乳源乳酸菌抗菌肽对鲜牛奶贮藏保鲜效果的影响

乳源乳酸菌抗菌肽抑菌广谱,稳定性高,且对生物体本身无害,其应用日益引起大量研究者的关注。本实验研究了乳源乳酸菌产抗菌肽对牛奶保鲜过程中产酸的抑制效果。实验结果表明:将抗菌肽添加到鲜牛奶中,贮存条件在4℃和25℃下都能有效地抑制牛奶中细菌增殖,而且牛奶的组织状态,感官质量良好。提示乳源乳酸菌抗菌肽在鲜牛奶贮藏保鲜中具有良好应用前景。     

Milk biologically active components as nutraceuticals: review

Milk contains components that provide critical nutritive elements, immunological protection, and biologically active substances to both neonates and adults. Milk proteins are currently the main source of a range of biologically active peptides. Concentrates of these peptides are potential health-enhancing nutraceuticals for food and pharmaceutical applications. Several bioactive peptides may be used as nutraceuticals, for example, in the treatment of diarrhea, hypertension, thrombosis, dental diseases, as well as mineral malabsorption, and immunodeficiency. Minor whey proteins, such as lactoferrin, lactoperoxidase, lysozyme, and immunoglobulins, are considered antimicrobial proteins. Milk also contains some natural bioactive substances. These include oligosaccharides, fucosylated oligosaccharides, hormones, growth factors, mucin, gangliosides, and endogenous peptides, which are present in milk at secretion. Most of the claimed physiological properties of milk bioactive components have been carried out in vitro or in animal model systems, and these hypothesized properties remain to be proven in humans. Whether these milk bioactive components will replace drugs entirely in the immediate future is still unclear, but the increasing appreciation of "drug foods" or nutraceuticals plays a complementary rather than a substitutional role to the synthetic pharmacological drugs.     

Identification of Anticancer Peptides from Bovine Milk Proteins and Their Potential Roles in Management of Cancer: A Critical Review

Cancer is the most widely recognized reason for human deaths globally. Conventional anticancer therapies, including chemotherapy and radiation, are very costly and induce severe side effects on the individual. The discovery of natural anticancer compounds like peptides may thus be a better alternative for cancer prevention and management. The anticancer peptides also exist in the amino acid chain of milk proteins and can be generated during proteolytic activities such as gastrointestinal digestion or food processing including fermentation. This paper presents an exhaustive overview of the contemporary literature on antitumor activities of peptides released from milk proteins. In addition, caseins and whey proteins have been evaluated for anticancer potential using the AntiCP database, a web‐based prediction server. Proline and lysine, respectively, dominate at various positions in anticancer peptides obtained from caseins and whey proteins. The remarkable number of potential anticancer peptides revealed milk proteins as favorable candidates for the development of anticancer agents or milk and milk products for reduction of cancer risks. Moreover, anticancer peptides liberated from milk proteins can be identified from fermented dairy products. Although current findings of correlation between dairy food intakes and cancer risks lack consistency, dairy‐derived peptides show promise as candidates for cancer therapy. This critical review supports the notion that milk proteins are not only a nutritious part of a normal daily diet but also have potential for prevention and/or management of cancer.     

概述乳制品加工中产生的生物活性肽

乳蛋白是许多生物活性肽的重要来源,主要的乳蛋白源生物活性肽有阿片样肽、降血压肽、免疫刺激肽、抗血栓肽和酪蛋白磷酸肽.文章对这些活性肽进行了介绍,并对乳制品(发酵乳和干酪)中的活性肽进行了讨论.乳制品中含有活性肽证明通过外源酶或微生物的作用可以将活性肽从乳蛋白中释放出来,这些肽的存在将促进乳制品的加工和消费.     

