采用碱法(浸灰法)提取鱼皮明胶,通过正交试验法对安康鱼皮明胶的提取工艺进行优化,并分别对明胶黏度、色价、等电点、氨基酸组成进行了测定。结果表明,优选出鱼皮明胶最佳提取工艺为Ca(OH)2质量分数0.2%、料液比为1∶10、提取温度为10℃、浸灰时间7d,明胶的提取率为11.23%。     

鲢鱼皮明胶提取方法和谷氨酰胺转氨酶改性对明胶结构和膜性能的影响

研究鲢鱼皮明胶的酶法、酸法、热水法3种常用的工业提取方法对其凝胶强度、黏度以及膜性能指标的影响,在此基础上进一步使用谷氨酰胺转氨酶(transglutaminase,TG)改性以达到改善膜性能的效果。同时以市售猪皮明胶为对照,采用圆二色谱、红外光谱分析3种提取方法对明胶高级结构的影响;通过红外光谱、原子力显微镜分析了鲢鱼皮明胶TG改性前后明胶高级结构和表面结构变化。结果表明,3种提取方法中酶法明胶的比黏度和凝胶强度最大,成膜后的酶法明胶膜抗拉强度最大、断裂延伸率最大、水蒸气透过率最低。继续经过TG改性后,抗拉强度、断裂延伸率指标显著增加(P0.05),接近猪皮明胶膜,水蒸气透过率进一步降低。圆二色谱及红外光谱结果发现酶法明胶α-螺旋相对含量增加、无规卷曲相对含量减少,并可保留更多的分子内氢键。而TG改性后明胶分子内氨基转变为亚氨基,同时增强了肽链间相互作用。原子力显微镜图像分析结果证明,TG改性的明胶膜具有更为致密均匀的表面结构。明胶膜的机械强度与明胶结构中α-螺旋的含量呈正相关。因此,酶法提取并通过TG改性是一种提高可食性明胶膜性能的有效方法。     

Use of lactic acid for extraction of fish skin gelatin

The ability of lactic acid compared to acetic acid for Dover sole (Solea vulgaris) skin swelling and the subsequent gelatin extraction was examined. The resultant gelatins were evaluated in terms of extraction yield, amino acid composition, molecular weight distribution, gel strength, viscoelastic properties, ability to refold into triple helical structures, and aggregation phenomena. Lactic acid (25 mM) proved to be an excellent substitute for acetic acid during the skin swelling process, as the gelatin preparation thus obtained presented quite similar properties to that prepared by using 50 mM acetic acid without the negative organoleptic properties of this acid. However, the application of 50 mM lactic acid gave rise to a highly hydrolysed gelatin, with lower folding ability, gel strength and viscoelastic properties than those obtained using 25 mM lactic acid or 50 mM acetic acid.     

Physicochemical properties of gelatin gels from walleye pollock (Theragra chalcogramma) skin cross-linked by gallic acid and rutin

Gelatin gels were cross-linked by gallic acid and rutin. The gel strength, viscoelastic properties, thermal stability, swelling property, ultrastructure, X-ray diffraction patterns and FTIR spectra were determined to evaluate the physicochemical properties of the modified gels. The gel strength increased with increasing gallic acid concentration up to 20 mg/g dry gelatin, and then decreased at further elevated gallic acid concentration, while it continuously increased with increasing levels of rutin. Either cross-linking agent could enhance the elastic modulus (G′) and the viscous modulus (G″) of hydrogels, but the gelling and melting points didn’t show a notable improvement. Rutin boosted the thermal stability of xerogels, but decreased the equilibrium swelling ratio significantly, while as for gallic acid, there were no obvious effects on the thermal stability and equilibrium swelling ratio of xerogels. Scanning electron microscopy (SEM) was applied to observe the ultrastructure changes of the modified xerogels suggesting that gelatin xerogel at rutin concentration of 8 mg/g dry gelatin showed the highest cross-linking density. X-ray diffraction revealed that both gallic acid and rutin could enter the spacing of polypeptide chains of gelatin to reinforce the intermolecular interaction. And FTIR spectra verified that gallic acid and rutin molecules mainly interacted with skeletal C–N–C group and carboxyl group of gelatin molecules in the formation of gels. The results suggested that rutin was a better cross-linking agent for gelatin, and gels treated with rutin could be found with different physicochemical properties.     

