用猫豆渣为原料制备口服水解蛋白

本文介绍从提取左旋多巴后的废渣——猫豆[Mueuna Cochinchinenris(Lour) A.Cheual]渣为原料制备口服水解蛋白。首先从豆渣中提取酪蛋白,再经酸水解法而制备。工艺设计考虑到原料的特点,排除了残存的左旋多巴,收得率为豆渣的11～13％。成品经氨基酸分析仪测定,证明含有七种必需氨基酸在内的十七种氨基酸,氨基氮的含量较国内同类产品高。各种必需氨基酸的配比,接近人乳模式。经测定小白鼠经口LD_(50)及95％可信限范围为27.8(25.4～30.2)g/kg。在亚急性毒性试验中未发现任何不良反应。     

新鲜猪血酶法制备口服水解蛋白

本文报导以新鲜猪血为主要原料,辅以它种蛋白质,酶法水解制备口服水解蛋白(简称“酶解蛋白”),收得率为10%(W/V),成品分析测定,证明所含氨基酸和肽类含氮物达88.1%,其中八种必需氨基酸俱全,并且,各种必需氨基酸种类、含量的配合比率接近人乳模式,质量分析结果符合规定标准及食品卫生要求。     

口服水解蛋白及其营养合剂的制备与研究

本文通过以猪血为原料胰酶水解制备口服水解蛋白及营养合剂的研究,它含有多种必需氦基酸、微量元素、维生素,氨基酸同时促进各种离子吸收,动物对照实验表明该合剂能促进小鼠生长（Ｐ＜０．０１）。对创伤病人,病后、手术后的恢复健康结果令人满意。     

水解蛋白针剂的制备

序言水解蛋白针剂是一种营养型的代血浆,它是酸法、碱法或酶法水解蛋白质后的产物,制剂中含有各种氨基酸或氨基酸及小肽。它适用于大面积烧伤病人、胃切除病人、胃肠道肿瘤病人及外科手术病人等等。早在本世纪四十年代国外已开始应用。由于内科、外科病人常产生低蛋白血症,注射水解蛋白后,可补充身体内缺少     

以青砖茶为原料的果茶饮料制备

以青砖茶、新鲜苹果汁、西瓜汁和菠萝汁为主要原料进行果茶饮料的研制,采用单因素试验及正交分析试验对果茶饮料的配方进行工艺优化,以感官评价和吸光值为评定指标,确定果茶饮料的最佳配方。结果表明,体积比分别为8∶2的茶汤与苹果汁的混合汁、5∶5的茶汤与西瓜汁的混合汁和3∶7的茶汤与菠萝汁的混合汁混匀调配出的茶饮料的口感最佳,色泽清透,且香气较佳。本研究为黑茶果茶饮料的研 制提供了理论依据。     

以L-天冬氨酸为原料制备D-天冬氨酸的新方法

以L-天冬氨酸为原料经过酯化、消旋、拆分和水解制备D-天冬氨酸。使L-2,3-二苯甲酰酒石酸(L-DBTA)与DL-天冬氨酸-β-甲酯在水溶液中于65~70℃反应形成非对映体盐,冷却到室温,D-天冬氨酸.L-DBTA盐析出,过滤后再经水解得到D-天冬氨酸,收率78.2%,旋光纯度达到99%以上。     

以DL-丝氨酸为原料制备D-丝氨酸的新方法

以DL-丝氨酸为原料经过酯化、拆分和水解制备D-丝氨酸。使L-2,3-二苯甲酰酒石酸(L-DBTA)与DL-丝氨酸甲酯在无水乙醇中于60℃反应形成非对映体盐,冷却到0℃,D-丝氨酸甲酯.L-DBTA二盐析出,过滤后再经水解,得到D-丝氨酸,总收率为74.8%,旋光纯度达到98%以上。     

以玉米淀粉糖渣为原料制备米曲发酵酱油

以玉米淀粉糖渣为原料制备米曲,米曲中的中性蛋白酶活力能够达到4000 U/g(干基),糖化酶比活力可达到120 U/g左右,满足酿造酱油所需要求。用糖渣米曲发酵酱油,氨基态氮和总氮质量浓度分别能够达到7.1 g/L和11.9 g/L,还原糖质量浓度为13.2 g/L,各项理化指标均可达到国家二级酱油标准。     