海洋生物抗菌肽研究进展及其在生物防治中的应用前景

抗菌肽是一种具有抗菌活性的生物短肽,广泛存在于生物界中。本文综述了抗菌肽的几种类型及作用机理,介绍了海洋生物抗菌肽的研究状况、存在的主要问题及其在生物防治中的应用前景。     

Peptides from milk proteins and their properties

This review has attempted to study the literature pertaining to peptides derived from milk proteins. Hydrolysis of milk proteins to generate peptides has been practiced for a long time and it was recognized early on in this process that the taste of hydrolyzates might hinder use of these products in food formulations. Modification of protein is necessary to form a more acceptable or utilizable product, to form a product that is less susceptible to deteriorative reactions and to form a product that is of higher nutritionall quality. Modifications may be achieved by a number of chemical and enzymatic means. This review has considered only enzymatic modification of dairy proteins. Modified proteins contain peptides and some of these peptides have been purified and their functionalities have been compared with unmodified proteins. This paper has examined the literature pertaining to improvement in functionality of enzyme-modified proteins. Improvements in solubility, emulsification, foaming and gelation were examined. There is limited information available on the sequence of the peptides necessary to improve the functional characteristics of proteins. Knowing the sequences of desirable functional peptides can lead to genetic alteration of proteins to improve functionality. Addition of synthetic peptides to intact proteins may be another way in which the functionality of proteins can be augmented. Some of the peptides in milk proteins are capable of affecting biological functions of an organism. These effects can be antimicrobial and probiotic, i.e., prevent the growth and proliferation of undesirable and pathogenic organisms, or they may promote the growth of desirable bacteria in the digestive tract of humans and animals. Peptides derived from milk protein have been shown to exert digestive and metabolic effects as well. They may also influence the immune system. These biological effects may play an important role in the development of medical foods that treat or mitigate the effects of diseases. Proteins are allergens and therefore it is possible that products derived from modification of proteins may also be allergens. The known literature about the allergenicity of peptides derived from milk proteins has been examined in this article. Last, but not the least, the taste attributes of peptides is also considered. Bitterness of hydrolyzates is a common occurrence and the origins of these bitter peptides and possible ways of mitigating this sensory defect has been discussed. Many of the peptides that enhance functionality and exert biological activity are likely to be bitter. Therefore, the bitter taste of hydrolysis products has to be dealt with in boosting the functional or nutraceutical aspects of foods containing these peptides. Analytical techniques for sequencing peptides have become more accessible and purification of peptides is commercially feasible. Computer based modeling techniques have aided the prediction of structures in these peptides. These advances, coupled with the advances in biotechnology, promise to revolutionize the future of nutraceutical and functional foods.     

Molecular Characterization and Identification of Bioactive Peptides Producing Lactobacillus sps. Based on 16S rRNA Gene Sequencing

In the present study, 3 bacterial cultures were isolated from faecal samples of human infant. The biochemical traits showed similarity with Lactobacillus sps and 16S rRNA sequence analyses, confirmed as Lactobacillus plantarum, Lactobacillus casei, and Lactobacillus rhamnosus. The cultures were screened for their proteolytic activity and good ability to release peptides from milk proteins was found. Hence, these bacteria were used as a proteolytic starter culture for the fermentation of skim milk and whey for the liberation of small peptides. Bioactive nature of the peptides released from whey and skim milk was tested, and results demonstrated that peptides obtained after fermentation of whey and skim milk by Lactobacillus strains showed antimicrobial activity against all the pathogens causing food borne infections in humans. These peptides also indicated antioxidant as well as ACE (angiotensin-converting enzymes) inhibitory activity.     

Functional Significance of Bioactive Peptides Derived from Milk Proteins

Bioactive peptides can be defined as protein fragments with potential biological activities. Milk proteins are precursors of many different biologically active peptides. Bioactive peptides from milk proteins are considered potential modulators of various regulatory processes in the body. They mediate physiological functions in cardiovascular, nervous, gastro intestinal and immune systems. The functional significance of bioactivities depends on peptide fragment. Bioactive peptides encrypted in major milk proteins are latent within the sequence of the parent protein molecule. They can be liberated by (i) gastro intestinal digestion of milk, (ii) fermentation of milk with proteolytic starter cultures, and (iii) hydrolysis by proteolytic enzymes. In relation to their mode of action, bioactive peptides may reach target sites at the luminal side of intestinal tract, or after absorption, in peripheral organs. The production, functionalities, and mode of action of bioactive milk peptides as well as latest peptide products and ingredients are reviewed.     

