Antioxidant Properties of Protein Hydrolysate Obtained from Oyster Saccostrea cucullata (Born, 1778)

The antioxidant activities of enzymatically hydrolyzed (protease from Bacillus cereus SU12) oyster (Saccostrea cucullata) protein were studied. The hydrolysate exhibited a strong antioxidant potential in 1, 1-diphenyl-2-picrylhydrazyl (DPPH, 85.7 ± 0.37%), followed by hydrogen peroxide radical scavenging activity (81.6 ± 0.3%), hydroxyl radical scavenging activity (79.32 ± 0.6%), and reducing power assay (2.63 ± 0.2 OD at 700 nm) at a concentration of 1 mg/mL. Due to the high antioxidant potential, the hydrolysate was purified in Sephadex G-25 gel filtration chromatography. The active peptide fraction was identified by DPPH and reducing power assay. The amino acid content of the purified active peptide fraction was analyzed by high performance liquid chromatography. The active fraction contained a good quantity of both essential and nonessential amino acids. The present study revealed that oyster (S. cucullata) protein hydrolysate is a potential source for natural antioxidants.     

Antioxidative Activitiy of Protein Hydrolysate from the Muscle of Common Kilka (Clupeonella cultriventris caspia) Prepared Using the Purified Trypsin from Common Kilka Intestine

Trypsin from the intestine of common kilka (Clupeonella cultriventris caspia) was purified using ammonium sulfate precipitation (30–50% saturation), Sephadex G-75, and DEAE-cellulose chromatography with the purity of 30-fold and the yield of 12%. The molecular weight of trypsin was estimated to be 23.2 kDa based on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The trypsin had optimal activity at pH 8.0 and 60°C using N-α-benzoyl-DL-arginine-ρ-nitroanilide hydrochloride (BAPNA) as a substrate and showed high stability in the pH range of 7.0–10.0. It was stable up to 50°C. Soybean trypsin inhibitor (SBTI) and N-ρ-tosyl-L-lysine-chloromethylketone (TLCK) significantly inhibited trypsin activity (p < 0.05). Protein hydrolysate from common kilka muscle with different degrees of hydrolysis (DHs; 20, 30, and 40%) was prepared using the purified trypsin, and antioxidative activities were determined. 1,1-Diphenyl-2-picrylhydrazyl (DPPH), 2,2’-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities, ferric reducing antioxidant power, and ferrous chelating activity of hydrolysate increased with increasing DH up to 40% (p < 0.05). Therefore, trypsin from intestine of common kilka could be used as a processing aid for production of fish protein hydrolysate with antioxidative activity.     

Effect of Degree of Hydrolysis and Protease Type on the Antioxidant Activity of Protein Hydrolysates From Cuttlefish (Sepia officinalis) By-Products

We have investigated the antioxidant activities of eight hydrolysates from cuttlefish by-products obtained by treatment with various gastrointestinal proteases (chymotrypsin, trypsin, and crude alkaline enzyme extracts from cuttlefish and sardinelle) and bacterial proteases (Alcalase and crude enzymes from Bacillus pumilus A1, Bacillus mojavensis A21, and Bacillus cereus BG1). The antioxidant activities of the cuttlefish by-products protein hydrolysates (CPHs) were evaluated using various in vitro antioxidant assays, such as 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity, reducing power, and total antioxidant capacity. All hydrolysates showed different degrees of hydrolysis (DH) and varying degrees of antioxidant activity. Among the different hydrolysates, cuttlefish crude enzyme hydrolysate exhibited the highest antioxidant activity, followed by sardinelle crude enzyme and Alcalase hydrolysates. Further, CPHs with different degrees of hydrolysis were prepared by treatment with proteolytic enzymes from cuttlefish, sardinelle, and B. mojavensis A21. All hydrolysates showed a greater antioxidative activity as indicated by all the methods considered. In addition, antioxidant activity in hydrolysates was positively correlated with the increase of DH. The results of this study indicated that CPHs might be a good candidate for further investigation in developing new antioxidants.     