两种方法提取的鸡肺胶原蛋白性质及保湿性研究

本文以鸡肺为原材料,利用酸提和超声辅助酸提法提取胶原蛋白,并对其性质及保湿性进行研究。结果表明,所提取的鸡肺胶原蛋白经氨基酸分析显示组成基本相似,甘氨酸含量最高,分别占24.12%和23.93%,亚氨基酸含量仅次之,分别占19.74%和22.28%。酸提和超声辅助酸提胶原蛋白在229.0和224.9 nm处有胶原蛋白的特征紫外吸收峰。SDS-PAGE显示两种鸡肺胶原蛋白中均含有α₁链、α₂链、少量的β链和γ链,傅里叶变换红外光谱及X-射线衍射图谱共同表明两种方法提取的鸡肺胶原蛋白分子排列紧密,均保持了原有的三螺旋结构,说明在超声辅助酸提过程中胶原蛋白的结构保持完好,三螺旋结构未被破坏。酸提的胶原蛋白等电点为7,粒径分布在340 nm左右;超声辅助酸提的胶原蛋白等电点为6,粒径分布在295 nm左右,结合胶原蛋白的溶解性说明了超声辅助酸提可破坏胶原蛋白的氢键,改变蛋白质的颗粒大小和聚集形态。扫描电镜结果表明超声辅助酸提的胶原蛋白结构呈连续纤维状并多孔,且颗粒直径明显减小。在放置24 h时,超声辅助酸提胶原蛋白的吸水性和保水性分别为常规酸提胶原蛋白的1.25倍和1.17倍。综上所述,超声辅助酸提未破坏胶原蛋白特有的三螺旋结构,通过改变氢键和蛋白的颗粒大小使得胶原蛋白具有更好的溶解性和吸湿保湿性。     

The role of salt washing of fish skins in chemical and rheological properties of gelatin extracted

Dover sole (Solea vulgaris) skins were washed with different salt solutions previous to gelatin extraction by a mild acid pre-treatment. The effects of NaCl, KCl, MgCl₂, MgSO₄ and no-salt washing on the mineral content, yield of extraction, molecular weight distribution, gel strength, aggregation phenomena and viscoelastic properties of gelatin newly dissolved and after overnight cold maturation were evaluated. Skin washing with NaCl and KCl induced noticeable changes in molecular weight distribution, and consequently in gel strength and rheological properties, especially when compared with unsalted gelatin preparations. However, salts containing Mg²⁺ gave rise to the retaining of this bivalent cation in the resultant gelatin, which is detrimental to the gelatin quality.     

Effects of Alkaline and Acid Pretreatments on Alaska Pollock Skin Gelatin Extraction

Pretreatments with different alkalis and acids at different concentrations were used to determine their effects on gelatin extraction from Alaska pollock skin. The alkaline pretreatments with the OH concentrations lower than 0.5 mol/L removed noncollagenous proteins without significant loss of skin collagen. The acid pretreatments caused loss of collagen, even using a weak acid with a low H concentration at a low temperature. The presence of proteases might cause degradation of gelatin extract, but the pretreatments with NaOH or Ca(OH)₂ at 0.1 mol/L OH concentration, or acetic acid at 0.05 mol/L H concentration could significantly decrease the degradation by proteases. The combination of an alkaline pretreatment followed by an acid pretreatment not only removed the noncollagenous proteins, but also provided the proper pH condition for extraction, during which some cross‐linkages could be further destroyed but with less breakage of polypeptide chains.     