Antimicrobial peptides generated from milk proteins: a survey and prospects for application in the food industry. A review

Milk proteins constitute a natural reservoir of bioactive peptides with physiological and/or antimicrobial properties, the release of which requires hydrolysis of the precursor molecules by digestive proteases or by fermentation with proteolytic micro‐organisms. Depending on the digestive or microbial proteases used, an array of bioactive peptides would be released either from caseins or whey proteins, but only a small part of these peptides has so far been identified and characterised with respect to their antimicrobial activity. The antimicrobial peptides known thus far have proven to be potent inhibitors to the growth of a wide range of undesirable micro‐organisms of health or spoilage significance. Nevertheless, previous research work has largely been oriented towards their possible application in medicine, which has hindered their high potential as food‐grade biopreservatives and/or as supplements in functional foods. This review attempts to study the literature pertaining to antimicrobial peptides derived from major milk proteins (caseins, α‐lactalbumin and β‐lactoglobulin) upon hydrolysis either by digestive proteases or by fermentation with proteolytic lactic acid bacteria. Their possible application in the food industry and their mechanism of action will also be discussed. Reference antimicrobial peptides produced by living micro‐organisms as innate immune defence components against microbial infections will occasionally be invoked for comparison purposes.     

乳源活性肽的研究进展

近年来，对肽的作用做了大量的研究工作，证实乳蛋白是许多生物活性肽的重要来源，主要的乳蛋白源生物活性肽有阿片样肽、抗菌肽、免疫刺激肽、抗血栓肽和矿质元素结合肽等。文章对这些活性肽的作用进行了介绍，并根据研究现状，对如何制备、纯化和分析活性肽做了简要的综述。     

Initial proteolysis of milk proteins and its effect on formation of ACE-inhibitory peptides during gastrointestinal proteolysis: a bioinformatic, in silico, approach

Angiotensin-I-converting enzyme (ACE)-inhibitory peptides are encrypted in milk protein sequences. They may express an antihypertensive effect if they are released by proteolysis in foods and/or during gastrointestinal digestion. A bioinformatic, in silico, approach was developed to evaluate how systematic initial proteolysis, i.e. cleavage after one specific type of amino acid (C-end) at a time in milk proteins, influence the formation of ACE-inhibitory peptides by subsequent gastrointestinal proteolysis. Computer simulation was done and a peptide QSAR model was used to estimate the combined ACE inhibition by digested proteins. Initial proteolytic cleavage at the C-end of amino acids isoleucine and proline gave, based on calculations, increased effect of ACE-inhibitory peptides after gastrointestinal proteolysis of milk proteins. Cleavage after most other amino acid residues had little or no effect. Results indicate that initial proteolysis in foods have to be specific in order to increase formation of bioavailable ACE-inhibitory peptides during gastrointestinal digestion.     

几种豆科植物抗菌肽的生物信息学预测与分析

植物抗菌肽是存在于植物组织细胞中的一类对于对外来侵害有防御作用的小分子蛋白,可抑制或杀伤多种细菌和真菌。随着人们健康意识的提高以及技术手段的进步,植物来源抗菌肽的发掘和应用逐渐成为食品开发领域的重要研究方向。该试验从蛋白数据库中筛选了7种豆科植物的抗菌肽,并对其蛋白序列进行了比对和系统进化树分析,结合生物信息学研究工具对豆科植物抗菌肽的疏水性、拓扑结构域、蛋白空间结构和亚细胞定位进行了预测和分析。结果表明,7种豆科植物抗菌肽序列相似度达到71.94%,均具有8个半胱氨酸保守位点;豆科植物抗菌肽为碱性膜结合蛋白,分布于液泡膜、细胞核膜或者细胞膜上;其3D结构均由一组β-折叠和一个α-螺旋组成,与硫堇、植物防卫素蛋白结构相似。     

Antioxidative and antibacterial peptides derived from bovine milk proteins

The search for alternative preservatives is on the rise due to safety issues linked with the application of synthetic antioxidants and the extensive increase in bacterial resistance to several conventional antibiotics. Therefore, the quest for finding suitable alternatives including bioactive peptides has received attention. This article reports a comprehensive insight concerning antioxidative and antibacterial peptides derived from milk proteins, a prolific source of peptides having various bioactivities. Caseins and whey proteins have also been evaluated for antioxidative and antibacterial potential using the BIOPEP database. A notable number of potentially active peptides are present in milk proteins. Technological approaches are here reported for the production of these peptides. The findings of this review show potentiality of utilizing dairy derived antioxidative and antibacterial peptides in the development of a superior alternative to the current generation of preservatives and therapeutic agents, as well as a functional ingredient in dietetic or pharmaceutical applications.     