Utilization of Shrimp By-Products by Bioconversion with Medical Fungi for Angiotensin I-Converting Enzyme Inhibitor and Antioxidant

ABSTRACT

A liquid fermentation process to bioconvert shrimp by-products was developed with two species of fungi, Boletus edulis and Suillus bovinus. Angiotensin I-converting enzyme (ACE) inhibitory, antioxidant activities of bioconverted products and the deodorization effect of fungal bioconversion were determined. Two species of fungi could grow quickly in shrimp by-products medium and deodorize shrimp by-products. Bioconverted products had higher ACE inhibitory and antioxidant activities than control medium. Water extracts without crude polysaccharides from mycelia of B. edulis had the highest ACE inhibitory activity (IC₅₀ = 0.084 ± 0.011 mg/mL). Crude exopolysaccharides of B. edulis had higher antioxidant activity. Bioconversion with the fungus was proven to be a novel, practicable way to recycle shrimp by-products.     

In Vivo Antioxidant Effects of Hydrolysate Derived from Waste Proteins of Mactra veneriformis

Mactra veneriformis has been used as seafood and traditional Chinese medicine for thousands of years in China. In the present study, hydrolysate was prepared from waste proteins of M. veneriformis by trypsin treatment. The protective effect of hydrolysate on the defense system against oxidative stress was investigated by estimating the superoxide dismutase (SOD) activity and malondialdehyde (MDA) level in normal mice. The antioxidant activity of hydrolysate was investigated in D-galactose-induced aging mice by estimating the SOD and glutathione peroxidases (GSH-px) activity and MDA level. Amino acid composition and molecular weight distribution were also determined. These investigations suggest that hydrolysate derived from by-products of M. veneriformis possess antioxidant activity and may be attributed to elevation of the activity of antioxidase and enhanced antioxidant defenses.     

Evaluation of the Antioxidant and Antimicrobial Activity of Protein Hydrolysates and Peptide Fractions Derived from Colossoma macropomum and Their Effect on Ground Beef Lipid Oxidation

The objective of this study was to obtain protein hydrolysate from the mechanically separated meat of blackfin pacu to evaluate the influence by ultrafiltration in the antioxidant and antimicrobial activities of the peptide fractions obtained and to apply in ground beef to evaluate the lipid stability. The enzymatic hydrolysis was performed using the enzyme Protamex (pH 7.0, 60°C) for 240 min. The protein hydrolysate was fractionated by ultrafiltration. Then, the antioxidant capacity of the protein hydrolysate and the peptide fractions were evaluated in vitro by the methods of 2,2’-azinobis (3-ethylbenzothiazoline sulfonic acid) radical capture, 2,2-diphenyl-1-picrylhydrazyl radical-scavenging assay, reducing power, and hydroxyl radical scavenging activity. The antimicrobial activity of the samples was evaluated by disc-diffusion against Staphylococcus aureus and Escherichia coli. After evaluation, the peptide fractions did not present higher bioactivities than that shown for the hydrolysate. The protein hydrolysate was applied to ground beef, where the substances reactive to thiobarbituric acid and color were evaluated during 7 days of storage at 4°C. Lipid oxidation was reduced up to 60.9% and there was no modification of the natural coloration. Thus, the protein hydrolysate can be used as an alternative source of antioxidant for the preservation of refrigerated meats.     

Antioxidant and protective effects of a peptide (VTAL) derived from simulated gastrointestinal digestion of protein hydrolysates of Magallana gigas against acetaminophen-induced HepG2 cells

Oxidative stress is an automatic mechanism responsible for the commencement and continuance of liver injury. In this study, an antioxidative peptide Val-Thr-Ala-Leu (VTAL) was purified from simulated gastrointestinal digestion of protein hydrolysates of the triploid oyster Magallana gigas. Significant antioxidant activity was identified, as well as a protective effect against acetaminophen (APAP)-induced human liver cancer (HepG2) cells. The results suggested that the antioxidant activity improved in a dose-dependent manner. The highest cell viability (88.105?±?3.62%) was observed in 15 mM APAP-induced cells when treated with 25 μg/mL M. gigas peptide [M.g (pep)]. The peptide sequences include hydrophobic amino acids, which could be responsible for its chemoprotective and antioxidant activities. Treatment with M.g (pep) significantly promoted the proliferation of HepG2 cells, thus protecting them against APAP and imbuing them with significant antioxidant capacity. M.g (pep) could be beneficial for treating drug-induced oxidative stress and liver damage. Additionally, M.g (pep) could serve as an alternative to synthetic antioxidant drugs.

