\documentclass[a4paper]{article}
\usepackage[a4paper,margin=2cm]{geometry}
\usepackage{multicol}
\usepackage{amsmath}
\usepackage{amssymb}
\usepackage{tcolorbox}
\usepackage{fancyhdr}
\usepackage{carbohydrates}
\usepackage{tabularx}
\usepackage{mhchem}

\pagestyle{fancy}
\fancyhead[LO,LE]{Food Chemistry}
\fancyhead[CO,CE]{Andrew Lorimer}

\setlength\parindent{0pt}

\begin{document}

  \title{Food chemistry}
  \author{Andrew Lorimer}
  \date{}
  \maketitle

  \section{Vitamins}

  \subsection*{Fat-soluble vitamins}

  \begin{itemize}
    \item Carbon and hydrogen
    \item Non-polar (few or no polar groups)
    \item Soluble in other non-polar solvents e.g. fats, oils
    \item Can be synthesised endogenously
  \end{itemize}

  \subsection*{Water-soluble vitamins}
  
  \begin{itemize}
    \item Absorbed directly into bloodstream
    \item Catalyse cellular reactions
    \item Excreted through kidneys in urine
    \item Must be obtained from food
  \end{itemize}

  \section{Proteins}

  \begin{itemize}
    \item All proteins contain C, H, O, N
    \item Plants make proteins from inorganic compounds, animals cannot
    \item Built from monomers called \textbf{amino acids}
  \end{itemize}

  \subsection*{Aminio acids}

  \begin{itemize}
    \item Contains amino (\ce{-NH2}) and carboxyl (\ce{-COOH})
    \item Most have four groups bonded to central atom
    \item May be polar or non-polar (amphoteric), acidic or basic
    \item \textbf{Essential amino acids} - cannot be synthesised, must be supplied in diet
    \item Amino acids (except glycine) are enantiomers due to chiral centres
    \item Must be correct chirality to act as a biological catalyst
  \end{itemize}

  % amino acid general structure (see Jacaranda p.328)

  \chemfig{{\color{red}N}(-[:135,,,,red]{\color{red}H})(-[:225,,,,red]{\color{red}H})-[:-45]C(-[:-90]\color{orange}\textit{R})(-H)-[:45]{\color{blue}C}(=[:90,,,,blue]{\color{blue}O})-[,,,,blue]{\color{blue}OH}}

  \subsection*{Zwitterions}

  \begin{itemize}
    \item Zwitterion = \textit{dipolar ion}
    \item Behaves as a base in acidic environments: \ce{-COOH- + H+ -> -COOH}
    \item Behaves as an acid in basic environments: ammonium group loses \ce{H+} \(\implies\) anionic form
  \end{itemize}

  % Zwitterion structural equation (Jacaranda p.330)

  \[ \ce{$\underset{\text{acid form}}{\ce{^+H3N-CH2-COOH}}$ <=>[+H+] $\underset{\text{zwitterion form}}{\ce{^+H3N-CH2-COO-}}$ <=>[-H+] $\underset{\text{basic form}}{\ce{H2N-CH2-COO-}}$} \]
  \[ \text{cationic} \hspace{12cm} \text{anionic} \]

  \subsection*{Formation of proteins}

  \[ \text{Amino acid} \rightarrow \text{peptide} \tag{polymerisation} \]

  Peptide group (amide): \ce{-C=ONH} (condensation reaction produces \ce{H2O})

  Amino acid \textit{residue} - product of peptide formation reaction

  Large polypeptides are called \textit{proteins}

  \subsection*{Protein structure}

  \begin{enumerate}
    \item \textbf{Primary structure} - order of amino acids in peptide chain
    \item \textbf{Secondary structure} - coils/pleats/folds in polymer
    \item \textbf{Tertiary structure} - three-dimensional structure, e.g. H-bonding, ionic bonding
    \item \textbf{Quaternary structure} - arrangement of multiple protein molecules
  \end{enumerate}

  % diagram of structural levels (Jacaranda p.332)

  \subsection*{Enzymes}

  \begin{itemize}
    \item Biological catalysts (lowers \(E_A\))
    \item Names usually end in \textit{-ase}
    \item Every enzyme has a unique 3D shape
    \item Rate of reaction \(\propto\) concentration up to \textit{saturation point}
    \item \textbf{Substrate} - reactant molecule
    \item \textbf{Active site} - destination of substrate
  \end{itemize}

  % enzyme catalyst diagram (Jacaranda p.334)

  \subsubsection*{Lock and key model}

  Reactants and enzymes must have complementary shapes

  \subsubsection*{Indicued fit model}

  Active site may change to fit subtrate

  \subsection*{Coenzymes}

  "Helper" molecules to enzymes. Non-protein molecules. Temporarily forms a loose bond with protein molecule to form active enzyme. Coenzymes are not specific to the substrate (different to enzymes).

  \section*{Digestion of protein}

  Proteins are hydrolysed by the \textit{pepsin} enzyme (\(\implies\) addition of \ce{H2O}).

  \begin{description}
    \item [Hydrolysis:] breaking of strong covalent (peptide) bonds
    \item [Denaturation:] breaking of weak bonds (dispersion, H-bonds)
  \end{description}

  \section{Carbohydrates}

  \subsubsection*{Monosaccharides}

  The smallest carbohydrates.

  \chemname{\glucose[model=haworth, ring]}{\(\alpha\) glucose \\ \ce{C6H12O6}}
  \chemname{\glucose[anomer=beta, model=haworth, ring]}{\(\beta\) glucose \\ \ce{C6H12O6}}
  \chemname{\galactose[model=haworth, ring]}{galactose \\ \ce{C6H12O6}}
  \chemname{\mannose[model=haworth, ring]}{mannose \\ \ce{C6H12O6}}
  \chemname{\xylose[model=haworth, ring]}{xylose\\ \ce{C5H10O5}}
  \setchemfig{cram width=2pt}
  \chemname{\chemfig{(-[:90]HO)(-[:270]HOCH2)-[:-45](-[:270, 0.5]HO)-(-[:90, 0.5]OH)-[:45]D-[:135]E}}{fructose \\ \ce{C6H12O6}}
  
\end{document}