Physico-chemical and film forming properties of giant squid (Dosidicus gigas) gelatin

Giant squid (Dosidicus gigas) inner and outer tunics were subjected to hydrolysis with pepsin prior to gelatin extraction (G1 gelatin) by a mild-acid procedure. Furthermore, a second gelatin extraction (G2 gelatin) was done using the collagenous residues that remained from the first extraction. Pepsin allows the collagen solubilisation and the extraction yield to increase by yielding extracts high in α-chains. G1 exhibited good gel forming ability but G2 showed poor viscoelastic behaviour and low gel strength, in agreement with the results for the molecular weight distribution, which showed a considerably higher content of low molecular weight components. In spite of these differences, both G1 and G2 showed good filmogenic ability and similar properties were found including the absence of colour, opacity, low water vapour permeability and high puncture deformation. Nevertheless, films made from G1 had a higher puncture force than films made from G2 as a result of the different molecular weight distribution.     

Effects of acid concentration and the UHP pretreatment on the gelatinisation of collagen and the properties of extracted gelatins

An ultra‐high‐pressure (UHP) transmission medium with HCl was applied as a pretreatment to extract gelatin. The effects of the acid concentration (0–1% (w/v)) on the gelatinisation of collagen and the properties of gelatin were investigated. An increase in the acid concentration decreased the thermostability of collagen and increased the yield of gelatin (from 64% increased to 80%). The content of the subunit components in the pretreated collagen and the gelatin declined slightly as the acid concentration was increased, resulted in slight decrease (P > 0.05) in the gel strength (from 435 g decreased to 408 g). The analysis of Fourier transform infrared spectroscopy (FTIR) spectra showed that the triple‐helical structure, secondary structures of the collagen and covalent cross‐linking in the collagenous fibres were damaged gradually as the acid concentration was increased. The scanning electron microscopy (SEM) images showed that the smooth surface of collagen was partly disrupted with microvoids after UHP/1% HCl pretreatment, which may be related to the damage on the covalent cross‐linking.     

In Vivo Digestibility of Insoluble Collagen from Bovine Tendon as Influenced by the Inhibition of Gastric Acid Secretion

Insoluble collagen (bovine Achilles tendon), gelatin and meat were each mixed with whole egg protein (about 50% of the nitrogen) and fed to rats. True digestibility was evaluated after inhibiting gastric acid secretion with omeprazole. Insoluble collagen, supplemented with small amounts of essential amino acids, was also given but without inhibiting gastric acid secretion. Egg protein was fully digested and not affected by inhibition. The true digestibility of insoluble collagen/egg was 85%, corresponding to 71% true digestibility for insoluble collagen alone. This was significantly lower than the value of 95% obtained for insoluble collagen without inhibiting gastric acid secretion. True digestibilities for gelatin/egg were 99% and meat/egg 98%. Inhibition of gastric acid secretion thus did not affect digestion of gelatin and meat.     

Characterization of edible film fabricated with channel catfish (Ictalurus punctatus) gelatin extract using selected pretreatment methods

ABSTRACT:  Farm-raised catfish are important to the economy of the southeastern states in the United States, and catfish processing produces about 55% of by-products for inexpensive sale. Therefore, the utilization of catfish by-products is of great interest to the catfish industry. The objectives of this research were to determine the optimum pretreatment method to extract catfish gelatin for edible film application, and to characterize physical, mechanical, and barrier properties of edible films fabricated with catfish skin gelatin. Catfish skins obtained from a local plant were treated with 6 selected pretreatment methods. The main extraction was performed with deionized water at 50 °C after pretreatment. The gelatin yield was calculated and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed to characterize molecular weight (MW) profile. Color, tensile strength (TS), elongation, and water barrier property were determined to characterize the fabricated catfish gelatin films. From the results of gelatin yield, color, SDS-PAGE, as well as mechanical and barrier properties of the film, the pretreatment method with 0.25 M NaOH and 0.09 M acetic acid, followed by extraction at 50 °C for 3 h, was determined as the optimum extraction method. The catfish gelatin exhibited higher MW fractions than commercial mammalian gelatin. The catfish gelatin extracts possessed film-forming properties determined by TS, elongation, and water vapor permeability (WVP) comparable to those of commercial mammalian gelatin. The selected formula for catfish gelatin film was determined as 1% gelatin and 20% glycerol, resulting in greatest TS and lowest WVP.     