     

金枪鱼鱼骨胶原肽的制备及抗氧化活性研究

为制备金枪鱼鱼骨胶原肽,并对其抗氧化活性进行研究,利用酶解、超滤、凝胶色谱和反相高效液相色谱制备抗氧化胶原肽,采用氨基酸序列分析仪测定其氨基酸序列,利用质谱(ESIMS)确定其分子量,采用羟自由基、DPPH自由基、ABTS自由基和超氧阴离子自由基清除实验和脂质过氧化抑制实验对胶原肽抗氧化能力进行评价。结果显示,金枪鱼鱼骨胶原蛋白经胃蛋白酶和胰蛋白酶2步酶解和分离纯化得到1个十肽(TFCH-P2),经氨基酸序列分析和质谱(ESIMS)确定其氨基酸序列为Gly-Pro-Ala-Gly-Pro-Ala-Gly-Glu-Gln-Gly(GPAGPAGQEG),分子量为839.87 u([M+H]+840.68 u)。体外抗氧化实验结果表明,GPAGPAGQEG对羟自由基(EC500.18 mg/mL)、DPPH自由基(EC500.97 mg/mL)、ABTS自由基(EC500.52 mg/mL)和超氧阴离子自由基(EC500.38 mg/mL)具有良好的清除作用;GPAGPAGQEG亦显示出良好的脂质过氧化抑制作用。研究表明,胶原肽GPAGPAGQEG抗氧化活性良好,可以用于抗氧化相关的功能食品、药物或者食品添加剂。     

大眼金枪鱼头蛋白酶解物1 ku超滤组分的抗氧化活性及其理化性质

研究大眼金枪鱼头蛋白酶解物1 ku超滤组分体外的还原力、自由基清除能力及对衰老小鼠体内抗氧化能力的影响,分析1 ku超滤组分的一般成分、氨基酸组成及分子量分布,为进一步分离纯化金枪鱼头抗氧化肽提供基础。体外结果显示,1 ku超滤组分对羟基自由基、超氧阴离子和DPPH自由基的清除活性随浓度的增加而增强,IC50分别为1.38、0.73与0.93mg/mL,还原力也随浓度的增加而增大,在浓度为12.5 mg/mL时为0.763;体内结果显示,灌胃30 mg/kg的1 ku超滤组分连续42 d,D-半乳糖致衰老小鼠肝组织的超氧化物歧化酶(SOD)活性、肝组织和血清的谷胱甘肽过氧化物酶(GSH-PX)活性显著提高(P<0.05),血清丙二醛(MDA)含量显著降低(P<0.01);理化分析结果显示,1 ku超滤组分(干基计)蛋白质含量为96.40%,脂肪0.11%,灰分4.86%,疏水性氨基酸占氨基酸总量的35.8%,活性组分分子量在1 802~2 519 u和422~922 u。     

Potential Precursor of Angiotensin-I Converting Enzyme (ACE) Inhibitory Activity and Structural Properties of Peptide from Peptic Hydrolysate of Cutlassfish Muscle

ABSTRACT

Peptic hydrolysates were prepared by digesting the cutlassfish muscle protein using pepsin for 1, 3, and 6 h, and their inhibitory activity against angiotensin-I converting enzyme (ACE) was studied. The ACE-inhibitory effect of the peptic hydrolysate of cutlassfish muscle generated at the 3 h time point exhibited the strongest activity. After identifying the optimal hydrolysate, the active peptide was isolated by ultrafiltration, gel permeation, and high performance liquid chromatography (HPLC). The resulting purified peptide was characterized using matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/TOF MS/MS) and was identified to be a 496.44 Da pentapeptide (Phe-Ser-Gly-Gly-Glu). The ACE-inhibitory activity of the active peptide exhibited an IC₅₀ value of 0.033 ± 0.003 mg/ml. A molecular docking program was used to simulate the interaction between the peptide and ACE, which revealed that the inhibitory effect was mainly due to the hydrogen bonds between ACE and the peptide. Based on the ACE-inhibitory properties and the molecular docking study of the resulting active peptide, we demonstrated an increase in nitric oxide (NO) production in a dose-dependent manner. In conclusion, cutlassfish protein hydrolysate and the resulting active peptide could be used as active ingredients in functional food as anti-hypertensive agents.     

