Characteristics and nutritional value of biscuits fortified with debittered salmon (Salmo salar) frame hydrolysate

Effect of debittered salmon frame hydrolysate (DSFH) at various levels (0, 5, 10, 15, 20 and 25 g/100 g) on physicochemical, textural, sensory and nutritional properties of biscuits was investigated. The highest thickness was obtained for the sample with 25 g/100 g DSFH (P < 0.05). There was no difference in diameter among all the biscuit samples (P > 0.05). The samples added with DSFH had lower weight, water activity and moisture content than the control (CONT, without DSFH) (P < 0.05). DSFH at 15 g/100 g showed no detrimental effect on sensory properties of resulting biscuits (DSFH-15). The DSFH-15 biscuit showed reduction in cutting force and fracturability. Scanning electron microscopic and cross-sectional images showed that DSFH-15 biscuit had more porous structure, compared to the CONT. The biscuits fortified with 15 g/100 g DSFH had higher protein but had lower energy value, fat and carbohydrate content than the CONT.     

云南磷肥工业副产氟资源综合利用途径初探

根据云南磷肥工业发展情况 ,提出对磷肥工业副产氟资源综合利用的设想 ,并介绍目前国内已有的一些氟资源综合利用的工艺技术     

Feasibility of fishmeal replacement by shrimp head silage protein hydrolysate in Nile tilapia (Oreochromis niloticus L) diets

This study provides information on the use of shrimp head silage protein hydrolysate (SPH) as an alternative protein source for tilapia feeding. Six diets (28% protein, 12% lipid) were prepared where fishmeal protein was replaced at levels of 0 (control), 10, 15, 20, 25 and 30% with the hydrolysate. The diets were supplied to Nile tilapia fry (338 mg initial weight) stocked in plastic recirculating 20 l tanks (10 animals per tank), with three replicates per treatment. After an 8 week experimental period, fish fed the diets containing 10 and 15% SPH showed significantly better performance in terms of final body weight, weight gain (%), mean daily weight gain (mg day^?1), specific growth ratio and feed conversion ratio than those fed the control diet (fishmeal as protein source) and higher‐SPH diets. It is concluded that shrimp head hydrolysate is a promising alternative protein source for tilapia feeding, improving growth ratio at dietary inclusion levels as high as 15%. In addition, the diets with added shrimp silage protein were well accepted by the fish, which avidly consumed the feed during the experiment. © 2002 Society of Chemical Industry     

镉质量浓度和鱼尺寸对罗非鱼积累和转移镉的影响

为研究尺寸和镉(Cd~(2+))质量浓度对罗非鱼积累和转移水环境中Cd~(2+)的影响,用室内培养的方法,选取4种尺寸的罗非鱼,设置不同质量浓度Cd~(2+)的暴露试验,分别测定其半致死率、Cd~(2+)积累量和对Cd~(2+)的转移系数以及罗非鱼的相对增长率.结果表明:不同尺寸的罗非鱼对Cd~(2+)的响应不同,其中,幼龄鱼的LC50浓度最低,体长为31.5±3.4 cm的罗非鱼LC50最高;低质量浓度Cd~(2+)(0.5 mg/kg)处理下,罗非鱼尺寸不同,相同鱼组织对Cd~(2+)的吸收积累量差异显著(P0.05),而高质量浓度Cd~(2+)处理时,不同尺寸罗非鱼的同一组织对Cd~(2+)的积累量无显著性差异;除体长27.4±2.9 cm罗非鱼外,相同尺寸的罗非鱼Cd~(2+)转移系数都是低质量浓度显著大于高质量浓度(P0.05);高质量浓度Cd~(2+)处理对各种尺寸罗非鱼质量增加的抑制率显著高于低质量浓度Cd~(2+)处理的抑制率.此外,不同Cd~(2+)质量浓度对相同尺寸的罗非鱼也产生不同的影响.因此,罗非鱼的尺寸和Cd~(2+)质量浓度都对罗非鱼积累和转移Cd~(2+)产生影响.     