以白薯母为原料用生香酵母提高白酒质量试验

白薯母是种薯采秧后剩下的块根,内含50%左右的淀粉。因有苦臭味,所以人畜都不能食用,以前只是将其晒干做燃料。1970年我厂开始用白薯母酿制白酒,出酒率35%左右,伹制出来的白酒具有白薯母的苦、臭味,不受群众欢迎。能否提高白酒质量,用带有苦、臭味的酿酒原料酿出香酒来是摆在我们面前的重要任务。我厂充分调动了全厂职工大搞技术革新的积极性,狠批了“群众落后论”。“爬行主义”等谬论,提高路线斗争觉悟。遵     

洋虫成虫脱脂蛋白酶解液的抗氧化作用

对洋虫Martianus dermestoides Chevrolat成虫脱脂蛋白酶解液的抗氧化作用进行了研究。用木瓜蛋白酶水解洋虫成虫脱脂蛋白,用截留分子量分别为10 kDa和6 kDa的超滤膜将其分离成3个组分,用邻苯三酚 鲁米诺发光法、DPPH自由基清除法、Fenton法和Oyaizu法,分别测定不同分子量的洋虫成虫脱脂蛋白酶解液清除超氧阴离子自由基、DPPH自由基及羟基自由基的能力。结果表明：洋虫成虫蛋白酶解液3个组分都有很好的清除自由基能力,且还原性较强,以分子量＜6 kDa的组分清除效果最佳(P＜0.05)。结果揭示洋虫成虫脱脂蛋白酶解液具有很好的抗氧化作用。     

黑水虻幼虫蛋白及其酶解产物的抗氧化活性研究

为了探究黑水虻Hermetia illucens幼虫蛋白及酶解产物的抗氧化活性,以鲜活黑水虻幼虫冻虫为原料,采用碱提酸沉法提取黑水虻蛋白,通过碱性蛋白酶、菠萝蛋白酶、风味蛋白酶、木瓜蛋白酶对其蛋白质溶液进行酶解,分别从2,2′-联氮-双-3-乙基苯并噻唑啉-6-磺酸（ABTS）自由基、羟自由基、1,1-二苯基-2-三硝基苯肼（DPPH）自由基3个方面对黑水虻蛋白及其酶解液的抗氧化能力进行测定。结果表明：黑水虻幼虫蛋白及4种酶解后的蛋白肽具有较好的抗氧化活性,其中黑水虻幼虫蛋白对ABTS自由基、羟自由基、DPPH自由基的半抑制浓度（IC50）分别为2.91、0.232、0.764 mg/mL,而酶解过后的蛋白肽具有更强的抗氧化活性,对ABTS自由基、羟自由基、DPPH自由基的最低半抑制浓度（IC50）分别为0.295、0.082、0.354 mg/mL。本研究初步证明了酶解制备抗氧化肽的可行性,为昆虫蛋白资源的利用和无抗饲料的研制提供了新的研究思路。     

Isolation and characterization of an abortifacient protein, momorcochin, from root tubers of Momordica cochinchinensis (family cucurbitaceae)

A glycoprotein with a molecular weight of 32,000 as estimated by SDS-polyacrylamide gel electrophoresis, and characterized by an abundance of Asp and Glu residues and an absence of Cys residues in its amino acid analysis, was isolated from fresh root tubers of Momordica cochinchinensis using a procedure that involved acetone precipitation, ammonium sulfate precipitation, ion exchange chromatography on DEAE Sepharose CL-6B and gel filtration on Sephadex G-75. The protein was capable of inducing mid-term abortion in mice. The characteristics of this protein were compared and contrasted with those of the abortifacient proteins isolated from other plants of the Cucurbitaceae family.     

A rapid autolytic method for the preparation of protein hydrolysate from poultry viscera

Protein hydrolysate was prepared from poultry viscera by a procedure involving autolysis for 6h at pH 2.8 and 55 degrees C followed by heat inactivation, filtration and drying. Recovery of nitrogen in the product was 87%. The process reduced the viable count of bacteria by 5-6logcfu/g. The product contained 84% protein, 6.5% ash and 8.8% moisture. Peptide analysis by gel filtration chromatography showed size in the range of 0.5-5kDa. RPHPLC exhibited the presence of hydrophilic peptides in higher concentration than that in trypsin digest of casein. Protein hydrolysate exhibited presence of all essential amino acids in comparison with reference protein except for methionine and threonine. The product possesses excellent solubility (>93%) over a pH range of 1-12. Efficacy of the product as a bacteriological media or feed supplement is discussed.     