Antioxidant and Angiotensin I Converting Enzyme Inhibition Effects and Antihypertensive Effect in Spontaneously Hyertensive Rats of Peptide Isolated from Boiled Abalone By-Products,Hallotis discus hannai

ABSTRACT

Abalone is a marine gastropod that is an important fishery and food industrial resource, massively maricultured in Asia, Africa, Australia, and America. Marine by-products from boiled abalone, normally discarded as industrial waste in manufacturing plants, were fractionated and concentrated using an ultrafiltration membrane system (? 1 kDa). In this study, the antioxidant and angiotensin I converting enzyme (ACE) inhibition effects of the boiled abalone by-products (BABs) were investigated. BABs have high antioxidant activities against free radicals (1,1-diphenyl-2-pycryl-hydrazyl (DPPH), hydroxyl, peroxyl, and superoxide radicals), reactive oxygen species (ROS) stress, and DNA damage in H₂O₂-treated RAW 264.7 macrophages. The structure of the purified peptide was identified to be ATPGDEG (MW 752 Da), and the ACE inhibition pattern of the peptide was found to be noncompetitive. In addition, the peptide exhibited an antihypertensive effect according to time-course measurement after oral administration to spontaneously hypertensive rats (SHR). BABs from this genus may be potential candidates for the development of unique natural substances for further industrial applications as functional foods and pharmaceuticals.     

Purification and Antioxidant Property of Antioxidative Oligopeptide from Short-Necked Clam (Ruditapes philippinarum) Hydrolysate In Vitro

Short-necked clam (Ruditapes philippinarum) muscle was hydrolyzed with trypsin, and the antioxidant activities of isolated peptides were investigated. The hydrolysate was fractionated by chromatographic methods using Sephadex G-25 gel filtration and Hypersil BDS C18 reversed phase high performance liquid chromatography (RP-HPLC). The antioxidant activities of the hydrolysate were determined by measuring 1,1-diphenyl-2-picrylhydrazyl (DPPH), reducing power assay, and the protective effect against hydroxyl-radical-induced DNA damage. The amino acid sequence of the purified antioxidant oligopeptide was found to be Gly-Asp-Gln-Gln-Lys.     

Evaluation of the Antioxidant Activity In Vitro and in Hippocampal HT-22 Cells System of Protein Hydrolysates of Common Carp (Cyprinus carpio) By-Product

Fish processing by-products may become more than 50% of the starting material. If mismanaged, these large quantities of discarded fish can create serious pollution problems and can also generate cost associated with their disposal. Enzymatic hydrolysis is one of the techniques that is currently being developed in order to recover and add value to these biomolecules. There is an increasing interest in natural antioxidants that are safer for consumers compared with synthetic antioxidants. In this study, common carp by-product was hydrolyzed using the enzymes Alcalase (A) and Protamex (P) to reach degrees of hydrolysis (DH) of 10 and 15%, respectively. Antioxidant capacity against peroxyl radicals (ACAP); 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging; and the measurement of intracellular reactive oxygen species (ROS) concentration after exposure to common carp protein hydrolysates were investigated. The results revealed that the hydrolysate A15 exhibited significantly (p < 0.05) higher antioxidant activity against the DPPH radical. A15 showed the highest in vitro antioxidant competence against peroxyl radicals, whereas P15 showed the lowest activity against peroxyl radicals (p < 0.05). Hydrolysates having the highest and the lowest in vitro antioxidant activity (A15 and P15, respectively) were selected for the determination of antioxidant activity in the HT-22 cells system. Measurement of intracellular ROS concentration revealed that P15 at the concentration of 1.25 mg/mL significantly (p < 0.05) reduced the intracellular ROS concentration. These results showed that common carp by-product protein hydrolysates are a source of antioxidant peptides with a high potential for food and pharmaceutical industries to develop new nutraceuticals and functional foods.     

Identification of oyster-derived hypotensive peptide acting as angiotensin-I-converting enzyme inhibitor

Angiotensin-I-converting enzyme (ACE) plays a crucial role in the crisis of hypertension. Some peptides that originate from protease hydrolysates are known to suppress ACE activity in vitro and in vivo. Here, we investigated whether trypsin hydrolysate of oyster Crassostrea gigas showed hypotensive activity and ACE inhibition. The hydrolysate significantly suppressed systolic blood pressure and ACE activity in spontaneously hypertensive rats following a one-shot oral administration and a long-term feeding experiment lasting 9 weeks. Each hydrolysate from oyster tissue showed ACE inhibitory activity, indicating the hypotensive effect was due to synergism. One potent ACE inhibitory peptide, Asp-Leu-Thr-Asp-Tyr, was identified from the hydrolysate of the striate muscle, and the peptide exhibited hypotensive activity in vivo. Protease digestion analysis suggested that Asp-Tyr could be the real effector of this penta-peptide in vivo.     