复合肥副产盐酸杂质含量高的原因分析及对策

介绍硫基复合肥副产盐酸杂质含量高的原因及技改情况。技改后,用脱盐水代替自来水,减少了停车清堵时间及维修费用,产品盐酸浓度,杂质SO42、Fe的含量均达到优等品标准,年增加利润108万元。     

酶法水解对罗非鱼下脚料蛋白功能特性的影响

以罗非鱼下脚料为原料,采用Alcalase蛋白酶、中性蛋白酶、风味蛋白酶对其进行控制酶解,通过pH-stat法控制水解程度,制备不同水解度(1.0%～15.0%)的罗非鱼下脚料酶解蛋白,探讨酶的种类和水解度对其乳化性和发泡性的影响。结果表明:在水解度较低(3.0%～5.0%)时,酶解蛋白的乳化性和发泡性较好,随着水解度进一步增大,酶解蛋白的乳化性和发泡性均降低;比较而言,由中性蛋白酶水解得到的酶解蛋白乳化性较好,而风味蛋白酶水解得到的酶解蛋白发泡性较好;此外,pH值(2～10)对轻度酶解蛋白的乳化性和发泡性影响较大,在pH 4.0～5.0范围内,酶解蛋白的乳化性和发泡性最差。     

以金属铝水解制氢副产品为原料制备a-A12O3粉体的研究

以金属铝一水反应法制氢的副产品为主要原料,添加表面活性剂十二烷基苯磺酸钠、晶种（1-A1203和相变促进剂ZnF2,在实验室制得a-Al2O3粉体,并利用ICP、XRD、TG-DSC、SEM、物理吸附仪等对试样进行表征。结果表明,该金属铝-水反应法制氢的副产品干燥后为单斜型三羟铝石（Al（OH）3）,纯度高达99．58％,经过1300℃×3h高温处理后完全转化为a-A12O3;以十二烷基苯磺酸钠作为表面活性剂,添加1％的ZnF2作为相变促进剂和1％的纳米a-Al2O3作为晶种,该副产品在1200℃下即可完全转化为a-Al2O3,粉体的比表面积为6．17m2／g,平均粒径为244nm。     

Process optimisation and physicochemical characterisation of enzymatic hydrolysates of proteins from co‐products of Atlantic Salmon (Salmo salar) and Yellowtail Kingfish (Seriola lalandi)

The aim of this study was to develop an enzymatic hydrolysis process of protein co‐products for two major commercial fish species in Australia: Atlantic salmon (AS) and Yellowtail kingfish (YTK). The outcomes are to produce high protein recovery of fish protein hydrolysates within controlled molecular weight ranges that display enhanced physicochemical properties of oil binding and emulsification. Three enzymes (Flavourzyme, Neutrase and Alcalase) were applied to processing co‐products. Protein recovery and physicochemical properties were evaluated with increasing hydrolysis time from 30 min to 180 min and ratio of enzyme to substrate (E/S) from 0.5% to 3.0%. In order to achieve a product with optimum emulsifying capacity (50 ± 0.6 m² g^?1), an E/S ratio of 0.6–1.3% Flavourzyme was applied for 30–111 min with a protein recovery of 55%; in order to achieve a product with optimum oil‐binding capacity (8.3 ± 0.3 g oil g hydrolysates^?1), an E/S ratio of 2.3–3.0% Flavourzyme was applied for 25–64 min with a protein recovery of 70%. YTK protein hydrolysates were further membrane‐fractionated into five fractions (>100 kDa, 50–100 kDa, 30–50 kDa, 10–30 kDa and <10 kDa), and of these, the 10–30 kDa exhibited the best properties of oil binding (19 ± 0.3 g oil g hydrolysates^?1) and emulsification (57 ± 0.7 m² g^?1). These results demonstrate the importance of enzymatic hydrolysis of seafood co‐products into high‐value ingredients for food products and processing.     

Angiotensin I‐converting enzyme inhibitory activity of protein hydrolysates prepared from three freshwater carps (Catla catla,Labeo rohita and Cirrhinus mrigala) using Flavorzyme

Fish protein hydrolysates from three freshwater carps, Catla catla, Labeo rohita and Cirrhinus mrigala with different degree of hydrolysis (DH) (5%, 10%, 15% and 20%), were prepared using Flavorzyme enzyme and designated as HCF, HRF and HMF, respectively. The angiotensin I‐converting enzyme (ACE) inhibitory activity of hydrolysates was found to vary from 43 ± 2% to 71 ± 3%. Based on ACE inhibitory activity, HRF with DH‐15% was taken up for further study. The mode of ACE activity inhibition by HRF‐DH 15% was mixed type as revealed by Lineweaver–Burk plot. Sequential digestion of HRF‐DH 15% using pepsin and pancreatin decreased the ACE inhibitory activity from 76% to 63%. Partial purification of HRF‐DH 15% by size exclusion chromatography gave three different fractions designated as F‐1, F‐2 and F‐3 with the molecular mass in the range of 6456–407 Da. Fraction 2 had significantly higher ACE inhibitory activity than the other fractions.