[Frontiers in Bioscience S3, 286-297, January 1, 2011]

Tryptophan metabolism in animals: important roles in nutrition and health

Kang Yao1,2,3, Jun Fang2 , Yu-long Yin1, Ze-Meng Feng 1,4, Zhi-Ru Tang1, Guoyao Wu1,3,5
1
Hunan Engineering and Research Center of Animal and Poultry Science and Key Laboratory for Agro-ecological Processes in
Subtropical Region, Institute of Subtropical Agriculture, Chinese Academy of Sciences, Hunan, China 410125,2College of
Bioscience and Biotechnology, Hunan Agricultural University, Changsha, China 410125,3Department of Animal Science, Texas
A&M University, College Station, TX, USA 77843-2471,4Graduate School of the Chinese Academy of Sciences, Beijing 100039,
China, 5State Key Laboratory of Animal Nutrition, China Agricultural University, Beijing, China 100193 *correspondence author

TABLE OF CONTENTS

1. Abstract
2. Introduction
3. Metabolism and nutrition of tryptophan in animals
3.1. Pathways of tryptophan metabolism
3.2. Tryptophan metabolites
3.3. Tryptophan and immunity
3.4. Tryptophan and neurological function
3.5. Dietary requirements of tryptophan
3.6. Safety of oral tryptophan and its metabolites
4. Summary and perspectives
5. Acknowledgements
6. References

1. ABSTRACT 2. INTRODUCTION

L-Tryptophan is a nutritionally essential amino L-Tryptophan (TRP;

acid for monogastric animals and preweaning ruminants L-α-aminoindole-3-propionic acid) is a nutritionally
because it cannot be synthesized in the body. Besides essential amino acid for monogastric animals (e.g., humans,
serving as a building block for proteins, tryptophan is a pigs, dogs, rats, mice, and chickens) and preweaning
critical nutrient for the functions of nervous and immune ruminants (e.g., calves and lambs) due to the lack of
systems. Over the past decades, much attention has been endogenous synthesis (1). It is a white powder and a
directed to study the role of tryptophan as a limiting amino neutral amino acid with the pI value of 5.96 [pKa (α-COOH)
acid in mammalian and avian nutrition. However, = 2.46; pKa (α-NH3+ = 9.41). TRP was first isolated from
emerging evidence from recent studies shows that casein in 1902 by F.G. Hopkins using base hydrolysis.
tryptophan and its metabolites [e.g., serotonin Like some amino acids (e.g., homocysteine and cysteine),
(5-hydroxytryptamine, 5-HT) and melatonin)] can regulate TRP binds non-covalently with serum albumin. The primary
feed intake, reproduction, immunity, neurological function, function of TRP is to serve as a building block in protein
and anti-stress responses. Additionally, tryptophan may biosynthesis. However, TRP’s metabolites are key
modulate gene expression and nutrient metabolism to neurotransmitters, thereby regulating immune responses
impact whole-body homeostasis in organisms. Thus, and the function of the nervous system (1). Thus, TRP
adequate intake of this amino acid from the diet is crucial plays an important role in metabolism, physiology, growth
for growth, development, and health of animals and and development of organisms (2). The aim of this review is
humans. to highlight recent developments in TRP metabolism and