Functional Properties of White Shrimp (Litopenaeus vannamei) By-Products Protein Recovered by Isoelectric Solubilization/Precipitation

The processing of fish in general entails quantities of by-products, such as exoskeleton and cephalothorax of shrimp, which may reach 70%. Protein recovered from by-products has been investigated in recent years for its ability to offer more nutritious foods and improved functional properties. The objective of the present study was the use of the pH shifting process to recover proteins from solubilization and precipitation that are present in the by-products (heads and shells) of white shrimp (Litopenaeus vannamei). The proximal composition of the by-products presented 58.5% protein (d.b). The isoelectric point used to precipitate the protein was defined at pH 4. The protein concentrate presented 73.1% of protein. The yield of the protein concentrate mass resulted in 47.8% (w.b). The greatest solubility found for the protein concentrate was 51.3% at pH 8. The oil and water retention capacity resulted in values of 8.5 and 2.5 mL/g of protein, respectively, and the highest emulsifying capacity was found at pH 8. The by-products and concentrate amino acids profiles confirmed the presence of 16 amino acids. In general, the shrimp protein concentrate obtained showed the potential to be included as an ingredient in food formulations.     

罗非鱼鱼皮酶解物及其硒螯合物的结构与抗氧化特性

为了高值化利用罗非鱼副产物资源以及为酶解物-硒螯合物的产业化提供理论依据,本实验以罗非鱼鱼皮胶原蛋白(TSC)为原料,用4种蛋白酶对其进行酶解,分别获得了酸性蛋白酶酶解物(TSCAc)、木瓜蛋白酶酶解物(TSCP)、菠萝蛋白酶酶解物(TSCB)、碱性蛋白酶酶解物(TSCAl),以Na₂SeO₃为硒源,制备并筛选出硒螯合量最高的酶解物,测定酶解物及其硒螯合物的紫外光谱、荧光光谱、红外光谱、表面疏水性,并对酶解物及其硒螯合物的抗氧化性与抗氧化稳定性进行分析。结果显示,TSCAl的水解度(DH)最高(18.2%),其与硒螯合后的硒螯合量最高(153.5 mg/g),硒螯合率最高(23.7%),小分子量(500～1 000 u)的含量最高。其与硒螯合后,紫外光谱吸收峰强度增大,荧光光谱吸收峰由波长419.8 nm红移到422.0 nm且荧光强度减弱,疏水性在螯合后降低,表明TSCAl与硒螯合生成了新的物质。推测酰胺键、氨基的氮原子、羧基的氧原子可能参与了与硒的螯合反应。研究表明,碱性蛋白酶酶解物-硒螯合物(TSCAl-Se)具有良好的抗氧化性,其在不...     

Cryoprotective effects of shrimp head protein hydrolysate on gel forming ability and protein denaturation of lizardfish surimi during frozen storage

ABSTRACT:   The effects of shrimp head protein hydrolysate (SHPH) from three species of shrimp (northern pink shrimp [ Pandalus eous ], endeavour shrimp [ Metapenaeus endeavouri ], black tiger shrimp [ Penaeus monodon ]) on gel forming ability and protein denaturation of lizardfish surimi during frozen storage at −25°C were evaluated. The quality of lizardfish surimi with 5% (dried matter) of any of the three SHPH or sodium glutamate (Na-Glu) was examined in terms of gel strength, whiteness, Ca-ATPase activity and the amount of unfrozen water, comparing with those of surimi without additive as the control. The residual Ca-ATPase activity and gel strength of surimi with SHPH were higher than those of the control throughout 180 days of frozen storage, regardless of shrimp species. The highest effect was found in surimi with Na-Glu. The gel strength and Ca-ATPase activity found a high positive correlation. The addition of SHPH to surimi also increased the amount of unfrozen water by approximately 1.29–1.36 fold higher than the control, however kamaboko gels of the control was significantly whiter. From these results, freeze-induced denaturation of lizardfish muscle protein could be lessened by the addition of SHPH, resulting in a high gel strength and Ca-ATPase activity.     