Angiotensin I converting enzyme (ACE) inhibitory peptides from salmon byproduct protein hydrolysate by Alcalase hydrolysis

Angiotensin I converting enzyme (ACE) inhibitory peptides were produced from salmon byproduct proteins via enzymatic hydrolysis using Alcalase, flavourzyme, neutrase, pepsin, protamex and trypsin. Among them, Alcalase hydrolysate showed the highest ACE inhibitory activity, thus ACE inhibitory peptides were purified using consecutive chromatography. The purified ACE inhibitory peptides were identified to be Val-Trp-Asp-Pro-Pro-Lys-Phe-Asp (P1), Phe-Glu-Asp-Tyr-Val-Pro-Leu-Ser-Cys-Phe (P2), and Phe-Asn-Val-Pro-Leu-Tyr-Glu (P4) by time of flight-mass spectrometry/mass spectrometry (TOF-MS) analysis. The IC₅₀ values against ACE activity were 9.10 μM (P1), 10.77 μM (P2) and 7.72 μM (P4). The inhibition mode of P1, P2 and P4 was analyzed using the Lineweaver–Burk plots, demonstrating P1 to be a non-competitive inhibitor, P2 and P4 having a mixed inhibition mode. Taken together, the salmon byproduct protein hydrolysate and/or its active peptides can be used in foods for its benefits against hypertension and related diseases.     

利用食用菌菌渣饲养鸡冠细身赤锹形虫

探索利用食用菌菌渣饲养锹甲科环锹属鸡冠细身赤锹形虫Cyclommatus mniszechi幼虫的新技术,以期为食用菌菌渣的二次利用和锹甲科昆虫人工饲养繁殖提供参考。本实验置于25℃±1℃,相对湿度60%±5%的黑暗条件下,通过控制变量法筛选出适合鸡冠细身赤锹形虫幼虫生长发育的食用菌种菌渣。研究发现,白木耳菌渣灭菌组幼虫雌虫化蛹率为75. 00%,羽化率为75. 00%,雄虫化蛹率为100%,羽化率为33. 33%; 3龄幼虫中仍用白木耳非灭菌菌渣单独饲养的幼虫(雌虫和雄虫)(白木耳非灭菌组A)均不能化蛹羽化,后期用白木耳非灭菌菌渣∶发酵木屑=1∶1饲养的幼虫(雌虫和雄虫)(白木耳非灭菌组B)化蛹率和羽化率均为100%;且试验所得的雌虫均可正常繁殖产卵;白木耳非灭菌组B的雄虫的体重和各形态特征(包括体长、上颚长、上颚基宽、鞘翅长、鞘翅宽)与对照组均无显著差异,说明在一定程度上,白木耳菌渣可作为人工饲料饲养鸡冠细身赤锹形虫幼虫。     

Purification and identification of novel angiotensin-I converting enzyme (ACE) inhibitory peptides from cultured marine microalgae (Nannochloropsis oculata) protein hydrolysate

Isolation of bioactive compounds and commercialization of marine microalgae sources are interesting targets in future marine biotechnology. Cultured biomass of the marine microalga, Nannochloropsis oculata, was used to purify angiotensin-I converting enzyme (ACE) inhibitory peptides using proteases including pepsin, trypsin, α-chymotrypsin, papain, alcalase, and neutrase. The pepsin hydrolysate exhibited the highest ACE inhibitory activity, compared to the other hydrolysates and then was separated into three fractions (F1, F2, and F3) using Sephadex G-25 gel filtration column chromatography. First fraction (F1) showed the highest ACE inhibitory activity and it was further purified into two fractions (F1-1 and F1-2) using reverse-phase high-performance liquid chromatography. The IC₅₀ value of purified ACE inhibitory peptides were 123 and 173 μM and identified as novel peptides, Gly-Met-Asn-Asn-Leu-Thr-Pro (GMNNLTP; MW, 728 Da) and Leu-Glu-Gln (LEQ; MW, 369 Da), respectively. In addition, nitric oxide production level (%) was significantly increased by the purified peptide (Gly-Met-Asn-Asn-Leu-Thr-Pro) compared to the purified peptide (Leu-Glu-Gln) and other treated pepsin hydrolysate fractions on human umbilical vein endothelial cells (HUVECs). Cell viability assay showed no cytotoxicity on HUVECs with the treated purified peptides and fractions. These results suggest that the isolated peptides from cultured marine microalga, N. oculata protein sources may have potentiality to use commercially as ACE inhibitory agents in functional food industry.