Milk proteins and their derived peptides on bone health: Biological functions,mechanisms, and prospects

Bone is a dynamic organ under constant metabolism (or remodeling), where a delicate balance between bone resorption and bone formation is maintained. Disruption of this coordinated bone remodeling results in bone diseases, such as osteoporosis, the most common bone disorder characterized by decreased bone mineral density and microarchitectural deterioration. Epidemiological and clinical evidence support that consumption of dairy products is beneficial for bone health; this benefit is often attributed to the presence of calcium, the physiological contributions of milk proteins on bone metabolism, however, are underestimated. Emerging evidence highlighted that not only milk proteins (including individual milk proteins) but also their derived peptides positively regulate bone remodeling and attenuate bone loss, via the regulation of cellular markers and signaling of osteoblasts and osteoclasts. This article aims to review current knowledge about the roles of milk proteins, with an emphasis on individual milk proteins, bioactive peptides derived from milk proteins, and effect of milk processing in particular fermentation, on bone metabolism, to highlight the potential uses of milk proteins in the prevention and treatment of osteoporosis, and, to discuss the knowledge gap and to recommend future research directions.     

Prevention of lipid oxidation in muscle foods by milk proteins and peptides: A review

Muscle foods (especially fresh meat, precooked, and restructured meat products) are highly prone to lipid oxidation, which ultimately leads to certain problems, viz. discoloration, off-flavor, drip losses, loss of essential fatty acids and vitamins, and generation of toxic products. These problems can be minimized with the help of various agents and or techniques such as use of natural/synthetic antioxidants, metal chelating agents, physical conditions, vacuum packaging, and encapsulation techniques. Among these, the role of synthetic antioxidants is quite debatable due to certain health risks to humans. Among the natural molecules, milk proteins and their bioactive peptides offer a promising potential for the meat industry. Various forms of milk proteins and peptides including caseinates, whey proteins, skim milk, and milk co-precipitates can be used to prevent lipid oxidation in meat products either in the form of added ingredients or as edible coatings. However, in addition to prevention of lipid oxidation, they also provide nutritional benefits and improve the technological processing and shelflife of meat and meat products. This review focuses on the utilization, mechanism of action, and efficacy of milk proteins and peptides to inhibit lipid oxidation in muscle food products.     

Enzymatic Production,Bioactivity, and Bitterness of Chickpea (Cicer arietinum) Peptides

Chickpeas are inexpensive, protein rich (approximately 20% dry mass) pulses available worldwide whose consumption has been correlated with positive health outcomes. Dietary peptides are important molecules derived from dietary proteins, but a comprehensive analysis of the peptides that can be produced from chickpea proteins is missing in the literature. This review provides information from the past 20 years on the enzymatic production of peptides from chickpea proteins, the reported bioactivities of chickpea protein hydrolysates and peptides, and the potential bitterness of chickpea peptides in food products. Chickpea peptides have been enzymatically produced with pepsin, trypsin, chymotrypsin, alcalase, flavorzyme, and papain either alone or in combination, but the sequences of many of the peptides in chickpea protein hydrolysates remain unknown. In addition, a theoretical hydrolysis of chickpea legumin by stem bromelain and ficin was performed by the authors to highlight the potential use of these enzymes to produce bioactive chickpea peptides. Antioxidant activity, hypocholesterolemic, and angiotensin 1‐converting enzyme inhibition are the most studied bioactivities of chickpea protein hydrolysates and peptides, but anticarcinogenic, antimicrobial, and anti‐inflammatory effects have also been reported for chickpea protein hydrolysates and peptides. Chickpea bioactive peptides are not currently commercialized, but their bitterness could be a major impediment to their incorporation in food products. Use of flavorzyme in the production of chickpea protein hydrolysates has been proposed to decrease their bitterness. Future research should focus on the optimization of chickpea bioactive peptide enzymatic production, studying the bioactivity of chickpea peptides in humans, and systematically analyzing chickpea peptide bitterness.     