Golden Grey Mullet (Liza aurata) Alkaline Proteases: Biochemical Characterization,Application in the Shrimp Wastes Deproteinization,Laundry Commercial Detergents,and Preparation of Antioxidant Protein Hydrolysate

Digestive alkaline proteinases from golden grey mullet (Liza aurata) were extracted and characterized. The crude alkaline protease showed optimum activity at pH 8.0 and 60°C, and it was highly stable over a wide range of pH from 4.0 to 10.0, retaining more than 80% activity after incubation for 1 h at 4°C. The alkaline proteases showed extreme stability toward nonionic and anionic surfactants after preincubation for 1 h at 25°C and relative stability toward oxidizing agents. Additionally, the crude enzyme showed excellent stability and compatibility with various solid and liquid detergents. Further, proteases from golden grey mullet viscera were found to be effective in the deproteinization of shrimp wastes. The protein removal after 3 h at 45°C with an enzyme/substrate (E/S) ratio of 10 U/mg protein was about 76%. The golden grey mullet proteases were also shown to be efficient in the production of antioxidant protein hydrolysate.     

Protein Hydrolysates from Shrimp (Metapenaeus dobsoni) Head Waste: Optimization of Extraction Conditions by Response Surface Methodology

Utilization of shrimp head waste from the processing industry offers a solution to environmental pollution and also produces valuable bioactive peptides. The present study was aimed to optimize the alcalase assisted extraction conditions by response surface methodology (RSM) to obtain protein hydrolysates from shrimp (Metapenaeus dobsoni) head waste with maximum antioxidant activity. Based on the models derived by RSM, the optimized conditions for maximum degree of hydrolysis (DH) were pH 8.2, temperature of 45.4°C, and enzyme/substrate (E/S) of 1.8%. Meanwhile, the optimized conditions for maximum antioxidant activity of protein hydrolysates as measured by 2, 2-diphenyl-1-picrylhydrozyl (DPPH) and ferric reducing antioxidant power (FRAP) assays were pH 8.2 and 8.1, temperatures of 49.7 and 59.4°C, and E/S of 2.1 and 2.7%, respectively. The maximum predicted values for DH, DPPH, and FRAP were 42.44%, 39.64% inhibition, and 8.3 μM Fe (II)/g wet wt. of sample, respectively. The extraction of protein hydrolysates at optimal conditions derived by these models resulted in DH, DPPH, and FRAPs of 40.31%, 38.93%, and 8.21 μM Fe (II)/g of sample, respectively, demonstrating the fitness of the models. The present study demonstrates the potential of Metapenaeus dobsoni head waste as a source of protein hydrolysates with prospective antioxidant activity.     

超声辅助酶解鲣加工副产物制备蛋白胨

为了提高水产加工副产物的利用率和附加值,以鲣加工副产物为原料,采用胰蛋白酶结合超声处理制备蛋白胨,并分析了鲣加工副产物超声辅助酶解过程中蛋白酶活性、水解度、氮回收率、TCA-可溶性氮回收率、酶解产物分子量分布等指标的变化,探究了超声辅助酶解的作用时间、温度以及超声功率等因素对鲣加工副产物酶解产物的影响,通过单因素实验优化确定了蛋白胨制备的最佳酶解工艺条件。结果显示,超声处理造成胰蛋白酶酶活发生显著变化,在功率为120 W的超声场下,胰蛋白酶酶活在30 min内呈上升趋势,但在超声场处理30 min后,胰蛋白酶的酶活呈明显下降趋势,至4 h后酶活变化趋势趋于平缓。超声功率和酶解温度都会影响胰蛋白酶对鲣加工副产物的酶解效率,在超声功率240 W和酶解温度50°C条件下,氮回收率比无超声处理组提高了18.66%,水解度提高了30.43%,TCA-可溶性氮回收率提高了33.20%,且超声处理有效提高了酶解液中小分子肽的含量。超声辅助酶解鲣加工副产物的最佳工艺条件为温度55°C,超声功率240 W,酶解时间4 h,此时氮回收率为81.40%,TCA-可溶性氮回收率为40.75%。