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nutrition, with particular reference to the regulation of feed the common nitrogenous substrate. Therefore, competition
intake, reproduction, immunity, growth, neurological for TRP exists between nicotinic acid and serotonin
function, and anti-stress response. synthesis in animals. Proinflammatory cytokines can
induce IDO under stressful or disease conditions, activate
3. METABOLISM AND NUTRITION OF TRP IN the KYN pathway, and reduce 5-HT synthesis (8).
ANIMALS
3.2. TRP metabolites
3.1. Pathways of TRP metabolism Nitrogenous products of TRP catabolism include
Two sources contribute to the free TRP pool in serotonin, N-acetylserotonin, melatonin, anthranilic acid,
plasma: the diet and intracellular protein degradation. and ammonia (1). Serotonin is a biogenic amine which
They provide approximately 1/3 and 2/3 of the TRP’s functions as: (a) a neurotransmitter; (b) a regulator of
whole-body flux, respectively. Because TRP is not gastrointestinal secretion, motility, and sensation; (c) a
synthesized by animal cells, the diet is the ultimate source modulator of cognition, sleep, mood, and appetite; and (d) a
of this amino acid in the body. In monogastric animals, mediator of a number of neurological diseases [e.g., mental
microbes in the lumen of the large intestine can ferment disorders (2,9-11)]. At elevated concentrations, serotonin
undigested foods and produce TRP. However, this is capable of promoting oxidative stress in cellular systems
synthetic event provides little TRP to the host because the or tissues (12). There is also evidence that an increase in
amount is quantitatively small and the absorption of TRP by serotonin synthesis can be a sensitive biomarker of
colonocytes is limited. Thus, monogastric animals cannot oxidative stress and the generation of reactive
grow or maintain a positive nitrogen balance when fed a oxygen/nitrogen species (11,12). Serotonin can also act
TRP-free diet (1). TRP is metabolized via three pathways in through specific membrane receptors involved in numerous
mammals: (a) hydroxylation and decarboxylation of TRP to physiological functions (1,2). Interestingly, exogenous
generate serotonin (5-hydroxytryptamine, 5-HT); (b) serotonin can increase fecal pellet output in rats and cause
deamination and decarboxylation of TRP to yield diarrhea in mice (13).
indoleacetic acid; and (3) degradation of TRP to niacin,
pyruvate and acetyl-CoA through kunurenine formation Melatonin is a versatile and ubiquitous hormonal
(Figure 1). Nicotinamide, serotonin and melatonin molecule (14). It is widely distributed throughout the body,
(N-acetyl- 5-methoxytryptamine) are important bioactive especially in the gastrointestinal tract (15) where melatonin
compounds derived from TRP (2). In healthy adult is produced by mucosal enteroendocrine cells. Melatonin
mammals, over 95% of the ingested TRP is catabolized exerts strong anti-inflammatory effects due to an inhibition
primarily in the liver via the kynurenine (KYN) pathway. of NF-kB and TNF-α expression (16). Melatonin and TRP
However, only 1–2% and 2-3% of dietary TRP are show strong protective efforts on the gastric mucosa and
converted into serotonin (mainly in the small intestine but, accelerate ulcer healing, while stimulating pancreatic
to a much lesser extent, other tissues including the lactating exocrine function via mechanisms involving
mammary gland) and indoleacetic acid (mainly in the enteropancreatic reflexes and cholecystokinin (CCK) (17).
gastrointestinal tract and liver), respectively (3-5). The Additionally, melatonin and TRP may limit or reverse some
gastrointestinal tract contains 80-90% of serotonin in the of the changes that occur in age-related sleep-wake rhythms
body. and body temperatures (18).

The first and rate-controlling step in this pathway Metabolites of the KYN pathway have either
(namely the conversion of TRP to KYN) is catalyzed by neurotoxic or neuroprotective activities depending on
either the ubiquitous indoleamine 2, 3-dioxygenase (IDO) products, in that 3-hydroxykynurenine and quinolinic acid
(4, 5) or TRP 2, 3-dioxygenase (TDO) which is primarily are neurotoxic whereas kynurenic acid is neuroprotective
localized to the liver (6). Notably, tetrahydrobiopterin is an (8). For example, quinolinic acid, as one of the
essential cofactor for IDO, TDO, and TRP hydroxylase. metabolites of TRP produced along an alternative branch of
The expression of IDO is strongly influenced by the state of the KYN pathway, has excitotoxic properties in the brain
the immune system in that IDO activity is potently induced and the peripheral nervous system due to: (a) potent action
by inflammatory cytokines (e.g., interferon-γ) and on NR2A and NR2B; (b) activation of N-methyl-D-aspartic
endotoxin. In contrast, TDO activity is increased by TRP acid (NMDA) receptor subtypes; and (c) an ability to
and its analogues via an allosteric binding site, but is generate free radicals independently of receptor-mediated
competitively inhibited by some common indoleamines, mechanisms (19). Of particular note, physiological
including tryptamine (6). concentrations of kynurenic acid acts as an antagonist of
ionotropic glutamate receptors (20,21) and an NMDA
Metabolism through the KYN pathway primarily receptor antagonist through its competitive blockade of the
results in the formation of quinolinic acid, particularly via glycine co-agonist site (19). However, pathological levels of
the production of 3-hydroxykynurenine and kynurenic acid contribute to the pathogenesis of
3-hydroxyanthranilic acid. Quinolinic acid may be neurological diseases by interfering with membrane
metabolized further to nicotinamide or nicotinic acid (7). receptors and cell signaling (22-25).
The kynurenine pathway also produces kynurenic acid,
picolinic acid, 5-hydroxyanthranilic acid, and xanthurenic Niacin is a component of nicotinamide adenine
acid, leading to the generation of pyruvate and acetyl-CoA. dinucleotide (NAD) and nicotinamide adenine dinucleotide
The KYN- and serotonin-synthetic pathways share TRP as phosphate (NADP) (1).Nicotinic acid (nicotinate) is the form