过氧化氢诱导的罗非鱼皮胶原纤维降解过程（Ⅱ）——降解过程中产物组成与性质的变化

研究过氧化氢溶液体系中罗非鱼皮胶原纤维热降解过程,反应体系中降解产物的氨基酸组成、分子质量和性质的变化。结果表明：反应1 h内,释放到溶液的胶原蛋白降解产物极少,不足以测试样品的凝胶强度和黏度。反应1～3 h,反应体系中溶液的表观黏度增加,反应液冷却后可凝结成凝胶,凝胶强度随时间的延长逐渐增大,说明释放到水溶液中胶原分子数量增加,溶质质量浓度提高。反应3～5 h后,反应液表观黏度随时间下降,反应液中溶质质量浓度提高,凝胶的凝胶强度下降,说明这个阶段以原胶原分子肽链的裂解为主体,导致胶原蛋白进一步水解断裂。电泳结果显示,反应4 h的样品,分子质量在130 kD以下的条带比例增加,说明样品中α链断裂片段增加。氨基酸组成分析显示,降解产物与鱼皮氨基酸组成略有差异,但不同反应时间点,明胶产物的氨基酸均没有显著变化,说明过氧化氢协同热效应,主要是通过水解肽键的方式实现胶原纤维向可溶态明胶的转变。     

兔皮明胶提取工艺优化

以兔皮为原料,研究稀盐酸短时诱导兔皮制备明胶的工艺。以明胶提取率和凝胶强度为评价指标,对兔皮明胶制备工艺中的盐酸质量分数、盐酸处理时间、提胶pH值、提胶温度4 个因素进行了优化,在此基础上通过正交试验确定最佳工艺为盐酸质量分数1%、盐酸处理时间10 min、提胶温度65 ℃、提胶pH 4。在此工艺条件下明胶提取率高达（86.85±1.71）%,凝胶强度为（481.43±16.89）g。明胶基本性质符合GB 6783-2013《食品添加剂：明胶》要求。     

Soft and Ca-retaining Gelatin Prepared by Conjugating with Acidic Saccharides

ABSTRACT: Gelatin samples conjugated with acidic saccharides such as glucuronic acid, alginic acid oligosac-charide, and low-molecular-weight alginic acid were prepared to improve the functional properties of ossein gelatin by the Maillard reaction. The conjugation resulted in a decreased isoelectric point, retardate gelation time, low storage modulus, and low melting temperature and enthalpy of gelatin gel; in particular, low-molecular-weight alginic acid resulted in a large improvement. The alginic acid oligosaccharide-conjugated gelatins and low-molecular-weight alginic acid-conjugated gelatins had calcium-retaining ability, and the latter exhibited calcium-aggregating ability. It is thus considered that conjugation with low-molecular-weight alginic acid could be effective for providing a new type of gelatin with a soft texture and calcium-retaining and calcium-aggregating ability.     

大目金枪鱼皮明胶的理化性质及结构分析

以大目金枪鱼皮为原料制备明胶,对所得明胶的凝胶强度、胶凝温度、熔化温度、氨基酸组成、十二烷基硫酸钠-聚丙烯酰氨凝胶电泳（sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE）、光谱学特性等理化性质及结构特性进行研究,并与猪皮明胶进行比较。结果表明,金枪鱼皮明胶的凝胶强度为403?g,胶凝温度和熔化温度分别为21.5?℃和28.8?℃,略低于猪皮明胶;氨基酸分析结果表明,金枪鱼皮明胶中亚氨基酸质量分数为19.09%,低于猪皮明胶的22.82%,可以解释金枪鱼皮明胶凝胶特性、胶凝温度和熔化温度低于猪皮明胶的原因。SDS-PAGE电泳结果显示,金枪鱼皮明胶的小分子组分质量分数仅为6.67%,说明预处理及热水提胶过程并没有破坏明胶中亚基的完整性。金枪鱼皮明胶的紫外光谱与红外光谱谱图均与猪皮明胶相似,进一步说明实验所制得的产物为高质量明胶。