Phytotherapy is the study of the use of extracts of natural origin as medicines or health-promoting agents. Phytotherapy medicines differ from plant-derived medicines in standard pharmacology. Where standard pharmacology isolates an active compound from a given plant, phytotherapy aims to preserve the complexity of substances from a given plant with relatively less processing.

Phytotherapy is distinct from homeopathy and anthroposophic medicine, and avoids mixing plant and synthetic bioactive substances. Traditional phytotherapy is a synonym for herbalism and regarded as alternative medicine by much of Western medicine. Although the medicinal and biological effects of many plant constituents such as alkaloids (morphine, atropine etc.) have been proven through clinical studies, there is debate about the efficacy and the place of phytotherapy in medical therapies.

Many herbs have shown positive results in-vitro, animal model or small-scale clinical tests,[1] while studies on some herbal treatments have found negative results.[2]

In 2002, the U.S. National Center for Complementary and Alternative Medicine of the National Institutes of Health began funding clinical trials into the effectiveness of herbal medicine.[3] In a 2010 survey of 1000 plants, 356 had clinical trials published evaluating their “pharmacological activities and therapeutic applications” while 12% of the plants, although available in the Western market, had “no substantial studies” of their properties.[4]

Even widely used remedies may not have undergone substantial clinical testing. In a review on herbal medicine in Malaria treatment, the authors found that “…better evidence from randomised clinical trials is needed before herbal remedies can be recommended on a large scale. As such trials are expensive and time consuming, it is important to prioritise remedies for clinical investigation….”[5]

Modern phytotherapy, following the scientific method, can be considered the study on the effects and clinical use of herbal medicines.


November 15, 2010

Kenneth Setchell

The importance of estrogens in homeostatic regulation of many cellular and biochemical events is well illustrated by the pathophysiologic changes that occur with estrogen deficiency. Many of the major diseases of Western populations are hormone dependent and epidemiologic data have shown a strong association between their incidence and diet. In particular, the importance of a plant-based diet is evident from the current dietary recommendations that emphasize an increase in the proportion and amount of fruit and vegetables that should be consumed. Although interpretation of the role of individual components of the diet is difficult from epidemiologic and dietary studies, it is recognized that there are many plant-derived bioactive nonnutrients that can confer significant health benefits. Among these phytochemicals is the broad class of nonsteroidal estrogens called phytoestrogens, and in the past decade there has been considerable interest in the role of isoflavones because of their relatively high concentrations in soy protein. The isoflavones in modest amounts of ingested soy protein are biotransformed by intestinal microflora, are absorbed, undergo enterohepatic recycling, and reach circulating concentrations
that exceed by several orders of magnitude the amounts of endogenous estrogens. These phytoestrogens and their
metabolites have many potent hormonal and nonhormonal activities that may explain some of the biological effects of diets rich in phytoestrogens


GardenBot is an open source garden monitoring system. This site is a collection of tutorials for how to build things (like a soil moisture sensor), software for running GardenBot, resources, links, and more.

To get started, you will want to browse the How-To section to see what is required to build the various modules.

The ultimate goal of the GardenBot project is to be a complete garden monitoring and automation system. A key design consideration  is to keep everything as easy as possible — especially for users new to Arduino and DIY electronics projects.


Trypsin (EC is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins.[2][3] Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerousbiotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.

Activation of trypsin from proteolytic cleavage of trypsinogen in the pancreas can lead to a series of events that cause pancreatic self-digestion, resulting in pancreatitis. One consequence of the autosomal recessive disease cystic fibrosis is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. This leads to the disorder termed meconium ileus. This disorder involves intestinal obstruction (ileus) due to overly thick meconium, which is normally broken down by trypsin and other proteases, then passed in feces.[7]

Trypsin is available in high quantity in pancreases, and can be purified rather easily. Hence it has been used widely in various biotechnological processes.

In a tissue culture lab, trypsin is used to re-suspend cells adherent to the cell culture dish wall during the process of harvesting cells.[8] Some cell types have a tendency to “stick” – or adhere – to the sides and bottom of a dish when cultivated in vitro. Trypsin is used to cleave proteins bonding the cultured cells to the dish, so that the cells can be suspended in fresh solution and transferred to fresh dishes.

Trypsin can also be used to dissociate dissected cells (for example, prior to cell fixing and sorting).

Trypsin can be used to break down casein in breast milk. If trypsin is added to a solution of milk powder, the breakdown of casein will cause the milk to become translucent. The rate of reaction can be measured by using the amount of time it takes for the milk to turn translucent.

Trypsin is commonly used in biological research during proteomics experiments to digest proteins into peptides for mass spectrometry analysis, e.g. in-gel digestion. Trypsin is particularly suited for this, since it has a very well defined specificity, as it hydrolyzes only the peptide bonds in which the carbonyl group is contributed either by an Arg or Lys residue.

Trypsin can also be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form.

In food

Commercial protease preparations usually consist of a mixture of various protease enzymes that often includes trypsin. These preparations are widely utilized in food processing:[9]

  • as a baking enzyme to improve the workability of dough;
  • in the extraction of seasonings and flavourings from vegetable or animal proteins and in the manufacture of sauces;
  • to control aroma formation in cheese and milk products;
  • to improve the texture of fish products;
  • to tenderize meat;
  • during cold stabilization of beer;
  • in the production of hypoallergenic food where proteases break down specific allergenic proteins into nonallergenic peptides. For example, proteases are used to produce hypoallergenic baby food from cow’s milk thereby diminishing the risk of babies developing milk allergies.

Trypsin inhibitor

Main article: Trypsin inhibitor

In order to prevent the action of active trypsin in the pancreas which can be highly damaging, inhibitors such as BPTI and SPINK1 in the pancreas and α1-antitrypsin in the serum are present as part of the defense against its inappropriate activation. Any trypsin prematurely formed from the inactive trypsinogen would be bound by the inhibitor. The protein-protein interaction between trypsin and its inhibitors is one of the tightest found, and trypsin is bound by some of its pancreatic inhibitors essentially irreversibly.[10] In contrast with nearly all known protein assemblies, some complexes of trypsin bound by its inhibitors do not readily dissociate after treatment with 8M urea.[11]


The cup is a unit of measurement for volume, used in cooking to measure liquids (fluid measurement) and bulk foods such as granulated sugar (dry measurement). It is principally used in the United States and Liberia where it is a legally defined unit of measurement. Actualcups used in a household in any country may differ from the cup size used for recipes; standard measuring cups, often calibrated in fluid measure and weights of usual dry ingredients as well as in cups, are available.

As a result of the fact that the imperial cup is actually out of use and the other definitions differ little (±3%), the U.S. measuring cups and metric measuring cups may be used as equal in practice.

No matter what size cup is used, the ingredients of a recipe measured with the same size cup will have their volumes in the same proportion to one another. The relative amounts to ingredients measured differently (by weight, or by different measures of volume such asteaspoons, etc.) may be affected by the definitions used.