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Figure 1. L-Tryptophan catabolism in animals. Degradation of L-tryptophan is initiated by indoleamine 2, 3-dioxygenase,

tryptophan 2, 3-dioxygenase, and tryptophan hydroxylase. Important products include NAD, serotonin, melatonin, kynurenine,
indoles, and acetyl-CoA. L-tryptophan is both a ketogenic and glucogenic amino acid.

of niacin required for the synthesis of NAD and NADP by 3.3. TRP and immunity
enzymes present in the cytosol of most cells. NAD and NADP A new, exciting development in TRP research is
are coenzymes for many oxidoreductase enzymes involved that TRP metabolism is altered markedly in immune cells
in the metabolism of nutrients (e.g., carbohydrate, fatty acids, and many of other cell types (e.g., neurons) in response to
and amino acids) and exogenous substances (e.g., alcohol). proinflammatory cytokines. This new knowledge may help
In addition, NAD is as a substrate for poly(ADP-ribose) explain the etiological and pathophysiological mechanisms
polymerase which catalyzes the attachment of ADP-ribose responsible for impaired immunity and depression in
to various chromosomal proteins, thereby participating in subjects under stressful conditions (8). Most of indolic
the post-translational modifications of a variety of proteins. compounds in living organisms are derived from TRP.
Thus, nicotinamide is essential for normal physiological These TRP products are not sensitive to nitric oxide, oxygen
function through the formation of NAD(P) and redox or superoxide anion, but react directly with other reactive
reactions in all cells. oxygen and reactive nitrogen species, yielding various
derivatives (26-28). Additionally, TRP metabolites may