成熟温度和时间对牦牛乳硬质干酪中生物活性肽的影响

以不同条件成熟的牦牛乳硬质干酪为研究对象,探究成熟温度和时间对牦牛乳硬质干酪中水溶性多肽的DPPH自由基清除能力、抑菌性以及抑制血管紧张素转换酶（ACE）活性的影响。结果表明,5 ℃、10 ℃、15 ℃成熟4～6个月牦牛乳硬质干酪的水溶性多肽对DPPH自由基均有清除能力。5 ℃、10 ℃成熟5个月、15 ℃成熟4个月牦牛乳硬质干酪的水溶性多肽对DPPH自由基清除率最高,分别为（20.38±1.20）%、（28.70±0.67）%和（30.19±0.32）%。5 ℃、10 ℃、15 ℃成熟的牦牛乳硬质干酪在4～6个月成熟过程中,其水溶性多肽对大肠杆菌、金黄色葡萄球菌的抑制程度分别呈增强趋势。成熟温度从5 ℃提高到15 ℃时,牦牛乳硬质干酪的水溶性多肽对大肠杆菌、金黄色葡萄球菌和血管紧张素转换酶的抑制作用呈加强趋势。     

Therapeutic potential of dairy bioactive peptides: A contemporary perspective

Dairy products are associated with numerous health benefits. These are a good source of nutrients such as carbohydrates, protein (bioactive peptides), lipids, minerals, and vitamins, which are essential for growth, development, and maintenance of the human body. Accordingly, dairy bioactive peptides are one of the targeted compounds present in different dairy products. Dairy bioactive compounds can be classified as antihypertensive, anti-oxidative, immmunomodulant, anti-mutagenic, antimicrobial, opoid, anti-thrombotic, anti-obesity, and mineral-binding agents, depending upon biological functions. These bioactive peptides can easily be produced by enzymatic hydrolysis, and during fermentation and gastrointestinal digestion. For this reason, fermented dairy products, such as yogurt, cheese, and sour milk, are gaining popularity worldwide, and are considered excellent source of dairy peptides. Furthermore, fermented and non-fermented dairy products are associated with lower risks of hypertension, coagulopathy, stroke, and cancer insurgences. The current review article is an attempt to disseminate general information about dairy peptides and their health claims to scientists, allied stakeholders, and, certainly, readers.     

Food‐derived immunomodulatory peptides

Food proteins contain specific amino acid sequences within their structures that may positively impact bodily functions and have multiple immunomodulatory effects. The functional properties of these specific sequences, also referred to as bioactive peptides, are revealed only after the degradation of native proteins during digestion processes. Currently, milk proteins have been the most explored source of bioactive peptides, which presents an interesting opportunity for the dairy industry. However, plant‐ and animal‐derived proteins have also been shown to be important sources of bioactive peptides. This review summarizes the in vitro and in vivo evidence of the role of various food proteins as sources of immunomodulatory peptides and discusses the possible pathways involving these properties. © 2016 Society of Chemical Industry     

A New Frontier in Soy Bioactive Peptides that May Prevent Age‐related Chronic Diseases

During gastrointestinal digestion or food processing of proteins, small peptides can be released and may act as regulatory compounds with hormone‐like activities. Numerous biologically active peptides (bioactive peptides) have been identified. Most bioactive peptides are derived from milk and dairy products, with the most common being angiotensin converting enzyme inhibitory peptides. Soybean protein and soybean derived peptides also play an important role in soybean physiological activities, particularly those related to the prevention of chronic diseases. However, the bioactive potential of soybean derived bioactive peptides is yet to be fully appreciated. After a general introduction of approaches and advances in bioactive peptides from food sources, this review focuses on bioactive peptides derived from soybean proteins and their physiological properties. Technological approaches to generate bioactive peptides, their isolation, purification, characterization, and quantification, and further application in food and drug design are also presented. Safety concerns, such as potential toxicity, allergenicity, and sensory aspect of these peptides are likewise discussed.