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contribute to pathological alterations in diabetes (27) and animals when the sanitary quality of environment is
the KYN pathway has been identified as a potential source compromised. Additionally, poor sanitary conditions lead to
of biomarkers for the irritable bowel syndrome (28). alterations of TRP metabolism, therefore reducing that the
amount of TRP available for growth and other metabolic
As noted previously, IDO can affect serotonergic functions in the host (55). Similarly, the induction of TRP
and glutamatergic functions through immune activation, degradation by inflammatory agents results in reduced
including infection and autoimmunity (29). This enzyme growth of pathogens and cancer cells by depriving them of
also has a complex role in pregnancy, transplantation, and TRP (4). TRP deficiency also occurs in people with
neoplasia (15,30-32). For example, exerting a fine control wounds (56) due to elevated catabolism of TRP via the
over inflammatory and adaptive antifungal responses can KYN pathway. Thus, while KYN production plays an
suppress the growth of intracellular bacteria, viruses, and important role in mediating tolerance to infection (57), TRP
parasites (5, 33, 34), as well as mediate the supply from the diet may be augmented in response to
inflammatory–anti-inflammatory state of dendritic cells in immunological challenges.
response to Candida and Aspergillus infection (35,36). The
IFN-γ–IDO axis may also accommodate fungal persistence Oral administration of TRP (125 mg/kg body
in the host (37). Moreover, the expression of IDO is weight) enhanced the phagocytic activity of macrophages
regulated by factors produced in the immune system, with and detoxification of superoxide anion radicals derived
IFNγ and TNFα being the main inducers. Interestingly, IDO from immune cells, possibly through the generation of
is expressed in nearly all human cells in response to immunoregulatory molecules, serotonin, and melatonin (58).
stimulation by these cytokines. Furthermore, IDO In a porcine model of dextran sodium sulfate (DSS)-induced
expression is regulated by other immunologically active colitis, oral administration of TRP could reduce
molecules such as prostaglandins (38) and the surface inflammation and enhance the rate of recovery from the
proteins CTLA4 (39), CD40 (40), and toll-like receptors disease (59). The TRP treatment also decreased the
(TLR) (41). Activation of IDO results in a decreased expression of proinflammatory cytokines [including TNF-α,
availability of TRP, which can inhibit T-cell proliferation interleukin (IL)-6, interferon (IFN)-γ, IL-12p40, IL-1β,
(42). A particularly high IDO activity can lead to a nearly IL-17, and IL-8] and intracellular adhesion molecule-1 (59).
complete depletion of TRP at the site of infection, which These findings indicate that TRP may be an effective
arrests the growth of several TRP-dependent immunomodulatory agent for the treatment of the irritable
microorganisms (43,44). Histochemical studies revealed the bowel syndrome (59)
presence of IDO in female reproductive organs and
alterations of its expression during pregnancy, a 3.4. TRP and neurological function
physiological event that is associated with immunological Like other essential amino acids, TRP must be
activation in the placenta and uterus (45). Interestingly, supplied in the diet to support the growth, development, and
concentrations of KYN and TRP in plasma reflect poorly function of the brain and peripheral nervous organs (1). TRP
IDO expression in the conceptus during early gestation, but is transported into neurons by neutral amino acid carriers
a closer relationship was detected during the last month of which are also shared by other large neutral amino acids
pregnancy in humans (45-48). This is likely due to (phenylalanine, leucine, isoleucine, tyrosine and valine)
multiple factors that regulate TRP absorption and (61). Through changes in serotonergic activity, TRP has
catabolism, intracellular protein turnover, and excretion of been implicated in the regulation of synthesis of key
KYN from the body. neurotransmitters (1, 60). Thus, TRP has been used to treat
neurological disorders, including depression, schizophrenia,
3-Hydroxy-DL-kynurenine and α-picolinic acid dysregulation of food intake, and other neuropsychiatric
may contribute to the anti-infectious activity of allografts by diseases (1).
directly inhibiting the growth of microorganisms (49). The An appropriate balance of dietary amino acids is
antimicrobial mechanism of 3-hydroxy-DL-kynurenine is important for neuronal TRP metabolism and thus the
unknown but may involve blockage of protein synthesis. function of the nervous system. For example, serotonin
In contrast, there is evidence that deprivation of iron by synthesis depends on extracellular concentrations of both
α-picolinic acid is attributable to its direct antimicrobial TRP and other large neutral amino acids because they
activity (50). This raises an important question of whether compete with TRP for transport across the blood-brain
TRP in the lumen of the gastrointestinal tract may be barrier. When serum TRP concentrations are elevated, the
beneficial for controlling microbial population and availability of TRP in the brain and other organs is increased,
numbers. resulting in enhanced synthesis of serotonin in serotonergic
neurons and pinealocytes of the pineal gland (62). Thus,
In patients with multiple trauma, TRP deficiency oral administration of TRP enhances serotonin levels in
has been found to be associated with the decline of both plasma and different brain regions (63). Conversely,
lymphocyte numbers (51) as a result of IDO activation (52). dietary deficiency of TRP leads to low levels of brain
Inflammatory conditions are associated with increased TRP serotonin (64) and altered neurological function (65).
catabolism and decreased TRP availability in cells (53). Acutely lowering serotonin synthesis by TRP depletion
For example, Increases in IDO activity and TRP promoted the intake of sweet-tasting foods by overweight
incorporation into acute phase proteins could explain TRP individuals due to serotonergic involvement in the control
deficiency in pigs suffering from chronic lung inflammation of food consumption (66). Hydrolyzed protein could
(54). A moderate inflammatory response is evident in augment brain TRP and serotonin levels, therefore

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improving mood and cognitive reactivity to depression (67). protein-bound TRP (89,90), but compelling evidence is
Additionally, oral administration of TRP (150-300 mg/kg) required to test this hypothesis. Nonetheless, dietary
to rats and chicks results in a rapid and dose-dependent supplementation with TRP is effective in increasing growth
elevation of melatonin in plasma (68, 69). Also, TRP performance and feed efficiency in young pigs fed a
supplementation may ameliorate poor appetite in human TRP-deficient diet.
subjects (70).
3.6. Safety of oral TRP and its metabolites
3.5. Dietary requirements of TRP TRP is widely available on the market as a
Accurate data on dietary TRP requirements by supplement for both animals and humans. However, there
animals and humans critically depend on accurate analysis have been concerns that excess administration of TRP may
of TRP in diets. Unfortunately, many investigators did not cause oxidative stress in the cerebral cortex (91), as well as
determine TRP content in experimental diets for animals or other adverse effects, including ataxia, tremors, diaphoresis,
humans due to its complete loss under conditions of acid blurred vision, dry mouth, muscle stiffness, palpitations,
hydrolysis. Based on nitrogen balance studies, urticaria, and the “eosinophilia–myalgia syndrome” (EMS)
good-quality protein intake and TRP intake of healthy adult (92-97). However, some of these side effects might have
subjects (both men and women) could be recommended at been caused by contaminated substance(s) in the former
0.8 g and 4 mg/day per kg body weight, respectively (67). TRP preparations, but not TRP itself. Two lines of
There has been much research on TRP requirements by evidence indicate that growing-finishing pigs (79-119 kg
poultry, pigs, cattle and sheep because they are body weight) pigs can tolerate considerable excesses of TRP
agriculturally important species worldwide (70-79). This and that oral ingestion of TRP is safe for swine. First,
work has made important contributions towards enhancing supplementing 0.1 or 1% TRP to a typical com- and
the efficiency of nutrient utilization by animals. soybean meal-based diet did not adversely affect growth
performance or blood variables (leukocyte and eosinophil
TRP is considered as the third or fourth limiting counts, as well as activities of aspartate transferase, creatine
amino acid in typical corn- and soybean meal-based diets phosphokinase, and lactate dehydrogenase). Second,
for young pigs after lysine, methionine, and threonine (73). mortality did not occur in pigs receiving acute intragastric
TRP deficiency reduces food intake, protein synthesis rate, administration of TRP at doses of 2 and 5.71 g/kg body
RNA activity, and growth in undernourished early-weaned weight. TRP excretion and the ratio of anthranilic acid to
piglets (73,77). Interestingly, piglets are able to detect kynurenic acid in urine could be useful indicators of
metabolic changes induced by TRP deficiency and respond excessive TRP intake (94).
with an aversion against the TRP-deficient diet (74).
Feeding a TRP-supplemented diet to pigs increased feed 5-Hydroxy-L-tryptophan (5-HTP), an
intake, the amounts of Cl- and H+ secreted from the intermediate in the biochemical synthesis of serotonin from
intestinal mucosa, efficiency of nutrient utilization for TRP, is a popular dietary supplement for humans. This
protein accretion, and growth performance, when compared TRP metabolite may ameliorate depression, improve the
with unsupplemented controls (74,77,78). The TRP debilitating symptoms of fibromyalgia, aid in weight loss,
supplementation may also reduce aggression and alleviate reduce blood pressure, prevent headaches, and treat
stress in many species, including pigs (78) and chickens insomnia (98-100). Dietary supplementation with 5-HTP
(79). Notably, oral ingestion of TRP enhanced plasma may be beneficial for subjects who could not tolerate a large
concentrations of ghrelin [a gastrointestinal hormone which dose of TRP. An important difference between TRP and
regulates food intake in both piglets and lactating sows 5-HTP is that 5-HTP can act as an antioxidant whereas
(71,80)] and serotonin (81) in pigs. excess TRP can cause oxidative damage (98). Oral 5-HTP is
well absorbed and can be taken with meals (99).
The current NRC recommendations for the Additionally, 5-HTP easily crosses the blood-brain barrier
requirements of dietary TRP (total TRP in diets) by swine and is readily transported by neurons (99). There is no
were based on a summary of studies published by various evidence to implicate 5-HTP as a cause of the EMS or
scientists (82-88). The values are 0.27, 0.24, 0.21, 0.17, 0.14, related disorders (100).
and 0.11% of diets for pigs weighing 3-5, 5-10, 10-20,
20-50, 50-80, and 80-120 kg, respectively (82). In the 4. SUMMARY AND PERSPECTIVES
ideal protein, lysine is used as a reference amino acid
relative to requirements of other amino acids. A ratio of Tryptophan plays versatile roles in nutrition and
TRP to lysine between 0.17 and 0.18 appeared to be physiology, particularly food intake, neurological function
sufficient to yield high feed intake and high growth rates in and immunity (1,101,102). Thus, there is growing interest
young pigs fed a diet containing adequate amounts of lysine in TRP requirements by mammalian, avian, and aquatic
and other amino acids (83,84). However, this ratio should species (103-107). Diets for animals and humans must
be increased to 0.195 to maximize growth performance in contain adequate TRP to maintain growth, nitrogen balance,
young pigs fed wheat- and barley-based diets deficient in and health, because this amino acid cannot be synthesized in
TRP (85,86). Dietary TRP requirements (total TRP in diets) the body (102). Optimal amounts of TRP in diets likely
for gestating and lactating pigs have been estimated to be depend on species, developmental stages, environmental
0.11% and 0.15-0.19% of diets, respectively, depending on factors, and health status. Tryptophan is usually the fourth
body weight change (82). The efficiency of crystalline TRP limiting amino acid in cereal-based diets for weanling and
for growth or protein deposition may be lower than that of growing pigs under practical conditions (after lysine,

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methionine, and threonine). Through reduction in syntheses 425-35 (1991)

of proteins and neurotransmitters, deficiency of TRP results
in retarded growth and neurological dysfunction. 6. Jon P. Ruddick, Andrew K. Evans, David J. Nutt, Stafford
Available evidence shows that dietary supplementation with L. Lightman, Graham A.W. Rook and Christopher
up to 1% TRP is safe for swine (an excellent animal model A. Lowry: Tryptophan metabolism in the central nervous
for studying human nutrition). Undoubtedly, research on system: medical implications. Expert Rev Mol Med 8(20),
TRP is exciting and fruitful. At present, little is known 1-27 (2006)
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are important events in the mammalian life (108-111); (b) 7. Trevor W. Stone and L. Gail Darlington: Endogenous
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(including epigenetics), a highly specific process in which a
gene can be switched on or off in response to regulatory 8. Hideki Miura, Norio Ozaki, Makoto Sawada , Kenichi
factors (120). With the recent developments of omics Isobe , Tatsuro Ohta and Toshiharu Nagatsu: A link
techniques (e.g., genomics, proteomics, and metabolomics) between stress and depression: Shifts in the balance
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powerful tools to study regulatory roles for TRP in gene and tryptophan metabolism and the etiology and
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Abbreviations: AMSR: 2-aminomuconate semialdehyde
Acids 37, 79-88 (2009)
reductase; ANH: anthranilate hydroxylase [also known as
Anthranilate 3-monooxygenase (deaminating)]; ASMT:
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Eosinophilia–myalgia syndrome; HDO:
177-186 (2009)
3-hydroxyanthranilate dioxygenase; HIMT:
5-hydroxyindole-O-methyltransferase; HKTA:
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Cynthia J. Meininger, Stephen B. Smith, Thomas E.
5-hydroxytryptamine; 5-HTP: 5-hydroxy-l-tryptophan; IDO:

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indoleamine 2, 3-dioxygenase; IFN: interferon; IL:

interleukin; KAD: α-ketoadipate dehydrogenase; KHL:
kynurenine hydroxylase; KNA: kynureninase; KTA:
kynurenine transaminase; KYN: kynurenine; MAO:
monoamine oxidase; NADS: NAD synthase; NF-kB:
NF-kappaB; NGH: NAD glycohydrolase; NMDA:
N-methyl-D-aspartic acid; OCR: oxalocrotonate reductase;
PCL, picolinate carboxylase; PLP: pyridoxal phosphate;
PRPP: 5-phosphoribosyl-1-pyrophosphate; QPRT:
quinolinate phosphoribosyl transferase; SNAT:
serotonin-N-acetyltransferase; SAM: S-adenosylmethionine;
SAHC, S-adenosylhomocyteine; SPR: spontaneous reaction;
SR: a series of reactions (glutaryl-CoA → glutaconyl-CoA
→ Crotonyl-CoA → Acetoacetyl-CoA → Acetyl-CoA);
TDO: tryptophan 2, 3-dioxygenase; THL: tryptophan
hydroxylase; TLR: toll-like receptors; TNF-α: tumor
necrosis factor-α; TRP: L-tryptophan

Key Words: Tryptophan, Metabolism, Feed Intake,

Immunity, Review

Send correspondence to: Yulong Yin, Hunan Engineering

and Research Center of Animal and Poultry Science and
Key Laboratory for Agro-ecological Processes in
Subtropical Region, Institute of Subtropical Agriculture,
Chinese Academy of Sciences, Hunan, China 410125, Tel:
979-845-1816, Fax: 979-845-6057,
E-mail:[email protected]

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